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Information on EC 3.1.1.117 - (4-O-methyl)-D-glucuronate---lignin esterase
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EC Tree
3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esteraseIUBMB Comments
The enzyme occurs in microorganisms and catalyses the cleavage of the ester bonds between glucuronoyl or 4-O-methyl-glucuronoyl groups attached to xylan and aliphatic or aromatic alcohols in lignin polymers.
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Word Map
- 3.1.1.117
-
esterases
- biofuel production
-
lignin-carbohydrate
- biotechnology
-
4-o-methyl-d-glucuronic
- glucuronoxylans
- xylans
-
cellulolytic
-
phanerochaete
-
schizophyllum
-
lignocellulosic
-
uronic
- molecular biology
-
saccharification
-
d-glucuronic
- 4-nitrophenyl
-
chrysosporium
-
white-rot
-
wood-rotting
- cellulases
-
sporotrichum
-
halleri
-
hypocrea
- xylanases
-
hemicellulolytic
-
jecorina
-
hemicellulases
-
meglca
-
gemmifera
- synthesis
- degradation
- industry
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
a 4-O-methyl-D-glucopyranuronate ester
+
=
+
Synonyms
glucuronoyl esterase, page1, ttce15a, pcgce, ckxyn10c-ge15a, stge2, otce15a, stge1, fungal glucuronoyl esterase, ttge1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-O-methyl-glucuronoyl methylesterase
4-O-methyl-glucuronoyl methylesterase 1
4-O-methyl-glucuronoyl methylesterase 2
AfGE
Afu6g14390
carbohydrate esterase family 15 domain protein
carbohydrate esterase family 15 protein
CE15 enzyme
Cip2
Cip2_GE
DsGE1
DsGE2
FGE
fungal CE15 enzyme
fungal GE
fungal glucuronoyl esterase
GCE
GCE1
GE Cip2
GE1
Ge2
glucuronoyl esterase
glucuronoyl esterase 1
glucuronoyl esterase 2
glucuronoyl esterase CE15
glucuronoyl methylesterase 1
glucuronoyl methylesterase 2
glucuronoyl-lignin ester hydrolase
-
-
-
-
HsGE1
NcGE
PaGE1
PaGE3
PcGCE
PcGE1
PHACADRAFT_157044
PHACADRAFT_247750
PiGE1
PrGE1
ScGE
ScGE1
ScGE2
StGE1
StGE2
SuCE15A
SuCE15B
SuCE15C
TERTU_0517
THITE_2055580
THITE_2117593
TrCip2
TRIREDRAFT_123940
TtCE15A
TtGE1
TtGE2
WcGE1
additional information
4-O-methyl-glucuronoyl methylesterase
-
-
-
-
4-O-methyl-glucuronoyl methylesterase 1
UniProt
carbohydrate esterase family 15 protein
UniProt
-
carbohydrate esterase family 15 protein
UniProt
-
glucuronoyl esterase
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
-
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
-
-
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
-
-
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SYSTEMATIC NAME
IUBMB Comments
(4-O-methyl)-D-glucuronate---lignin ester hydrolase
The enzyme occurs in microorganisms and catalyses the cleavage of the ester bonds between glucuronoyl or 4-O-methyl-glucuronoyl groups attached to xylan and aliphatic or aromatic alcohols in lignin polymers.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylitol + H2O
?
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranuronate
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
3-(4-methoxyphenyl)propan-1-ol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl) propyl 4-O-methyl-alpha-D-glucopyranosiduronate
the substrate mimics the ester linkage between lignin and hemicellulose
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl)propyl 4-O-methyl-alpha-D-glucopyranosiduronate
3-(4-methoxyphenyl)propyl-methyl-4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 3-(4-methoxyphenyl)propyl-4-O-methyl-alpha-D-glucopyranuronate
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
benzyl methyl alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl alpha-D-glucopyranosiduronic acid
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-1,4-beta-D-xylopyranoside + H2O
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
methyl beta-D-xylopyranosyl-1,4-[2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)]-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl-4-O-methyl-D-glucopyranosyluronate + H2O
methanol + 4-O-methyl-D-glucopyranosyluronic acid
-
-
-
-
?
methylx02betaD-xylopyranosyl-1,4-(3-O-beta-D-xylopyranosyl)-beta-D-xylopyranosyl-1,4-[2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)]-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
O-methyl-alpha-D-glucopyranuronate + H2O
methanol + alpha-D-glucuronic acid
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
Thermothelomyces thermophilus DSM 1799
-
-
-
?
2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylitol + H2O
?
-
-
-
-
?
2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylitol + H2O
?
-
-
-
-
?
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
3-(4-methoxyphenyl)propan-1-ol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
3-(4-methoxyphenyl)propan-1-ol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl)propyl D-glucopyranosyluronate + H2O
?
-
-
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
?
-
-
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
?
-
-
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl)propyl 4-O-methyl-alpha-D-glucopyranosiduronate
a chromogenic substrate
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl)propyl 4-O-methyl-alpha-D-glucopyranosiduronate
a chromogenic substrate
-
-
?
3-(4-methoxyphenyl)propyl-methyl-4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 3-(4-methoxyphenyl)propyl-4-O-methyl-alpha-D-glucopyranuronate
substrate mimicking the ligninhemicellulose linkage
-
-
?
3-(4-methoxyphenyl)propyl-methyl-4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 3-(4-methoxyphenyl)propyl-4-O-methyl-alpha-D-glucopyranuronate
substrate mimicking the ligninhemicellulose linkage
-
-
?
3-phenyl-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
Thermothelomyces thermophilus ATCC 34628
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
a chromogenic substrate
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
a chromogenic substrate
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
Phanerodontia chrysosporium ATCC MYA-4764
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
Phanerodontia chrysosporium FGSC 9002
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
-
low activity
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
-
low activity
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
acetylxylan esterase activity
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
-
very low activity
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerodontia chrysosporium ATCC MYA-4764
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerodontia chrysosporium FGSC 9002
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer + H2O
?
-
-
-
?
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer + H2O
?
-
-
-
?
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer + H2O
?
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
Phanerodontia chrysosporium ATCC MYA-4764
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
Phanerodontia chrysosporium FGSC 9002
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 20% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 80% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 80% compared to the activity with benzyl glucuronic acid
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
moderate activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
Phanerodontia chrysosporium ATCC MYA-4764
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
Phanerodontia chrysosporium FGSC 9002
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
moderate activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
moderate activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
activity is 20% compared to activity with benzyl D-glucuronate
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
high activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
high activity
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronic acid ester + H2O
?
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
?
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
?
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus BCRC 31852
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus DSM 1799
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
Phanerodontia chrysosporium ATCC MYA-4764
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
Phanerodontia chrysosporium FGSC 9002
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
isozymes SuCE15A or SuCE15C show high activity on BnzGlcA at pH 5.5
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
isozymes SuCE15A or SuCE15C show high activity on BnzGlcA at pH 5.5
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
isozyme SlCE15A shows high activity on BnzGlcA at pH 5.5
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus DSM 1799
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
lignin-rich pellet + H2O
aldotetrauronic acids
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-1,4-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-1,4-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methylglucuronic acid
-
-
-
?
methyl 4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methylglucuronic acid
-
-
-
?
methyl 4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methylglucuronic acid
-
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
Phanerodontia chrysosporium ATCC MYA-4764
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
Phanerodontia chrysosporium FGSC 9002
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity isabout 5% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 15% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 15% compared to the activity with benzyl glucuronic acid
-
-
?
methyl-4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl-4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
Phanerodontia chrysosporium ATCC MYA-4764
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
Phanerodontia chrysosporium FGSC 9002
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
-
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
-
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
poor activity with isozyme OtCE15D
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
low activity
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
very low activity
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
very low activity
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
-
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
low activity
-
-
?
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate + H2O
?
-
-
-
?
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate + H2O
?
-
-
-
?
additional information
?
-
the enzyme is active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA)
-
-
-
additional information
?
-
Lys209 plays an important role in the preference for the substrates containing 4-O-methyl group in the glucopyranose ring. The purified recombinant enzyme displays the ability to degrade the synthetic substrates mimicking the ester linkage between hemicellulose and lignin. Self-degradation of the substrates under high alkaline condition
-
-
-
additional information
?
-
-
Lys209 plays an important role in the preference for the substrates containing 4-O-methyl group in the glucopyranose ring. The purified recombinant enzyme displays the ability to degrade the synthetic substrates mimicking the ester linkage between hemicellulose and lignin. Self-degradation of the substrates under high alkaline condition
-
-
-
additional information
?
-
Lys209 plays an important role in the preference for the substrates containing 4-O-methyl group in the glucopyranose ring. The purified recombinant enzyme displays the ability to degrade the synthetic substrates mimicking the ester linkage between hemicellulose and lignin. Self-degradation of the substrates under high alkaline condition
-
-
-
additional information
?
-
-
no activity is detected with methyl-D-galacturonate, indicating that CkGE15A has a strict preference for GlcA-derived esters
-
-
-
additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity. To investigate putative lignin- and xylan-binding sites in the solved structures, docking simulations of SuCE15C with a benzyl ester of 4-O-methyl-glucuronoxylotriose (glucuronoate alpha-1,2 linked to the middle xylose residue) are performed
-
-
-
additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity. To investigate putative lignin- and xylan-binding sites in the solved structures, docking simulations of SuCE15C with a benzyl ester of 4-O-methyl-glucuronoxylotriose (glucuronoate alpha-1,2 linked to the middle xylose residue) are performed
-
-
-
additional information
?
-
the enzyme catalyze removal of all glucuronoxylan associated with lignin. This is a direct result of enzymatic cleavage of the ester bonds connecting glucuronoxylan to lignin via 4-O-methyl glucuronoyl-ester linkages
-
-
?
additional information
?
-
a lignin-enriched substrate is prepared from raw birchwood by thermal ethanol extraction, the generated lignin-rich precipitate (LRP) serves as substrate for CuGE. The chemical composition of LRP and raw birchwood is determined by acid hydrolysis and confirmes an enrichment of glucuronoyl substituted xylan and lignin with practically no structural glucan in comparison to the raw birchwood substrate. CuGE catalyzes the release of a mixture of acetylated aldouronic acids upon reaction on LRP. The enzyme shows no endoxylanase or acetyl xylan esterase activity. Glucuronoyl esterases are capable of hydrolyzing ester-linked LCCs of glucuronoxylan and lignin. LC-MS analysis shows that the product profiles contain a mixture of acetylated aldouronic acids containing 4-O-methyl-glucuronosyl (MeGlcA) ranging from DP 3 to DP 5. Substrate specificity, detailed overview
-
-
-
additional information
?
-
analysis of the interactions between CuGE and the alpha-1,2-linked 4-O-methyl-D-glucuronoyl moieties on xylo-oligomers, the binding of the 4-O-methyl-alpha-D-glucuronoyl moiety is not influenced by the nature of the attached xylo-oligosaccharide. Enzyme-substrate binding analysis, overview
-
-
-
additional information
?
-
-
analysis of the interactions between CuGE and the alpha-1,2-linked 4-O-methyl-D-glucuronoyl moieties on xylo-oligomers, the binding of the 4-O-methyl-alpha-D-glucuronoyl moiety is not influenced by the nature of the attached xylo-oligosaccharide. Enzyme-substrate binding analysis, overview
-
-
-
additional information
?
-
the enzyme is active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA)
-
-
-
additional information
?
-
UDH-coupled spectrophotometric assaying of GE enzymatic reaction, hydrolysis of BnGlcA catalyzed by GE and spectrophotometric assaying by NAD+-dependent oxidation of GlcA using uronate dehydrogenase (UDH), overview
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity. Isozyme OtCE15B shows lower activity compared to the other isozymes. To investigate putative lignin- and xylan-binding sites in the solved structures, docking simulations of OtCE15A with a benzyl ester of 4-O-methyl-glucuronoxylotriose (glucuronoate alpha-1,2 linked to the middle xylose residue) are performed
-
-
-
additional information
?
-
-
the enzyme is active with the glucuronoxylan oligosaccharide (XUX). The oligosaccharide is produced from beech xylan and contains the 4-O-methyl-alpha-D-glucuronate moiety. Docking study, structure analysis of enzyme OtCE15A in complex with glucuronoxylooligosaccharide 23-(4-O-methyl-alpha-D-glucuronyl)-xylotriose (commonly referred to as XUX). The structure of the enzyme with the disaccharide xylobiose reveals a surface binding site that possibly indicates a recognition mechanism for long glucuronoxylan chains
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcoholesters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcoholesters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
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-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
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-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
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-
-
additional information
?
-
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
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-
-
additional information
?
-
Phanerodontia chrysosporium ATCC MYA-4764
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerodontia chrysosporium ATCC MYA-4764
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerodontia chrysosporium ATCC MYA-4764
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerodontia chrysosporium ATCC MYA-4764
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
Phanerodontia chrysosporium ATCC MYA-4764
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
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-
-
additional information
?
-
Phanerodontia chrysosporium FGSC 9002
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerodontia chrysosporium FGSC 9002
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerodontia chrysosporium FGSC 9002
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerodontia chrysosporium FGSC 9002
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
Phanerodontia chrysosporium FGSC 9002
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
UDH-coupled spectrophotometric assaying of GE enzymatic reaction, hydrolysis of BnGlcA catalyzed by GE and spectrophotometric assaying by NAD+-dependent oxidation of GlcA using uronate dehydrogenase (UDH), overview
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-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme is active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA)
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-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. The deesterification of 4-O-methyl-D-glucuronosyl residues in both substrates proceeds at a similar rate, pointing to the same or a very similar specific activity of the enzyme for high and low molecular mass substrates. 1H NMR spectra of glucuronoxylan methyl ester, overview
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-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
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-
-
additional information
?
-
-
enzyme substrate specificity, overview. The glucuronoyl esterase attacks exclusively the esters of MeGlcA. The methyl ester of free or glycosidically linked MeGlcA is not hydrolysed by other carbohydrate esterases
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additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. The glucuronoyl esterase attacks exclusively the esters of MeGlcA. The methyl ester of free or glycosidically linked MeGlcA is not hydrolysed by other carbohydrate esterases
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-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme hydrolyses glucuronic acid esters present in LCC fractions from spruce and birch
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-
?
additional information
?
-
-
the enzyme hydrolyses glucuronic acid esters present in LCC fractions from spruce and birch
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-
?
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
lignin-carbohydrate complexes (LCCs) fractions from spruce and birch are treated with a recombinantly produced glucuronoyl esterase (GE) originating from Acremonium alcalophilum (AaGE1). A combination of size exclusion chromatography and 31P NMR analyses of phosphitylated LCC samples, before and after AaGE1 treatment, provide evidence for cleavage of the lignin-carbohydrate (LC) ester linkages existing in wood by the enzyme. Structures of gamma and alpha ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid residues of glucuronoxylans are the proposed target bonds of enzyme AaGE1. Estimation of hydroxyl groups in LCCs before and after GE treatment. 31Phosphorous NMR and 2D HSQC NMR analysis confirming the GE activity on LC ester bonds and AaGE1 specificity, respectively
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-
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additional information
?
-
-
lignin-carbohydrate complexes (LCCs) fractions from spruce and birch are treated with a recombinantly produced glucuronoyl esterase (GE) originating from Acremonium alcalophilum (AaGE1). A combination of size exclusion chromatography and 31P NMR analyses of phosphitylated LCC samples, before and after AaGE1 treatment, provide evidence for cleavage of the lignin-carbohydrate (LC) ester linkages existing in wood by the enzyme. Structures of gamma and alpha ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid residues of glucuronoxylans are the proposed target bonds of enzyme AaGE1. Estimation of hydroxyl groups in LCCs before and after GE treatment. 31Phosphorous NMR and 2D HSQC NMR analysis confirming the GE activity on LC ester bonds and AaGE1 specificity, respectively
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-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides. The recombinant GE from Acremonium alcalophilum reduces the molecular mass of isolated lignin-carbohydrate complexes from spruce and birch
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-
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additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity
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-
-
additional information
?
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
-
-
-
additional information
?
-
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
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-
-
additional information
?
-
enzyme is active on substrates containing glucuronic acid methyl ester
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-
?
additional information
?
-
-
enzyme is active on substrates containing glucuronic acid methyl ester
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-
?
additional information
?
-
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
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-
?
additional information
?
-
-
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
-
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
-
the enzyme is active on substrates containing glucuronic acid methyl ester
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-
-
additional information
?
-
Thermothelomyces thermophilus ATCC 34628
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
enzyme is active on substrates containing glucuronic acid methyl ester
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-
?
additional information
?
-
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
enzyme is active on substrates containing glucuronic acid methyl ester
-
-
?
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
enzyme is active on substrates containing glucuronic acid methyl ester
-
-
?
additional information
?
-
Thermothelomyces thermophilus DSM 1799
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
Thermothelomyces thermophilus DSM 1799
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme is slightly active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA). TtGE shows low overall activity
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
two substrates of glucuronoyl esterase are utilized, substrate I: methyl ester of 4-O-methyl-D-glucuronic acid; substrate II: methyl ester of 4-O-methyl-D-glucuronic acid linked alpha-1,2 to 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
additional information
?
-
-
two substrates of glucuronoyl esterase are utilized, substrate I: methyl ester of 4-O-methyl-D-glucuronic acid; substrate II: methyl ester of 4-O-methyl-D-glucuronic acid linked alpha-1,2 to 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
two substrates of glucuronoyl esterase are utilized, substrate I: methyl ester of 4-O-methyl-D-glucuronic acid; substrate II: methyl ester of 4-O-methyl-D-glucuronic acid linked alpha-1,2 to 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerodontia chrysosporium ATCC MYA-4764
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerodontia chrysosporium FGSC 9002
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerodontia chrysosporium ATCC MYA-4764
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerodontia chrysosporium FGSC 9002
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
Thermothelomyces thermophilus ATCC 34628
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
the enzyme is not affected by Zn2+ at 1 mM. AfGE activity is not affected by EDTA, indicating that this enzyme is not a metalloenzyme
additional information
-
the enzyme is not affected by Zn2+ at 1 mM. AfGE activity is not affected by EDTA, indicating that this enzyme is not a metalloenzyme
additional information
divalent metal ions, such as Mg2+ and Ca2+, are not necessary for the enzyme to exert its activity
additional information
poor effects on enzyme activity at 1 mM by Mn2+ and Fe2+, and by 5 mM EDTA, 10 mM acetic anhydride, 10 mM ascorbic acid, and 10 mM glycerol
additional information
-
poor effects on enzyme activity at 1 mM by Mn2+ and Fe2+, and by 5 mM EDTA, 10 mM acetic anhydride, 10 mM ascorbic acid, and 10 mM glycerol
additional information
divalent metal ions, such as Mg2+ and Ca2+, are not necessary for the enzyme to exert its activity
additional information
-
the enzyme does not loose activity on addition of 1 mM EDTA as an evidence that it is not a metal-dependent enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethyl sulfoxide
10 mM, 14% loss of activity; 16% inhibition at 10 mM
reduced 23-(4-O-methyl-D-glucuronyl)-alpha-D-xylotetraitol
XUXXR, inhibits the wild-type, mutant F174D, and mutant F174A, but not mutant W376A
-
2-mercaptoethanol
10 mM, 16% loss of activity; 16% inhibition at 10 mM
EDTA
10 mM, 30°C, 20 min, about 15% loss of activity; 15% inhibition at 10 mM
EDTA
10 mM, 30°C, 20 min, about 15% loss of activity; 15% inhibition at 10 mM
glycerol
46% inhibition at 5% glycerol; 5%, 30°C, 20 min, about 45% loss of activity
glycerol
46% inhibition at 5% glycerol; 5%, 30°C, 20 min, about 45% loss of activity
imidazole
5 mM, 30°C, 20 min, about 30% loss of activity
PMSF
1 mM, 10 min, 20% loss of activity. 5 mM, 10 mon, 80% loss of activity; 5-10 mM, over 80% inhibition
SDS
1%, 30°C, 20 min, complete loss of activity; almost complete inhibition at 1%
SDS
1%, 30°C, 20 min, about 95% loss of activity; almost complete inhibition at 1%
tris(2-carboxyethyl)phosphine
5 mM, 30°C, 20 min, about 35% loss of activity
tris(2-carboxyethyl)phosphine
5 mM, 30°C, 20 min, about 20% loss of activity
additional information
AfGE activity is not affected by EDTA, indicating that this enzyme is not a metalloenzyme. No significant effect by glycerol, acetic anhydride, ascorbic acid, dimethyl sulfoxide, SDS, and urea at 10 mM; the enzyme is not affected by EDTA, indicating that this enzyme is not a metalloenzyme
-
additional information
-
AfGE activity is not affected by EDTA, indicating that this enzyme is not a metalloenzyme. No significant effect by glycerol, acetic anhydride, ascorbic acid, dimethyl sulfoxide, SDS, and urea at 10 mM; the enzyme is not affected by EDTA, indicating that this enzyme is not a metalloenzyme
-
additional information
the enzyme is not affected by 5 mM EDTA, suggesting that it is not a metallo enzyme
-
additional information
-
the enzyme is not affected by 5 mM EDTA, suggesting that it is not a metallo enzyme
-
additional information
-
the glucuronoyl esterase is not inhibited by 1 mM PMSF or 1 mM EDTA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no significant effect by EDTA, glycerol, acetic anhydride, ascorbic acid, dimethyl sulfoxide, SDS, and urea at 10 mM
-
additional information
-
no significant effect by EDTA, glycerol, acetic anhydride, ascorbic acid, dimethyl sulfoxide, SDS, and urea at 10 mM
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Diabetes Mellitus
Improvement of quality of life through glycemic control by liraglutide, a GLP-1 analog, in insulin-naive patients with type 2 diabetes mellitus: the PAGE1 study.
Diabetes Mellitus, Type 2
Improvement of quality of life through glycemic control by liraglutide, a GLP-1 analog, in insulin-naive patients with type 2 diabetes mellitus: the PAGE1 study.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.9 - 12.1
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol
-
1.34
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
1.34
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
15.8
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
pH 5.0, 30°C
4.31
3-(4-methoxyphenyl)propyl D-glucopyranosyluronate
-
pH 6.0, 30°C
-
1.78
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
-
pH 6.0, 30°C
0.31
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
pH 6.0, 30°C
-
0.5 - 1.3
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
49
allyl-D-glucuronate
pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme
23.7
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
pH 5.0, 30°C
8.9
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol
pH 6.0, 45°C
-
12.1
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol
pH 6.0, 35°C
-
0.94
3-phenyl-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
7.24
3-phenyl-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
7.24
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
0.5
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
pH 5.5, 30°C
1.3
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
pH 6.0, 50°C
1.4
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer
pH 6.0, 30°C
-
3.4
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer
pH 6.0, 30°C
-
0.184
benzyl-D-glucuronate
-
mutant H408A, pH and temperature not specified in the publication
0.502
benzyl-D-glucuronate
-
mutant E290A/D356A, pH and temperature not specified in the publication
1.86
benzyl-D-glucuronate
-
mutant D356A, pH and temperature not specified in the publication
2.03
benzyl-D-glucuronate
-
mutant E290A, pH and temperature not specified in the publication
2.83
benzyl-D-glucuronate
-
mutant S267A, pH and temperature not specified in the publication
3.47
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme
3.57
benzyl-D-glucuronate
-
wild-type enzyme, pH and temperature not specified in the publication
4
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S281A
12.7
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S304E/E374A
15.4
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant W376D
21.8
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant E374A
22.7
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant W376A
25.8
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant F174A
29.4
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S304E
53.1
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant F174D
3.63
cinnamyl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
0.0939
lignin-rich pellet
recombinant enzyme, pH 6.0, 50°C
-
0.155
lignin-rich pellet
recombinant enzyme, pH 6.0, 50°C
-
5.31
methyl-D-galacturonate
-
wild-type enzyme, pH and temperature not specified in the publication
-
11.9
methyl-D-galacturonate
-
mutant L269Y, pH and temperature not specified in the publication
-
1.69
methyl-D-glucuronate
-
mutant L269Y, pH and temperature not specified in the publication
-
2.77
methyl-D-glucuronate
-
wild-type enzyme, pH and temperature not specified in the publication
-
2.66
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
3.63
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
StGE2 hydrolysis results towards ester VI, a substrate analogue with a hydroxyl substituent on benzene ring, are unable to fit in Michaelis-Menten function, as plateau is not achieved up to substrate concentrations of 8.0 mM, the Km value is estimated erroneously high, indicating low specificity of StGE2 for substrate VI
-
additional information
additional information
-
StGE2 hydrolysis results towards ester VI, a substrate analogue with a hydroxyl substituent on benzene ring, are unable to fit in Michaelis-Menten function, as plateau is not achieved up to substrate concentrations of 8.0 mM, the Km value is estimated erroneously high, indicating low specificity of StGE2 for substrate VI
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5 - 7.8
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol
-
0.19
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
0.19
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
67.1
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
pH 5.0, 30°C
7.8
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
-
pH 6.0, 30°C
3.2
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
pH 6.0, 30°C
-
0.808 - 4.5
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
200
allyl-D-glucuronate
pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme
66.4
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
pH 5.0, 30°C
3.5
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol
pH 6.0, 45°C
-
7.8
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol
pH 6.0, 35°C
-
0.78
3-phenyl-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
2.77
3-phenyl-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
2.77
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
0.808
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
pH 6.0, 50°C
4.5
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
pH 5.5, 30°C
125
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer
pH 6.0, 30°C
-
285
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer
pH 6.0, 30°C
-
0.000983
benzyl-D-glucuronate
-
mutant S267A, pH and temperature not specified in the publication
0.00999
benzyl-D-glucuronate
-
mutant H408A, pH and temperature not specified in the publication
0.196
benzyl-D-glucuronate
-
mutant E290A/D356A, pH and temperature not specified in the publication
0.36
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S281A
0.37
benzyl-D-glucuronate
pH 6.0, 35°C, recombinant enzyme
0.79
benzyl-D-glucuronate
pH 6.0, 35°C, recombinant enzyme
1.92
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S304E
2.83
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S304E/E374A
4.12
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant E374A
5.21
benzyl-D-glucuronate
-
mutant D356A, pH and temperature not specified in the publication
10.3
benzyl-D-glucuronate
-
mutant E290A, pH and temperature not specified in the publication
12.8
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant W376D
16.6
benzyl-D-glucuronate
-
wild-type enzyme, pH and temperature not specified in the publication
18.3
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant W376A
43.1
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant F174D
132
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme
136
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant F174A
1.93
cinnamyl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
0.0886
lignin-rich pellet
recombinant enzyme, pH 6.0, 50°C
-
2.87
lignin-rich pellet
recombinant enzyme, pH 6.0, 50°C
-
0.012
methyl-D-galacturonate
pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme
-
2.7
methyl-D-galacturonate
-
mutant L269Y, pH and temperature not specified in the publication
-
28.8
methyl-D-galacturonate
-
wild-type enzyme, pH and temperature not specified in the publication
-
16.1
methyl-D-glucuronate
-
mutant L269Y, pH and temperature not specified in the publication
-
19
methyl-D-glucuronate
-
wild-type enzyme, pH and temperature not specified in the publication
-
1.93
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
5.26
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
0.14
3-(4-hydroxyphenyl)prop-1-yl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
4.24
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
pH 5.0, 30°C
0.046
3-(4-methoxyphenyl)propyl D-glucopyranosyluronate
-
pH 6.0, 30°C
-
4.38
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
-
pH 6.0, 30°C
10.32
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
pH 6.0, 30°C
-
0.622 - 9.7
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
2.8
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate
pH 5.0, 30°C
0.38
3-phenyl-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
0.82
3-phenyl-1-propyl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
0.38
3-phenylprop-1-yl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
0.622
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
pH 6.0, 50°C
9
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
pH 5.5, 30°C
9.7
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
pH 5.5, 30°C
2.56
4-nitrophenylacetate
-
isozyme OtCE15B, pH and temperature not specified in the publication
5.09
4-nitrophenylacetate
-
isozyme SuCE15A, pH and temperature not specified in the publication
9.51
4-nitrophenylacetate
-
isozyme OtCE15D, pH and temperature not specified in the publication
10.9
4-nitrophenylacetate
-
isozyme SuCE15C, pH and temperature not specified in the publication
18.2
4-nitrophenylacetate
-
isozyme SuCE15B, pH and temperature not specified in the publication
30.9
4-nitrophenylacetate
-
isozyme SlCE15A, pH and temperature not specified in the publication
32.3
4-nitrophenylacetate
-
isozyme OtCE15A, pH and temperature not specified in the publication
39.7
4-nitrophenylacetate
-
isozyme OtCE15C, pH and temperature not specified in the publication
83
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer
pH 6.0, 30°C
-
89
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer
pH 6.0, 30°C
-
2.82
allyl-D-glucuronate
-
isozyme OtCE15B, pH and temperature not specified in the publication
4.08
allyl-D-glucuronate
pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme
111
allyl-D-glucuronate
-
isozyme SlCE15C, pH and temperature not specified in the publication
365
allyl-D-glucuronate
-
isozyme SuCE15B, pH and temperature not specified in the publication
908
allyl-D-glucuronate
-
isozyme SlCE15B, pH and temperature not specified in the publication
1000
allyl-D-glucuronate
-
isozyme SlCE15A, pH and temperature not specified in the publication
2490
allyl-D-glucuronate
-
isozyme OtCE15C, pH and temperature not specified in the publication
3450
allyl-D-glucuronate
-
isozyme OtCE15D, pH and temperature not specified in the publication
5470
allyl-D-glucuronate
-
isozyme SuCE15A, pH and temperature not specified in the publication
8800
allyl-D-glucuronate
-
isozyme OtCE15A, pH and temperature not specified in the publication
15700
allyl-D-glucuronate
-
isozyme SuCE15C, pH and temperature not specified in the publication
0.00035
benzyl-D-glucuronate
-
mutant S267A, pH and temperature not specified in the publication
0.054
benzyl-D-glucuronate
-
mutant H408A, pH and temperature not specified in the publication
0.065
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S304E
0.09
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S281A
0.128
benzyl-D-glucuronate
pH 6.0, 35°C, recombinant enzyme
0.189
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant E374A
0.223
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant S304E/E374A
0.39
benzyl-D-glucuronate
-
mutant E290A/D356A, pH and temperature not specified in the publication
0.465
benzyl-D-glucuronate
pH 6.0, 35°C, recombinant enzyme
0.806
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant W376A
0.811
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant F174D
0.831
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant W376D
2.8
benzyl-D-glucuronate
-
mutant D356A, pH and temperature not specified in the publication
4.65
benzyl-D-glucuronate
-
wild-type enzyme, pH and temperature not specified in the publication
5.07
benzyl-D-glucuronate
-
mutant E290A, pH and temperature not specified in the publication
5.27
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, mutant F174A
18.6
benzyl-D-glucuronate
-
isozyme OtCE15B, pH and temperature not specified in the publication
38
benzyl-D-glucuronate
pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme
96.9
benzyl-D-glucuronate
-
isozyme SlCE15C, pH and temperature not specified in the publication
1490
benzyl-D-glucuronate
-
isozyme SuCE15B, pH and temperature not specified in the publication
1880
benzyl-D-glucuronate
-
isozyme SlCE15A, pH and temperature not specified in the publication
2600
benzyl-D-glucuronate
-
isozyme SlCE15B, pH and temperature not specified in the publication
4640
benzyl-D-glucuronate
-
isozyme OtCE15A, pH and temperature not specified in the publication
11100
benzyl-D-glucuronate
-
isozyme OtCE15D, pH and temperature not specified in the publication
11600
benzyl-D-glucuronate
-
isozyme OtCE15C, pH and temperature not specified in the publication
22000
benzyl-D-glucuronate
-
isozyme SuCE15A, pH and temperature not specified in the publication
22700
benzyl-D-glucuronate
-
isozyme SuCE15C, pH and temperature not specified in the publication
0.53
cinnamyl 4-O-methyl-D-glucopyranuronate
pH 6.0, 50°C
0.916
lignin-rich pellet
recombinant enzyme, pH 6.0, 50°C
-
18.49
lignin-rich pellet
recombinant enzyme, pH 6.0, 50°C
-
0.000000366
methyl-D-galacturonate
-
isozyme SlCE15B, pH and temperature not specified in the publication
-
0.00000195
methyl-D-galacturonate
-
isozyme OtCE15D, pH and temperature not specified in the publication
-
0.00000373
methyl-D-galacturonate
-
isozyme SlCE15C, pH and temperature not specified in the publication
-
0.009
methyl-D-galacturonate
-
isozyme SuCE15B, pH and temperature not specified in the publication
-
0.23
methyl-D-galacturonate
-
mutant L269Y, pH and temperature not specified in the publication
-
5.42
methyl-D-galacturonate
-
wild-type enzyme, pH and temperature not specified in the publication
-
8.68
methyl-D-galacturonate
-
isozyme OtCE15B, pH and temperature not specified in the publication
-
38.2
methyl-D-galacturonate
-
isozyme SlCE15A, pH and temperature not specified in the publication
-
1190
methyl-D-galacturonate
-
isozyme OtCE15C, pH and temperature not specified in the publication
-
1590
methyl-D-galacturonate
-
isozyme SuCE15C, pH and temperature not specified in the publication
-
1620
methyl-D-galacturonate
-
isozyme SuCE15A, pH and temperature not specified in the publication
-
4850
methyl-D-galacturonate
-
isozyme OtCE15A, pH and temperature not specified in the publication
-
0.06
methyl-D-glucuronate
-
isozyme SuCE15B, pH and temperature not specified in the publication
-
1.14
methyl-D-glucuronate
-
isozyme OtCE15B, pH and temperature not specified in the publication
-
6.86
methyl-D-glucuronate
-
wild-type enzyme, pH and temperature not specified in the publication
-
9.53
methyl-D-glucuronate
-
mutant L269Y, pH and temperature not specified in the publication
-
103
methyl-D-glucuronate
-
isozyme SlCE15C, pH and temperature not specified in the publication
-
457
methyl-D-glucuronate
-
isozyme SlCE15B, pH and temperature not specified in the publication
-
519
methyl-D-glucuronate
-
isozyme OtCE15D, pH and temperature not specified in the publication
-
898
methyl-D-glucuronate
-
isozyme OtCE15C, pH and temperature not specified in the publication
-
1550
methyl-D-glucuronate
-
isozyme SlCE15A, pH and temperature not specified in the publication
-
2320
methyl-D-glucuronate
-
isozyme SuCE15A, pH and temperature not specified in the publication
-
6850
methyl-D-glucuronate
-
isozyme OtCE15A, pH and temperature not specified in the publication
-
16600
methyl-D-glucuronate
-
isozyme SuCE15C, pH and temperature not specified in the publication
-
0.53
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
1.98
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate
pH 7.0, 50°C, recombinant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.51
reduced 23-(4-O-methyl-D-glucuronyl)-alpha-D-xylotetraitol
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
-
0.83
4-coumaric acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
4.84
4-coumaric acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant mutant F174A
26
4-coumaric acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant mutant F174D
0.084
ferulic acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant mutant F174A
0.4
ferulic acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant mutant F174D
0.55
ferulic acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
0.19
Sinapic acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant mutant F174A
0.56
Sinapic acid
Teredinibacter turnerae
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12.47
purified recombinant isozyme TtGE2, pH 5.5, 55°C, substrate methyl (4-nitrophenyl beta-D-glucopyranoside)uronate
19.98
35.1
-
substrate methyl-4-O-methyl-D-glucopyranosyluronate, pH 6.0, 30°C
37.6
-
substrate methylx02betaD-xylopyranosyl-1,4-(3-O-beta-D-xylopyranosyl)-beta-D-xylopyranosyl-1,4-[2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)]-beta-D-xylopyranoside, pH 6.0, 30°C
4.6
40.9
-
substrate methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside, pH 6.0, 30°C
41.6
-
substrate methyl beta-D-xylopyranosyl-1,4-[2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)]-beta-D-xylopyranoside, pH 6.0, 30°C
43.95
purified recombinant isozyme TtGE1, pH 5.5, 55°C, substrate methyl (4-nitrophenyl beta-D-glucopyranoside)uronate
47.1
-
substrate methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-1,4-beta-D-xylopyranoside, pH 6.0, 30°C
additional information
additional information
recombinant enzyme expressed in Aspergillus vadensis strain NW282 shows 0.036 U/ml activity, the enzyme expressed from Pycnoporus cinnabarinus strain BMR44 shows 0.417 U/ml, and the enzyme from Schizophyllum commune strain 4.8B 0.453 U/ml, at pH 6.0, 30°C
additional information
recombinant enzyme expressed in Aspergillus vadensis strain NW282 shows 0.036 U/ml activity, the enzyme expressed from Pycnoporus cinnabarinus strain BMR44 shows 0.417 U/ml, and the enzyme from Schizophyllum commune strain 4.8B 0.453 U/ml, at pH 6.0, 30°C
additional information
-
recombinant enzyme expressed in Aspergillus vadensis strain NW282 shows 0.036 U/ml activity, the enzyme expressed from Pycnoporus cinnabarinus strain BMR44 shows 0.417 U/ml, and the enzyme from Schizophyllum commune strain 4.8B 0.453 U/ml, at pH 6.0, 30°C
additional information
recombinant enzyme expressed in Schizophyllum commune strain 4.8B shows 0.530 U/ml activity, at pH 6.0, 30°C
additional information
recombinant enzyme expressed in Schizophyllum commune strain 4.8B shows 0.530 U/ml activity, at pH 6.0, 30°C
additional information
-
recombinant enzyme expressed in Schizophyllum commune strain 4.8B shows 0.530 U/ml activity, at pH 6.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.2
7 - 8.5
5.5
substrate 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
7
-
with substrate 4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7
over 50% of maximal activity within the range of pH 4.5-6.7, profile overview
4 - 8
over 60% of maximal activity within this range, profile overview
4.5 - 6.5
over 50% of maximal activity within this range, profile overview
5 - 8
5 - 8
over 70% of maximal activity within this range, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
40
40 - 50
45
50
55
50
-
with substrate 4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 40
-
assay at, the activity at 40°C is about 6fold higher compared to 22°C
30 - 60
over 50% of maximal activity within this range, profile overview
30 - 65
over 50% of maximal activity within this range, profile overview
30 - 70
42 - 60
over 50% of maximal activity within this range, profile overview
30 - 70
30°C: about 80% of maximal activity, 70°C: about 60% of maximal activity
30 - 70
over 60% of maximal activity within this range, profile overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.48
4.6
5.6
6.1
6.7
7.3
8.2
8.5
8.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Phanerodontia chrysosporium ATCC MYA-4764
Phanerodontia chrysosporium FGSC 9002
-
SwissProt
brenda
Thermothelomyces thermophilus DSM 1799
a multidomain esterase composed of acetylxylan esterase, EC 3.1.1.72, and 4-O-methyl-glucuronoyl methylesterase
SwissProt
brenda
Teredinibacter turnerae encodes three CE15 enzymes: TtCE15A, -B, and -C, locus tags are TERTU_0517, TERTU_3447, and TERTU_3514, respectively
UniProt
brenda
Teredinibacter turnerae encodes three CE15 enzymes: TtCE15A, -B, and -C, locus tags are TERTU_0517, TERTU_3447, and TERTU_3514, respectively
UniProt
brenda
Teredinibacter turnerae encodes three CE15 enzymes: TtCE15A, -B, and -C, locus tags are TERTU_0517, TERTU_3447, and TERTU_3514, respectively
UniProt
brenda
member of Carbohydrate Esterase Family 15
UniProt
brenda
Sporotrichum thermophile
UniProt
brenda
Sporotrichum thermophile
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
grown on glucose, xylose, corn cob xylan, and milled corn cob biomass. Gene slce15b is constitutively expressed in all growth conditions, expression of slce15a is similar for glucose, xylose, and xylan, but increases twofold on milled corn cob, and slce15c shows a three to fourfold increase in response to any xylose-containing carbon source compared to glucose
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is anchored to the cell wall by its C-terminal surface layer homology (SLH)-domains, overview
brenda
the enzyme contains an N-terminal signal peptide sequence
-
brenda
-
the enzyme contains an N-terminal signal peptide sequence
-
-
brenda
-
the enzyme contains an N-terminal signal peptide sequence
-
-
brenda
-
the enzyme contains an N-terminal signal peptide sequence
-
-
brenda
-
the enzyme contains an N-terminal signal peptide sequence
-
-
brenda
-
the enzyme contains an N-terminal signal peptide sequence
-
-
brenda
additional information
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 17 and 18 for LfGE1, and between amino acids 16 and 17 for LfGE2 and LfGE3
-
brenda
additional information
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
brenda
additional information
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
brenda
additional information
Phanerodontia chrysosporium ATCC MYA-4764
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
-
brenda
additional information
Phanerodontia chrysosporium FGSC 9002
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
-
brenda
additional information
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
-
brenda
additional information
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 18 and 19
-
brenda
additional information
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 18 and 19
-
-
brenda
additional information
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
brenda
additional information
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
brenda
additional information
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
brenda
additional information
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
brenda
additional information
-
the enzyme contains a signal peptide sequence, the cleavage site is between amino acids 19 and 20
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
evolution
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
evolution
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
evolution
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
evolution
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
evolution
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
evolution
building of a phylogenetic tree from almost 400 putative FGEs obtained on BLAST analysis and definition of six main clades. In the phylogenetic tree, all the putative FGEs of ascomycetes cluster in clades I to IV, and most of the putative FGEs of basidiomycetes (B-FGEs) cluster in clades V to VI, several B-FGEs are found to cluster in clade II. Most FGEs of clade II have higher theoretical isoelectric points than those in the other five clades. The enzyme from Ceriporiopsis subvermispora belongs to clade V
evolution
building of a phylogenetic tree from almost 400 putative FGEs obtained on BLAST analysis and definition of six main clades. In the phylogenetic tree, all the putative FGEs of ascomycetes cluster in clades I to IV, and most of the putative FGEs of basidiomycetes (B-FGEs) cluster in clades V to VI, several B-FGEs are found to cluster in clade II. Most FGEs of clade II have higher theoretical isoelectric points than those in the other five clades. The enzyme from Pleurotus eryngii belongs to clade II
evolution
CuGE is an alpha/beta-hydrolase belonging to carbohydrate esterase family 15 (CE15), part of the alpha/beta-hydrolase superfamily. CuGE belongs to the group of fungal CE15-B enzymes with an open and flat substrate-binding site. Conservation of carbohydrate recognition among fungal CE15s. The fungal members of CE15-A display low overall sequence identity compared to the members of CE15-B, furthermore they differ in the configuration of the catalytic triad. The overall sequence identity within the fungal CE15-A group is 40-75%, whereas the sequence identity between the two groups is merely 25-36%. Residues involved in carbohydrate recognition are almost invariant among fungal CE15-B enzymes and most of these residues appear to be conserved in fungal CE15-A members
evolution
-
enzyme glucuronoyl esterase (GE) belongs to the carbohydrate esterase family 15 (CE15), CE15 phylogenetic analysis and tree, overview. Fungal and bacterial glucuronoyl esterases have been biochemically characterized using alkyl and alkyl aryl alcohol esters of 4-O-methyl glucuronic acid of varying complexity
evolution
-
enzyme glucuronoyl esterase (GE) belongs to the carbohydrate esterase family 15 (CE15), CE15 phylogenetic analysis and tree, overview. Fungal and bacterial glucuronoyl esterases have been biochemically characterized using alkyl and alkyl aryl alcohol esters of 4-O-methyl glucuronic acid of varying complexity
evolution
-
enzyme glucuronoyl esterase (GE) belongs to the carbohydrate esterase family 15 (CE15), CE15 phylogenetic analysis and tree, overview. Fungal and bacterial glucuronoyl esterases have been biochemically characterized using alkyl and alkyl aryl alcohol esters of 4-O-methyl glucuronic acid of varying complexity
evolution
-
enzyme StGE1 is a family 15 glucuronoyl esterase that shows the highest homology with the hypothetical glucuronoyl esterase CHGG_10774 (UniProt ID Q2GMN0) of Chaetomium globosum strain CBS 148.51
evolution
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
evolution
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
evolution
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
evolution
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
evolution
-
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
evolution
glucuronoyl esterases (GEs) belong to a family of carbohydrate esterases recently added to the CAZy database as family 15 (CE15)
evolution
glucuronoyl esterases (GEs) belong to a family of carbohydrate esterases recently added to the CAZy database as family 15 (CE15)
evolution
glucuronoyl esterases (GEs) belong to a family of carbohydrate esterases recently added to the CAZy database as family 15 (CE15)
evolution
glucuronoyl esterases (GEs) belong to a family of carbohydrate esterases recently added to the CAZy database as family 15 (CE15)
evolution
glucuronoyl esterases (GEs) belong to the family 15 of carbohydrate esterases (CE15)
evolution
glucuronoyl esterases (GEs) belong to the family 15 of carbohydrate esterases (CE15). Sequence comparison with enzyme Cip2 (UniProt ID G0RV93) from Hypocrea jecorina strain QM6a
evolution
-
glucuronoyl esterases have been assigned to CAZymes family 15 of carbohydrate esterases, phylogenetic analysis, detailed overview
evolution
glucuronoyl esterases have been assigned to CAZymes family 15 of carbohydrate esterases, phylogenetic analysis, detailed overview
evolution
glucuronoyl esterases have been assigned to CAZymes family 15 of carbohydrate esterases, phylogenetic analysis, detailed overview
evolution
-
sequence analysis of CE15 has revealed that several members, such as OtCE15A from the soil bacterium Opitutus terrae, have acidic residues at both the canonical and noncanonical positions. OtCE15A is a member of the CE15 family and the alpha/beta-hydrolase superfamily. It features acidic residues at both the canonical and noncanonical positions (Glu290 and Asp356). The observation of CE15 members with acidic residues at both positions may implicate evolutionary transitions between the two positions that could affect interactions with substrates and/or products. All CE15 members contain a catalytic triad comprised of Ser-His-Glu/Asp, as found in other serine-type hydrolases
evolution
the amino acid sequence of GE1 is used to identify homologous genes in the genomes of twenty-four fungi. Approximately half of the genomes, both from ascomycetes and basidiomycetes, contain putative orthologues, but their presence cannot be assigned to any of fungal class or subclass. Comparison of the amino acid sequences of identified and putative glucuronoyl esterases to other types of carbohydrate esterases (CE) confirms that they form a separate family of CEs
evolution
the enzyme belongs to the C15 family of carbohydrate esterases, the characteristic serine residue in the consensus sequence G-C-S-R-X-G involved in the catalytic mechanism is also conserved in enzyme NcGE. The enzyme harbors another two additional consensus sequences containing the glutamic acid and histidine residues that constitute the catalytic triad of enzyme NcGE
evolution
the enzyme belongs to the carbohydrate esterase family 15
evolution
the enzyme belongs to the carbohydrate esterase family 15 (CE-15)
evolution
the enzyme belongs to the carbohydrate esterase family, CE15
evolution
the enzyme belongs to the carbohydrate esterase family, CE15. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site of CE15 hydrolases
evolution
the enzyme belongs to the family 15 of carbohydrate esterases (CE15)
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. In Teredinibacter turnerae, a shipworm gut bacterium, GE is connected with endo-beta-1,4-xylanase of glycoside hydrolase (GH) family 11. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. In the bacterium Ruminococcus flavefaciens, GE occurs in a bifunctional enzyme in combination with a catalytic module of an acetylxylan esterase. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete carnosa each contain three GE genes, two of which code for CBM-containing enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete chrysosporium each contain three GE genes, two of which code for CBM-containing enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete chrysosporium each contain three GE genes, two of which code for CBM-scontaining enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
evolution
the enzyme is a member of the carbohydrate esterase family 15 (CE15)
evolution
the enzyme is a member of the CE15 family of carbohydrate esterases
evolution
-
the enzyme is a member of the CE15 family of carbohydrate esterases
-
evolution
-
the enzyme belongs to the carbohydrate esterase family 15 (CE-15)
-
evolution
-
the enzyme belongs to the carbohydrate esterase family, CE15
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
-
evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
-
evolution
-
the enzyme belongs to the carbohydrate esterase family, CE15. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site of CE15 hydrolases
-
evolution
-
the enzyme belongs to the carbohydrate esterase family, CE15. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site of CE15 hydrolases
-
evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
-
evolution
-
enzyme glucuronoyl esterase (GE) belongs to the carbohydrate esterase family 15 (CE15), CE15 phylogenetic analysis and tree, overview. Fungal and bacterial glucuronoyl esterases have been biochemically characterized using alkyl and alkyl aryl alcohol esters of 4-O-methyl glucuronic acid of varying complexity
-
evolution
-
the enzyme belongs to the C15 family of carbohydrate esterases, the characteristic serine residue in the consensus sequence G-C-S-R-X-G involved in the catalytic mechanism is also conserved in enzyme NcGE. The enzyme harbors another two additional consensus sequences containing the glutamic acid and histidine residues that constitute the catalytic triad of enzyme NcGE
-
evolution
Phanerodontia chrysosporium ATCC MYA-4764
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
Phanerodontia chrysosporium ATCC MYA-4764
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete carnosa each contain three GE genes, two of which code for CBM-containing enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
-
evolution
Phanerodontia chrysosporium ATCC MYA-4764
-
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
-
evolution
Phanerodontia chrysosporium ATCC MYA-4764
-
the amino acid sequence of GE1 is used to identify homologous genes in the genomes of twenty-four fungi. Approximately half of the genomes, both from ascomycetes and basidiomycetes, contain putative orthologues, but their presence cannot be assigned to any of fungal class or subclass. Comparison of the amino acid sequences of identified and putative glucuronoyl esterases to other types of carbohydrate esterases (CE) confirms that they form a separate family of CEs
-
evolution
-
glucuronoyl esterases (GEs) belong to the family 15 of carbohydrate esterases (CE15). Sequence comparison with enzyme Cip2 (UniProt ID G0RV93) from Hypocrea jecorina strain QM6a
-
evolution
-
the enzyme belongs to the C15 family of carbohydrate esterases, the characteristic serine residue in the consensus sequence G-C-S-R-X-G involved in the catalytic mechanism is also conserved in enzyme NcGE. The enzyme harbors another two additional consensus sequences containing the glutamic acid and histidine residues that constitute the catalytic triad of enzyme NcGE
-
evolution
-
the enzyme belongs to the carbohydrate esterase family, CE15. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site of CE15 hydrolases
-
evolution
Phanerodontia chrysosporium FGSC 9002
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
Phanerodontia chrysosporium FGSC 9002
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete carnosa each contain three GE genes, two of which code for CBM-containing enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
Phanerodontia chrysosporium FGSC 9002
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glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
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evolution
Phanerodontia chrysosporium FGSC 9002
-
the amino acid sequence of GE1 is used to identify homologous genes in the genomes of twenty-four fungi. Approximately half of the genomes, both from ascomycetes and basidiomycetes, contain putative orthologues, but their presence cannot be assigned to any of fungal class or subclass. Comparison of the amino acid sequences of identified and putative glucuronoyl esterases to other types of carbohydrate esterases (CE) confirms that they form a separate family of CEs
-
evolution
-
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
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evolution
-
glucuronoyl esterases have been assigned to CAZymes family 15 of carbohydrate esterases, phylogenetic analysis, detailed overview
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evolution
-
the enzyme belongs to the C15 family of carbohydrate esterases, the characteristic serine residue in the consensus sequence G-C-S-R-X-G involved in the catalytic mechanism is also conserved in enzyme NcGE. The enzyme harbors another two additional consensus sequences containing the glutamic acid and histidine residues that constitute the catalytic triad of enzyme NcGE
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evolution
-
the enzyme belongs to the C15 family of carbohydrate esterases, the characteristic serine residue in the consensus sequence G-C-S-R-X-G involved in the catalytic mechanism is also conserved in enzyme NcGE. The enzyme harbors another two additional consensus sequences containing the glutamic acid and histidine residues that constitute the catalytic triad of enzyme NcGE
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evolution
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glucuronoyl esterases (GEs) belong to the family 15 of carbohydrate esterases (CE15)
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evolution
Thermothelomyces thermophilus BCRC 31852
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the enzyme belongs to the carbohydrate esterase family 15 (CE-15)
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evolution
Thermothelomyces thermophilus BCRC 31852
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the enzyme belongs to the carbohydrate esterase family, CE15
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evolution
Thermothelomyces thermophilus BCRC 31852
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the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
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the enzyme belongs to the carbohydrate esterase family, CE15. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site of CE15 hydrolases
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evolution
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glucuronoyl esterases (GEs) belong to the family 15 of carbohydrate esterases (CE15)
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evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
-
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
-
evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. In Teredinibacter turnerae, a shipworm gut bacterium, GE is connected with endo-beta-1,4-xylanase of glycoside hydrolase (GH) family 11. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
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the enzyme belongs to the carbohydrate esterase family 15
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evolution
Thermothelomyces thermophilus ATCC 34628
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enzyme StGE1 is a family 15 glucuronoyl esterase that shows the highest homology with the hypothetical glucuronoyl esterase CHGG_10774 (UniProt ID Q2GMN0) of Chaetomium globosum strain CBS 148.51
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evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
Thermothelomyces thermophilus DSM 1799
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the enzyme belongs to the carbohydrate esterase family 15 (CE-15)
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evolution
Thermothelomyces thermophilus DSM 1799
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the enzyme belongs to the carbohydrate esterase family, CE15
-
evolution
Thermothelomyces thermophilus DSM 1799
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the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
Thermothelomyces thermophilus DSM 1799
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the enzyme is a member of the CE15 family of carbohydrate esterases
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evolution
-
the enzyme belongs to the C15 family of carbohydrate esterases, the characteristic serine residue in the consensus sequence G-C-S-R-X-G involved in the catalytic mechanism is also conserved in enzyme NcGE. The enzyme harbors another two additional consensus sequences containing the glutamic acid and histidine residues that constitute the catalytic triad of enzyme NcGE
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evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
-
evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. In Teredinibacter turnerae, a shipworm gut bacterium, GE is connected with endo-beta-1,4-xylanase of glycoside hydrolase (GH) family 11. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
-
the enzyme belongs to the carbohydrate esterase family 15
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete chrysosporium each contain three GE genes, two of which code for CBM-containing enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete chrysosporium each contain three GE genes, two of which code for CBM-scontaining enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
-
evolution
-
the enzyme belongs to the family 15 of carbohydrate esterases (CE15)
-
evolution
-
the glucuronoyl esterases evolve for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
evolution
-
the enzyme belongs to the family of carbohydrate esterases (CE15). The glucuronoyl esterases (GEs) evolved for hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. The genome of the white-rot fungus and also the genome of its close relative Phanerochaete carnosa each contain three GE genes, two of which code for CBM-containing enzymes. The majority of the genomes of white-rot fungi contain two GE genes, whereas the genomes of brown-rot fungi contain usually only one CE15 gene. Basidiomycetes have on average more genes in CE15 than do aspergilli, uneven GE gene distribution in microbial wood decay. Phylogenetic tree of confirmed and putative GEs, acetylxylan esterases, feruloyl esterases, and pectin methyl esterases, overview
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evolution
-
glucuronoyl esterases (GEs) are members of the carbohydrate esterase 15 family (CE15). Phylogenetic analysis, the evolutionary relationships of CE15 proteins are inferred by maximum likelihood method
-
evolution
-
the amino acid sequence of GE1 is used to identify homologous genes in the genomes of twenty-four fungi. Approximately half of the genomes, both from ascomycetes and basidiomycetes, contain putative orthologues, but their presence cannot be assigned to any of fungal class or subclass. Comparison of the amino acid sequences of identified and putative glucuronoyl esterases to other types of carbohydrate esterases (CE) confirms that they form a separate family of CEs
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malfunction
recombinant expression of enzyme PcGE in Arabidopsis thaliana strain Col-0 results in 3 transgenic lines consistently displaying a leaf-yellowing phenotype, as well as reduced glucose and xylose content by as much as 30% and 35%, respectively. Histological analysis reveals 50% reduction in cell wall thickness in the interfascicular fibres of transgenic plants, and FT-IR microspectroscopy of interfascicular fibre walls indicates reduction in lignin cross-linking in plants overexpressing PcGCE
malfunction
removal of an N-terminal CBM domain of CuGE affects the catalytic efficiently of the enzyme by reducing Kcat by more than 30%
malfunction
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recombinant expression of enzyme PcGE in Arabidopsis thaliana strain Col-0 results in 3 transgenic lines consistently displaying a leaf-yellowing phenotype, as well as reduced glucose and xylose content by as much as 30% and 35%, respectively. Histological analysis reveals 50% reduction in cell wall thickness in the interfascicular fibres of transgenic plants, and FT-IR microspectroscopy of interfascicular fibre walls indicates reduction in lignin cross-linking in plants overexpressing PcGCE
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metabolism
Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. Expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
metabolism
Phanerodontia chrysosporium ATCC MYA-4764
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Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. Expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
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metabolism
Phanerodontia chrysosporium FGSC 9002
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Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. Expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
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metabolism
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Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. Expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
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physiological function
Cip2 protein is a bimodular protein in which the catalytic module is connected to a carbohydrate binding module of family 1
physiological function
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family
physiological function
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
physiological function
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
physiological function
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
physiological function
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
physiological function
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
physiological function
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
physiological function
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
physiological function
a natural catalytic function of CuGE glucuronoyl esterase lays in hydrolysis of genuine lignin-carbohydrate complexes from birch. The detailed product profile of aldouronic acids released from birchwood lignin by a glucuronoyl esterase from the white-rot fungus Cerrena unicolor (CuGE): CuGE releases substrate for GH10 endo-xylanase which results in significantly increased product release compared to the action of endo-xylanase alone. CuGE also releases neutral xylo-oligosaccharides that can be ascribed to the enzymes feruloyl esterase side activity as demonstrated by release of ferulic acid from insoluble wheat arabinoxylan
physiological function
cellulose in plant cell walls is mainly covered by hemicellulose and lignin, and thus efficient removal of these components is thought to be a key step in the optimal utilization of lignocellulose. The carbohydrate esterase (CE) 15 family of glucuronoyl esterases (GEs), which cleave the linkages between the free carboxyl group of D-glucuronic acid in hemicellulose and the benzyl groups in lignin residues, can contribute to this process
physiological function
-
enzyme OtCE15A, and likely most of the CE15 family, can utilize esters of glucuronoxylooligosaccharides supporting the proposal that these enzymes work on lignin-carbohydratecomplexes in plant biomass
physiological function
fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes
physiological function
fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
physiological function
glucuronoyl esterases are considered to play a unique role as accessory enzymes in lignocellulosic material biodegradation by cleaving the covalent ester linkage between 4-O-methyl-D-glucuronic acid (MeGlcA) and lignin in lignin-carbohydrate complexes (LCCs). A substantial increase in the release of monomeric sugars and glucuronic acid from autohydrolysis of corn bran is observed by the supplementing TtGEs into commercial xylanase, demonstrating that the TtGEs play a significant role in this degradation process
physiological function
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase (GE) that constitutes the C15 family of carbohydrate esterases, displays a unique ability to cleave the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
physiological function
-
the enzyme hydrolyzes esters between xylan-bound 4-O-methyl-D-glucuronic acid and lignin alcohols occurring in plant cell walls
physiological function
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
physiological function
-
the enzyme might be involved in disruption of ester linkages connecting hemicellulose and lignin in plant cell walls
physiological function
-
the enzyme seems to play key roles in reducing lignocellulose recalcitrance by cleaving covalent ester bonds found between lignin and glucuronoxylan
physiological function
-
the enzyme seems to play key roles in reducing lignocellulose recalcitrance by cleaving covalent ester bonds found between lignin and glucuronoxylan
physiological function
-
the enzyme seems to play key roles in reducing lignocellulose recalcitrance by cleaving covalent ester bonds found between lignin and glucuronoxylan. Differential regulation of isozyme expression indicates nonredundancy and different roles of the CE15 enzymes in the biology of Spirosoma linguale
physiological function
the glucuronoyl esterase (GE) from Cerrena unicolor (CuGE) catalyzes cleavage of lignin-carbohydrate ester bonds
physiological function
-
the thermostable, dual-function enzyme CkXyn10C-GE15A from the hyperthermophilic bacterium Caldicellulosiruptor kristjanssonii shows xylanase as well as glucuronoyl esterase activities. Although the enzyme domains are naturally linked together, when added separately to biomass, the expected boosting of the xylanase action is not seen. This lack of intramolecular synergy might suggest, that increased xylose release is not the main beneficial trait given by glucuronoyl esterases
physiological function
-
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the enzyme hydrolyzes esters between xylan-bound 4-O-methyl-D-glucuronic acid and lignin alcohols occurring in plant cell walls
-
physiological function
-
the enzyme might be involved in disruption of ester linkages connecting hemicellulose and lignin in plant cell walls
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the enzyme seems to play key roles in reducing lignocellulose recalcitrance by cleaving covalent ester bonds found between lignin and glucuronoxylan
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase (GE) that constitutes the C15 family of carbohydrate esterases, displays a unique ability to cleave the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
Phanerodontia chrysosporium ATCC MYA-4764
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
Phanerodontia chrysosporium ATCC MYA-4764
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
cellulose in plant cell walls is mainly covered by hemicellulose and lignin, and thus efficient removal of these components is thought to be a key step in the optimal utilization of lignocellulose. The carbohydrate esterase (CE) 15 family of glucuronoyl esterases (GEs), which cleave the linkages between the free carboxyl group of D-glucuronic acid in hemicellulose and the benzyl groups in lignin residues, can contribute to this process
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase (GE) that constitutes the C15 family of carbohydrate esterases, displays a unique ability to cleave the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
Phanerodontia chrysosporium FGSC 9002
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
Phanerodontia chrysosporium FGSC 9002
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase (GE) that constitutes the C15 family of carbohydrate esterases, displays a unique ability to cleave the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase (GE) that constitutes the C15 family of carbohydrate esterases, displays a unique ability to cleave the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
glucuronoyl esterases are considered to play a unique role as accessory enzymes in lignocellulosic material biodegradation by cleaving the covalent ester linkage between 4-O-methyl-D-glucuronic acid (MeGlcA) and lignin in lignin-carbohydrate complexes (LCCs). A substantial increase in the release of monomeric sugars and glucuronic acid from autohydrolysis of corn bran is observed by the supplementing TtGEs into commercial xylanase, demonstrating that the TtGEs play a significant role in this degradation process
-
physiological function
Thermothelomyces thermophilus BCRC 31852
-
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family
-
physiological function
Thermothelomyces thermophilus BCRC 31852
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
glucuronoyl esterases are considered to play a unique role as accessory enzymes in lignocellulosic material biodegradation by cleaving the covalent ester linkage between 4-O-methyl-D-glucuronic acid (MeGlcA) and lignin in lignin-carbohydrate complexes (LCCs). A substantial increase in the release of monomeric sugars and glucuronic acid from autohydrolysis of corn bran is observed by the supplementing TtGEs into commercial xylanase, demonstrating that the TtGEs play a significant role in this degradation process
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
Thermothelomyces thermophilus ATCC 34628
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
physiological function
-
Cip2 protein is a bimodular protein in which the catalytic module is connected to a carbohydrate binding module of family 1
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
Thermothelomyces thermophilus DSM 1799
-
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family
-
physiological function
Thermothelomyces thermophilus DSM 1799
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
the complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase (GE) that constitutes the C15 family of carbohydrate esterases, displays a unique ability to cleave the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
physiological function
-
the enzyme plays an important role in microbial breakdown of plant cell walls. The microbial enzyme hydrolyses the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls
-
physiological function
-
glucuronoyl esterases (GEs) catalyze the hydrolysis of the ester linkages between 4-O-methyl-D-glucuronic acid of plant glucuronoxylans and lignin alcohols, one of the crosslinks in the plant cell walls. They have catalytic properties on artificial substrates and positive effect on enzymatic saccharification of plant biomass. The enzyme plays an important role in plant cell wall degradation
-
additional information
-
as there are no bacterial CBM1 modules, it is possible that the CBM9 modules present in CkXyn10C-GE15A are performing a similar function as the CBM1 modules would in fungal enzymes
additional information
-
at pH 6.0, the enzyme does not bind to cellulose indicating the absence of a cellulose binding module, and the enzyme is not inhibited by PMSF suggesting that it does not belong to serine-type esterases
additional information
catalytic domain structure analysis, overview. Wild-type CuGE has a modular architecture with a N-terminal carbohydrate-binding module 1 (CBM1) domain connected to the catalytic domain by a proline-rich linker region. The structure of CuGE is potentially flexible and shows heterogenous N- and O-glycosylation. Active site architecture and ligand-induced oxyanion hole. Structure and substrate binding comparisons of CE15-A and CE15-B enzymes. Detailed structure-function analysis of CE15 enzymes, overview
additional information
-
catalytic domain structure analysis, overview. Wild-type CuGE has a modular architecture with a N-terminal carbohydrate-binding module 1 (CBM1) domain connected to the catalytic domain by a proline-rich linker region. The structure of CuGE is potentially flexible and shows heterogenous N- and O-glycosylation. Active site architecture and ligand-induced oxyanion hole. Structure and substrate binding comparisons of CE15-A and CE15-B enzymes. Detailed structure-function analysis of CE15 enzymes, overview
additional information
docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template. Enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site
additional information
-
docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template. Enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site
additional information
enzyme active site structure and structure comparisons, overview. TtCE15A has an alpha/beta-hydrolase fold similar to other CE15 structures, consisting of a three-layer sandwich with a solvent-exposed cleft comprising the active site with its catalytic triad. Three TtCE15A molecules are found in the asymmetric unit, with a Calpha root mean square deviation below 0.2A, indicating a high degree of similarity between the protein chains. The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
additional information
-
enzyme active site structure and structure comparisons, overview. TtCE15A has an alpha/beta-hydrolase fold similar to other CE15 structures, consisting of a three-layer sandwich with a solvent-exposed cleft comprising the active site with its catalytic triad. Three TtCE15A molecules are found in the asymmetric unit, with a Calpha root mean square deviation below 0.2A, indicating a high degree of similarity between the protein chains. The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
additional information
-
kinetic characterization of catalytic residue substitutions, structure, ligand interactions, and catalytic mechanism of catalytic OtCE15A variants in complex with GlcA and benzyl glucuronoate, structure analysis of OtCE15A S267A mutant in complex with methylgalacturonate and with the glucuronoxylan oligosaccharide XUX, overview
additional information
molecular docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template
additional information
-
molecular docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template
additional information
role of conserved Lys209 residue in the preference for 4-O-methyl glucuronoyl esters, AfGE docking study and structure homology molecular modeling using the crystal structure of StGE2 S213A mutant docked with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB ID 4G4J) as the template, overview
additional information
-
role of conserved Lys209 residue in the preference for 4-O-methyl glucuronoyl esters, AfGE docking study and structure homology molecular modeling using the crystal structure of StGE2 S213A mutant docked with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB ID 4G4J) as the template, overview
additional information
structure homology modelling, structure comparisons, overview
additional information
-
structure homology modelling, structure comparisons, overview
additional information
-
the catalytic triad (Ser/His/Glu) and most of the residues shown to interact with the glucuronoate ester moiety in the previously solved fungal structures are conserved in OtCE15A, structure-function analysis, overview
additional information
-
the catalytic triad (Ser/His/Glu) and most of the residues shown to interact with the glucuronoate ester moiety in the previously solved fungal structures are conserved in SuCE15C, structure-function analysis, overview
additional information
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family, the candidate nucleophilic residue Ser213 is responsible for catalyzing the enzymatic reaction
additional information
-
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family, the candidate nucleophilic residue Ser213 is responsible for catalyzing the enzymatic reaction
additional information
the enzyme has a S-E-H catalytic triad
additional information
the enzyme has a S-X-H catalytic triad
additional information
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM). NcGE has a consensus G-C-S-R-X-G motif conserved in the CE15 family where the serine residue serves as the catalytic nucleophile
additional information
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM). NcGE has a consensus G-C-S-R-X-G motif conserved in the CE15 family where the serine residue serves as the catalytic nucleophile
additional information
three-dimensional homology structure modelling of StGE2 by molecular replacement using the structure of Cip2_GE (PDB ID 3pic, UniProt ID G0RV93) from Hypocrea jecorina strain QM6a as a starting model. The three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit. The residues lining the H12 alpha-helix and the preceding loop region are distorted compared with those in the Cip2_GE structure since the N-linked glycosylation sequence motif (Asn-X-Ser) and the N-acetylglucosamine molecule bound at Asn447 observed in the latter are missing in StGE2 (Asn-X-Ala) is the corresponding motif in StGE2. Determination of the StGE2 catalytic site structure, overview. The catalytic triad residues, namely Ser213, Glu236 and His346, participate in a concrete ready-for-nucleophilic-attack configuration
additional information
-
three-dimensional homology structure modelling of StGE2 by molecular replacement using the structure of Cip2_GE (PDB ID 3pic, UniProt ID G0RV93) from Hypocrea jecorina strain QM6a as a starting model. The three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit. The residues lining the H12 alpha-helix and the preceding loop region are distorted compared with those in the Cip2_GE structure since the N-linked glycosylation sequence motif (Asn-X-Ser) and the N-acetylglucosamine molecule bound at Asn447 observed in the latter are missing in StGE2 (Asn-X-Ala) is the corresponding motif in StGE2. Determination of the StGE2 catalytic site structure, overview. The catalytic triad residues, namely Ser213, Glu236 and His346, participate in a concrete ready-for-nucleophilic-attack configuration
additional information
three-dimensional structure determination and analysis, the structure has an alpha/beta-hydrolase fold with an overall alphabetaalpha-sandwich architecture. The twisted beeta-sheet is sandwiched between two layers of alpha-helices with the catalytic triad Ser-His-Glu exposed on the protein surface
additional information
three-dimensional structure determination and analysis, the structure has an alpha/beta-hydrolase fold with an overall alphabetaalpha-sandwich architecture. The twisted beeta-sheet is sandwiched between two layers of alpha-helices with the catalytic triad Ser-His-Glu exposed on the protein surface
additional information
-
usage of peptide pattern recognition (PPR) to identify putative CE15 enzymes
additional information
usage of peptide pattern recognition (PPR) to identify putative CE15 enzymes
additional information
usage of peptide pattern recognition (PPR) to identify putative CE15 enzymes
additional information
-
three-dimensional homology structure modelling of StGE2 by molecular replacement using the structure of Cip2_GE (PDB ID 3pic, UniProt ID G0RV93) from Hypocrea jecorina strain QM6a as a starting model. The three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit. The residues lining the H12 alpha-helix and the preceding loop region are distorted compared with those in the Cip2_GE structure since the N-linked glycosylation sequence motif (Asn-X-Ser) and the N-acetylglucosamine molecule bound at Asn447 observed in the latter are missing in StGE2 (Asn-X-Ala) is the corresponding motif in StGE2. Determination of the StGE2 catalytic site structure, overview. The catalytic triad residues, namely Ser213, Glu236 and His346, participate in a concrete ready-for-nucleophilic-attack configuration
-
additional information
-
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family, the candidate nucleophilic residue Ser213 is responsible for catalyzing the enzymatic reaction
-
additional information
-
molecular docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template
-
additional information
-
three-dimensional structure determination and analysis, the structure has an alpha/beta-hydrolase fold with an overall alphabetaalpha-sandwich architecture. The twisted beeta-sheet is sandwiched between two layers of alpha-helices with the catalytic triad Ser-His-Glu exposed on the protein surface
-
additional information
-
at pH 6.0, the enzyme does not bind to cellulose indicating the absence of a cellulose binding module, and the enzyme is not inhibited by PMSF suggesting that it does not belong to serine-type esterases
-
additional information
-
docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template. Enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site
-
additional information
-
docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template. Enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site
-
additional information
-
the catalytic triad (Ser/His/Glu) and most of the residues shown to interact with the glucuronoate ester moiety in the previously solved fungal structures are conserved in SuCE15C, structure-function analysis, overview
-
additional information
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM). NcGE has a consensus G-C-S-R-X-G motif conserved in the CE15 family where the serine residue serves as the catalytic nucleophile
-
additional information
-
role of conserved Lys209 residue in the preference for 4-O-methyl glucuronoyl esters, AfGE docking study and structure homology molecular modeling using the crystal structure of StGE2 S213A mutant docked with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB ID 4G4J) as the template, overview
-
additional information
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM). NcGE has a consensus G-C-S-R-X-G motif conserved in the CE15 family where the serine residue serves as the catalytic nucleophile
-
additional information
-
docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template. Enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site
-
additional information
-
usage of peptide pattern recognition (PPR) to identify putative CE15 enzymes
-
additional information
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM). NcGE has a consensus G-C-S-R-X-G motif conserved in the CE15 family where the serine residue serves as the catalytic nucleophile
-
additional information
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM). NcGE has a consensus G-C-S-R-X-G motif conserved in the CE15 family where the serine residue serves as the catalytic nucleophile
-
additional information
Thermothelomyces thermophilus BCRC 31852
-
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family, the candidate nucleophilic residue Ser213 is responsible for catalyzing the enzymatic reaction
-
additional information
Thermothelomyces thermophilus BCRC 31852
-
molecular docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template
-
additional information
Thermothelomyces thermophilus BCRC 31852
-
three-dimensional structure determination and analysis, the structure has an alpha/beta-hydrolase fold with an overall alphabetaalpha-sandwich architecture. The twisted beeta-sheet is sandwiched between two layers of alpha-helices with the catalytic triad Ser-His-Glu exposed on the protein surface
-
additional information
-
docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template. Enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. The conserved sequence G-C-S-R-N-G contains the catalytic nucleophile serine as component of the catalytic site
-
additional information
-
enzyme active site structure and structure comparisons, overview. TtCE15A has an alpha/beta-hydrolase fold similar to other CE15 structures, consisting of a three-layer sandwich with a solvent-exposed cleft comprising the active site with its catalytic triad. Three TtCE15A molecules are found in the asymmetric unit, with a Calpha root mean square deviation below 0.2A, indicating a high degree of similarity between the protein chains. The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
-
additional information
-
structure homology modelling, structure comparisons, overview
-
additional information
-
three-dimensional structure determination and analysis, the structure has an alpha/beta-hydrolase fold with an overall alphabetaalpha-sandwich architecture. The twisted beeta-sheet is sandwiched between two layers of alpha-helices with the catalytic triad Ser-His-Glu exposed on the protein surface
-
additional information
Thermothelomyces thermophilus DSM 1799
-
the consensus sequence G-C-S-R-X-G features the characteristic serine residue involved in the generally conserved catalytic mechanism of the esterase family, the candidate nucleophilic residue Ser213 is responsible for catalyzing the enzymatic reaction
-
additional information
Thermothelomyces thermophilus DSM 1799
-
molecular docking calculations using the crystal structure of GE2 S213A mutant from Myceliophthora thermophila in complex with methyl 4-O-methyl-beta-D-glucopyranuronate (PDB code 4G4J) as template
-
additional information
Thermothelomyces thermophilus DSM 1799
-
three-dimensional structure determination and analysis, the structure has an alpha/beta-hydrolase fold with an overall alphabetaalpha-sandwich architecture. The twisted beeta-sheet is sandwiched between two layers of alpha-helices with the catalytic triad Ser-His-Glu exposed on the protein surface
-
additional information
Thermothelomyces thermophilus DSM 1799
-
three-dimensional homology structure modelling of StGE2 by molecular replacement using the structure of Cip2_GE (PDB ID 3pic, UniProt ID G0RV93) from Hypocrea jecorina strain QM6a as a starting model. The three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit. The residues lining the H12 alpha-helix and the preceding loop region are distorted compared with those in the Cip2_GE structure since the N-linked glycosylation sequence motif (Asn-X-Ser) and the N-acetylglucosamine molecule bound at Asn447 observed in the latter are missing in StGE2 (Asn-X-Ala) is the corresponding motif in StGE2. Determination of the StGE2 catalytic site structure, overview. The catalytic triad residues, namely Ser213, Glu236 and His346, participate in a concrete ready-for-nucleophilic-attack configuration
-
additional information
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM). NcGE has a consensus G-C-S-R-X-G motif conserved in the CE15 family where the serine residue serves as the catalytic nucleophile
-
additional information
-
enzyme active site structure and structure comparisons, overview. TtCE15A has an alpha/beta-hydrolase fold similar to other CE15 structures, consisting of a three-layer sandwich with a solvent-exposed cleft comprising the active site with its catalytic triad. Three TtCE15A molecules are found in the asymmetric unit, with a Calpha root mean square deviation below 0.2A, indicating a high degree of similarity between the protein chains. The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40200
40300
44000
calculated, enzyme with a Myc-His tag added to the C-terminal end of AfGE by the fusion PCR
46700
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
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x * 44000, recombinant deglycosylated Myc-His-tagged enzyme AfGE, SDS-PAGE
?
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x * 44000, recombinant deglycosylated Myc-His-tagged enzyme AfGE, SDS-PAGE
-
?
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x * 44700, recombinant His6-tagged isozyme LfGE1, SDS-PAGE, x * 42100, recombinant His6-tagged isozyme LfGE2, SDS-PAGE, x * 43900, recombinant His6-tagged isozyme LfGE3, SDS-PAGE
?
x * 41300, about, sequence calculation, x * 44000, recombinant c-myc- and His6-tagged enzyme, SDS-PAGE
?
-
x * 41300, about, sequence calculation, x * 44000, recombinant c-myc- and His6-tagged enzyme, SDS-PAGE
-
?
-
x * 41300, about, sequence calculation, x * 44000, recombinant c-myc- and His6-tagged enzyme, SDS-PAGE
-
?
-
x * 41300, about, sequence calculation, x * 44000, recombinant c-myc- and His6-tagged enzyme, SDS-PAGE
-
?
-
x * 41300, about, sequence calculation, x * 44000, recombinant c-myc- and His6-tagged enzyme, SDS-PAGE
-
?
-
x * 41300, about, sequence calculation, x * 44000, recombinant c-myc- and His6-tagged enzyme, SDS-PAGE
-
?
x * 72000, recombinant glycosylated His-tagged enzyme, SDS-PAGE, x * 42000, about, sequence calculation, x * 50000, recombinant PNGase F-deglycosylated enzyme, SDS-PAGE
?
-
x * 72000, recombinant glycosylated His-tagged enzyme, SDS-PAGE, x * 42000, about, sequence calculation, x * 50000, recombinant PNGase F-deglycosylated enzyme, SDS-PAGE
-
?
x * 50942, calculated, x * 63000, SDS-PAGE of recombinant protein
?
x * 63000, recombinant enzyme, SDS-PAGE, x * 51700, about, sequence calculation
?
-
x * 50942, calculated, x * 63000, SDS-PAGE of recombinant protein
-
?
-
x * 63000, recombinant enzyme, SDS-PAGE, x * 51700, about, sequence calculation
-
?
-
x * 63000, recombinant enzyme, SDS-PAGE, x * 51700, about, sequence calculation
-
?
-
x * 50942, calculated, x * 63000, SDS-PAGE of recombinant protein
-
?
-
x * 63000, recombinant enzyme, SDS-PAGE, x * 51700, about, sequence calculation
-
?
-
x * 63000, recombinant enzyme, SDS-PAGE, x * 51700, about, sequence calculation
-
?
x * 42881, calulated, x * 43000, recombinant protein with His-tag
?
x * 43000, recombinant enzyme, SDS-PAGE, x * 40056, sequence calculation
?
-
x * 42881, calulated, x * 43000, recombinant protein with His-tag
-
?
-
x * 43000, recombinant enzyme, SDS-PAGE, x * 40056, sequence calculation
-
?
Thermothelomyces thermophilus BCRC 31852
-
x * 42881, calulated, x * 43000, recombinant protein with His-tag
-
?
Thermothelomyces thermophilus BCRC 31852
-
x * 43000, recombinant enzyme, SDS-PAGE, x * 40056, sequence calculation
-
?
Thermothelomyces thermophilus DSM 1799
-
x * 42881, calulated, x * 43000, recombinant protein with His-tag
-
?
Thermothelomyces thermophilus DSM 1799
-
x * 43000, recombinant enzyme, SDS-PAGE, x * 40056, sequence calculation
-
?
x * 50000, about, recombinant glycosylated enzyme, SDS-PAGE, x * 39000, recombinant deglycosylated enzyme, SDS-PAGE
?
-
x * 50000, about, recombinant glycosylated enzyme, SDS-PAGE, x * 39000, recombinant deglycosylated enzyme, SDS-PAGE
-
?
-
x * 50000, about, recombinant glycosylated enzyme, SDS-PAGE, x * 39000, recombinant deglycosylated enzyme, SDS-PAGE
-
?
x * 46400, sequence calculation, x * 55000, recombinant enzyme, SDS-PAGE
?
-
x * 46400, sequence calculation, x * 55000, recombinant enzyme, SDS-PAGE
-
additional information
-
domain architecture of CkXyn10C-GE15A with ten domains: enzyme CkXyn10C-GE15A contains two distinct putative catalytic modules: a GH10 xylanase and a GE from CE15. In addition, two N-terminal CBM22 domains as well as three CBM9 domains sandwiched between the catalytic domains are predicted, as well as a cadherin-like domain and two surface layer homology (SLH) domains following the GE domain at the C-terminus
additional information
the enzyme is modular, comprised of a catalytic and a carbohydrate-binding domain. CuGE is an elongated rigid molecule where the two domains are connected by a rigid linker. The overall fold of the catalytic domain of CuGE features a large ten-stranded twisted beta-sheet flanked by alpha-helical elements and a surface-exposed active site. The structure complies with the characteristics of a serine esterase belonging to the alpha/beta-hydrolase superfamily
additional information
-
the enzyme is modular, comprised of a catalytic and a carbohydrate-binding domain. CuGE is an elongated rigid molecule where the two domains are connected by a rigid linker. The overall fold of the catalytic domain of CuGE features a large ten-stranded twisted beta-sheet flanked by alpha-helical elements and a surface-exposed active site. The structure complies with the characteristics of a serine esterase belonging to the alpha/beta-hydrolase superfamily
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
multidomain structures of glucuronoyl esterases (GEs), Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. The catalytic domains of the GEs are almost identical
additional information
multidomain structures of glucuronoyl esterases (GEs), Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. The catalytic domains of the GEs are almost identical
additional information
Phanerodontia chrysosporium ATCC MYA-4764
-
multidomain structures of glucuronoyl esterases (GEs), Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. The catalytic domains of the GEs are almost identical
-
additional information
Phanerodontia chrysosporium FGSC 9002
-
multidomain structures of glucuronoyl esterases (GEs), Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. The catalytic domains of the GEs are almost identical
-
additional information
-
multidomain structures of glucuronoyl esterases (GEs), Phanerochaete chrysosporium produces two enzyme forms, one without (GE2) and one with (GE1) the CBM1 module. The catalytic domains of the GEs are almost identical
-
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
the sequence predicts a family 1 carbohydrate-binding module (CBM1) (22-59), a linker peptide (60-105), and a catalytic CE15 module (106-481)
additional information
-
the sequence predicts a family 1 carbohydrate-binding module (CBM1) (22-59), a linker peptide (60-105), and a catalytic CE15 module (106-481)
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
-
the sequence predicts a family 1 carbohydrate-binding module (CBM1) (22-59), a linker peptide (60-105), and a catalytic CE15 module (106-481)
-
additional information
-
the sequence predicts a family 1 carbohydrate-binding module (CBM1) (22-59), a linker peptide (60-105), and a catalytic CE15 module (106-481)
-
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
-
the sequence predicts a family 1 carbohydrate-binding module (CBM1) (22-59), a linker peptide (60-105), and a catalytic CE15 module (106-481)
-
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
-
the sequence predicts a family 1 carbohydrate-binding module (CBM1) (22-59), a linker peptide (60-105), and a catalytic CE15 module (106-481)
-
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
-
StGE1 is a modular enzyme, peptide fragmentation fingerprint, and mass spectrometric analysis, amino acid sequence comparison
additional information
the three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit
additional information
-
the three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit
additional information
Thermothelomyces thermophilus ATCC 34628
-
StGE1 is a modular enzyme, peptide fragmentation fingerprint, and mass spectrometric analysis, amino acid sequence comparison
-
additional information
-
the three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit
-
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
Thermothelomyces thermophilus BCRC 31852
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
Thermothelomyces thermophilus DSM 1799
-
multidomain structures of glucuronoyl esterases (GEs)
-
additional information
Thermothelomyces thermophilus DSM 1799
-
the three-dimensional protein structures of wild-type and mutant enzymes have an alpha/beta-hydrolase fold with a three-layer alphabetaalpha-sandwich architecture and a Rossmann topology and comprise one molecule per asymmetric unit
-
additional information
multidomain structures of glucuronoyl esterases (GEs)
additional information
the full-length Cip2 protein contains a carbohydrate-binding module, a linker and a catalytic domain
additional information
-
the full-length Cip2 protein contains a carbohydrate-binding module, a linker and a catalytic domain
additional information
the mass of the Cip2 CBM and linker (unglycosylated) domains is 3.73 kDa and 3.92 kDa, respectively. Peptide mapping, pepitdes are identified by HPLC/tandem mass spectrometry after trypsin digestion of Cip2
additional information
-
the mass of the Cip2 CBM and linker (unglycosylated) domains is 3.73 kDa and 3.92 kDa, respectively. Peptide mapping, pepitdes are identified by HPLC/tandem mass spectrometry after trypsin digestion of Cip2
additional information
-
the mass of the Cip2 CBM and linker (unglycosylated) domains is 3.73 kDa and 3.92 kDa, respectively. Peptide mapping, pepitdes are identified by HPLC/tandem mass spectrometry after trypsin digestion of Cip2
-
additional information
-
multidomain structures of glucuronoyl esterases (GEs)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
glycoprotein
-
the enzyme has two potential N-glycosylation sites
-
glycoprotein
heterogenous N- and O-glycosylation. Deglycosylation by Endo H and alpha-1-2,3,6 mannosidase
glycoprotein
enzyme PcGE contains eight putative N-glycosylation sites, treatment of PcGCE with N-glycosidase F (PNGase F) reduces the molecular weight of the enzyme from 72 kDa to approximately 50 kDa
glycoprotein
-
enzyme PcGE contains eight putative N-glycosylation sites, treatment of PcGCE with N-glycosidase F (PNGase F) reduces the molecular weight of the enzyme from 72 kDa to approximately 50 kDa
-
glycoprotein
PcGE1 does not contain the Asn-Xaa-Ser/Thr sequon that usually signifies an N-glycosylation site in eukaryotes, but the observed molecular weight of PcGE1 is about 10 kDa higher than calculated, which could be due to a heavily O-glycosylated linker region between the CBM1 and the CE15 catalytic domain
glycoprotein
Phanerodontia chrysosporium ATCC MYA-4764
-
PcGE1 does not contain the Asn-Xaa-Ser/Thr sequon that usually signifies an N-glycosylation site in eukaryotes, but the observed molecular weight of PcGE1 is about 10 kDa higher than calculated, which could be due to a heavily O-glycosylated linker region between the CBM1 and the CE15 catalytic domain
-
glycoprotein
Phanerodontia chrysosporium FGSC 9002
-
PcGE1 does not contain the Asn-Xaa-Ser/Thr sequon that usually signifies an N-glycosylation site in eukaryotes, but the observed molecular weight of PcGE1 is about 10 kDa higher than calculated, which could be due to a heavily O-glycosylated linker region between the CBM1 and the CE15 catalytic domain
-
glycoprotein
-
PcGE1 does not contain the Asn-Xaa-Ser/Thr sequon that usually signifies an N-glycosylation site in eukaryotes, but the observed molecular weight of PcGE1 is about 10 kDa higher than calculated, which could be due to a heavily O-glycosylated linker region between the CBM1 and the CE15 catalytic domain
-
glycoprotein
the enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. No potential N-glycosylation sites are identified along the whole protein sequence, but 22 O-glycosylation sites are predicted located in the linker region upstream of the catalytic domain of PaGE1
glycoprotein
-
the enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. No potential N-glycosylation sites are identified along the whole protein sequence, but 22 O-glycosylation sites are predicted located in the linker region upstream of the catalytic domain of PaGE1
-
glycoprotein
-
the enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. No potential N-glycosylation sites are identified along the whole protein sequence, but 22 O-glycosylation sites are predicted located in the linker region upstream of the catalytic domain of PaGE1
-
glycoprotein
-
the enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. No potential N-glycosylation sites are identified along the whole protein sequence, but 22 O-glycosylation sites are predicted located in the linker region upstream of the catalytic domain of PaGE1
-
glycoprotein
-
the enzyme GE1 possesses a N-terminal family 1 carbohydrate-binding module (CBM) and a catalytic domain, linked by a hinge region. No potential N-glycosylation sites are identified along the whole protein sequence, but 22 O-glycosylation sites are predicted located in the linker region upstream of the catalytic domain of PaGE1
-
glycoprotein
AaGE1 does not contain the Asn-Xaa-Ser/Thr sequon that usually signifies an N-glycosylation site in eukaryotes, but the observed molecular weight of AaGE1 is about 10 kDa higher than calculated, which is due to a heavily O-glycosylated linker region between the CBM1 and the CE15 catalytic domain
glycoprotein
-
StGE1 contains a noncatalytic carbohydrate-binding module
glycoprotein
Thermothelomyces thermophilus ATCC 34628
-
StGE1 contains a noncatalytic carbohydrate-binding module
-
glycoprotein
enzyme TtGE1 is N-glycosylated, and possesses three predicted N-glycosylation sites
glycoprotein
enzyme TtGE2 is N-glycosylated, and possesses two predicted N-glycosylation sites
glycoprotein
-
enzyme TtGE1 is N-glycosylated, and possesses three predicted N-glycosylation sites
-
glycoprotein
-
enzyme TtGE2 is N-glycosylated, and possesses two predicted N-glycosylation sites
-
glycoprotein
-
enzyme TtGE1 is N-glycosylated, and possesses three predicted N-glycosylation sites
-
glycoprotein
-
enzyme TtGE2 is N-glycosylated, and possesses two predicted N-glycosylation sites
-
glycoprotein
an N-linked glycosylation site is expected by the sequence motif (Asn-Xxx-Ser/Thr) at Asn447. A molecule of N-acetylglucosamine (NAG) is modeled into the density linked to the side chain of Asn447 in all three protein chains. There is weak density to indicate the presence of another sugar moiety attached to the first NAG molecule in each case. There could be more sugar molecules linked but they are disordered in the crystal. No evidence of any O-linked glycosylation in the catalytic domain of Cip2
glycoprotein
family 1 CBM sequences are found in enzyme TrCip2, N-glycosylation site N447QS might be glycosylated. N- and/or O-glycosylation is commonly found for secreted proteins by Hypocrea jecorina
glycoprotein
-
family 1 CBM sequences are found in enzyme TrCip2, N-glycosylation site N447QS might be glycosylated. N- and/or O-glycosylation is commonly found for secreted proteins by Hypocrea jecorina
-
glycoprotein
-
an N-linked glycosylation site is expected by the sequence motif (Asn-Xxx-Ser/Thr) at Asn447. A molecule of N-acetylglucosamine (NAG) is modeled into the density linked to the side chain of Asn447 in all three protein chains. There is weak density to indicate the presence of another sugar moiety attached to the first NAG molecule in each case. There could be more sugar molecules linked but they are disordered in the crystal. No evidence of any O-linked glycosylation in the catalytic domain of Cip2
-
glycoprotein
enzyme WcGE1 is predicted to contain between two and five sites of the Asn-Xaa-Ser/Thr sequon that usually signifies an N-glycosylation site in eukaryotes. WcGE1 has up to 5 N-glycans
glycoprotein
-
enzyme WcGE1 is predicted to contain between two and five sites of the Asn-Xaa-Ser/Thr sequon that usually signifies an N-glycosylation site in eukaryotes. WcGE1 has up to 5 N-glycans
-
no glycoprotein
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM)
no glycoprotein
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM)
-
no glycoprotein
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM)
-
no glycoprotein
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM)
-
no glycoprotein
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM)
-
no glycoprotein
-
the genomic sequence encoding NcGE does not contain any intron and the deduced protein lacks the carbohydrate binding module (CBM)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray diffraction structure determination and analysis of isozyme SuCE15C at 2.02 A resolution, solved by SAD phasing with seleno-L-methionine, PDB ID 6gu8, structure comparison
-
purified isolated deglycosylated wild-type and mutant S207A catalytic domains, X-ray diffraction structure determination and analysis at 1.46-1.96 A resolution, structure modelling by molecular replacement using Cip2 (PDB ID 3PIC) as search model
purified OtCE15A S267A mutant in complex with methylgalacturonate and in complex with the glucuronoxylan oligosaccharide XUX, X-ray diffraction structure determination analysis
-
X-ray diffraction structure determination and analysis of isozyme OtCE15A at 1.5 A resolution, solved by SAD phasing gold-derivatized, PDB ID 6grw, structure comparison
-
purified recombinant enzyme TtCE15A, sitting drop vapour diffusion method, mixing of protein:reservoir volume ratios of 3:1 or 1:1 using 35 mg/ml protein in 20 mM Tris, pH 8.0, and reservoir solution containing 0.09 M halogens, 0.1 M imidazole and MES buffer, and 50% v/v precipitant mixture 2 containing 40% v/v ethylene glycol and 20% w/v PEG 8000, X-ray diffraction structure determination and analysis at 2.5 A, molecular replacement and model building
purified unliganded wild-type and mutant S213A enzymes, and S213A mutant in complex with a substrate analogue methyl 4-O-methyl-beta-D-glucopyranuronate, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 30% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.0, for the mutant and 0.1 M sodium acetate, pH 4.6, 25% v/v PEG 550 MME for the wild-type as precipitant solutions, at 16°C, X-ray diffraction structure determination and analysis at 1.55 A, 1.9 A, and 2.35 A resolution, respectively
wild-type and mutant S213A, to 1.55 A and 1.9 A resolution, and mutant S213A in complex with substrate analogue, methyl 4-O-methyl-beta-D-glucopyranuronate. Serine-type hydrolase, its overall architecture follows the three-layer alphabetaalpha-sandwich hydrolase fold with a Rossmann-fold topology. Ser213, His346 and Glu236 are putative catalytic triad residues
purified catalytic domain from glucuronoyl esterase Cip2, for obtaining a heavy atom derivative, the native crystals are briefly (2-3 min) soaked in the reservoir solution containing K2PtCl4 (1 mg in 0.01 ml of Quik Screen D3), X-ray diffraction structure determination and analysis at 2.50 A resolution. Cocrystallization experiments of Cip2_GE are carried out in the presence of the inhibitor PMSF (2 mM) and in the presence of substrate methyl ester of 4-O-methyl-D-glucuronic acid (7 mM) and substrate 4-O-methyl-D-glucuronic acid linked alpha-1,2 to 4-nitrophenyl-beta-D-xylopyranoside (0.6 mM) in the conditions that produced native crystals, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified isolated glucuronoyl esterase catalytic domain, sitting drop vapor diffusion method using 1.4 M sodium/potassium phosphate pH 6.9, equilibrating a mixture of 400 nl 25 mg/ml protein in 20 mM Tris, pH 7.5, with 400 nl screen solution over a reservoir of 0.2 ml screen solution, containing 27% w/v sucrose and 0.5 M NaBr for crystal 1, 27% w/v sucrose and 1.0 M NaBr for crystal 2, and 27% w/v sucrose only for crystal 3, the crystals belong to space group P212121, at 35°C, crystals typically form in 2-3 days and grow to full size in a week, X-ray diffraction structure determination and analysis at 1.95-2.50 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K209A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
K209E
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
K209Q
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
K209R
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzymethe mutant shows altered substrate specificity compared to the wild-type enzyme
K209A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
K209E
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
K209Q
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
K209R
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzymethe mutant shows altered substrate specificity compared to the wild-type enzyme
-
S270A
site-directed mutagenesis, truncated mutant S270A is an inactive variant of the truncated mutant DELTAWT where the catalytic serine is replaced with an alanine. The inactive truncated variant S270A is destabilized by ca 3°C compared to variants with an intact catalytic triad, implying that some stabilizing interactions have been lost, but the overall conclusion is that CuGE is a highly stable enzyme with Ti's in the range of 72.2-75.8°C for all variants. Binding between truncated S270A and the 4-O-methyl-glucuronoyl moiety alone has about 10times higher dissociation constant compared to binding of aldotetrauronic acid (Um4XX-OH)
H408A
-
site-directed mutagenesis of the catalytic His reduces kcat by 1700fold
L269Y
-
site-directed mutagenesis, the mutant shows altered kinetics and substrate specificity compared to wild-type
S267A
-
site-directed mutagenesis of the catalytic Ser reduces kcat by 17000fold, the S267A variant of OtCE15A is dramatically crippled
E374A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
F174A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
F174D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
S281A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
S304E
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
S304E/E374A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
W376A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
W376D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
E374A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
F174A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
F174D
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
S281A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
W376A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
E374A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
F174A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
F174D
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
S281A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
W376A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
S213A
S217A
site-directed mutagenesis, mutation of thee catalytic serine, inactive mutant
S213A
S217A
-
site-directed mutagenesis, mutation of thee catalytic serine, inactive mutant
-
S213A
S217A
Thermothelomyces thermophilus BCRC 31852
-
site-directed mutagenesis, mutation of thee catalytic serine, inactive mutant
-
S213A
S217A
Thermothelomyces thermophilus DSM 1799
-
site-directed mutagenesis, mutation of thee catalytic serine, inactive mutant
-
additional information
S213A
mutation in putative catalytic triad residue, crystallization data
S213A
site-directed mutagenesis, the S213A mutant exhibits a complete loss of enzyme activity towards methyl 4-O-methyl-D-glucopyranuronate, inactive mutant
S213A
-
mutation in putative catalytic triad residue, crystallization data
-
S213A
-
site-directed mutagenesis, the S213A mutant exhibits a complete loss of enzyme activity towards methyl 4-O-methyl-D-glucopyranuronate, inactive mutant
-
S213A
Thermothelomyces thermophilus DSM 1799
-
mutation in putative catalytic triad residue, crystallization data
-
S213A
Thermothelomyces thermophilus DSM 1799
-
site-directed mutagenesis, the S213A mutant exhibits a complete loss of enzyme activity towards methyl 4-O-methyl-D-glucopyranuronate, inactive mutant
-
additional information
construction of a truncated mutant (DELTAWT), comprising residues 78-458 (corresponding to the catalytic domain only) and lacking the carbohydrate-binding domain (CBM1). Neither the truncation nor the deglycosylation affects protein stability significantly
additional information
-
construction of a truncated mutant (DELTAWT), comprising residues 78-458 (corresponding to the catalytic domain only) and lacking the carbohydrate-binding domain (CBM1). Neither the truncation nor the deglycosylation affects protein stability significantly
additional information
-
kinetic characterization of catalytic residue substitutions, structure, ligand interactions, and catalytic mechanism of catalytic OtCE15A variants in complex with GlcA and benzyl glucuronoate, overview
additional information
recombinant expression of enzyme PcGE in Arabidopsis thaliana strain Col-0 results in 3 transgenic lines (PcGCE6, PcGCE7, and PcGCE13) consistently displaying a leaf-yellowing phenotype, as well as reduced glucose and xylose content by as much as 30% and 35%, respectively. Histological analysis reveals 50% reduction in cell wall thickness in the interfascicular fibres of transgenic plants, and FT-IR microspectroscopy of interfascicular fibre walls indicates reduction in lignin cross-linking in plants overexpressing PcGCE. These characteristics can be correlated with improved xylose recovery in transgenic plants, up to 15%. The promotion of glucuronoyl esterase activity in plants can alter the extent of intermolecular cross-linking within plant cell walls. Phenotype, detailed overview
additional information
-
recombinant expression of enzyme PcGE in Arabidopsis thaliana strain Col-0 results in 3 transgenic lines (PcGCE6, PcGCE7, and PcGCE13) consistently displaying a leaf-yellowing phenotype, as well as reduced glucose and xylose content by as much as 30% and 35%, respectively. Histological analysis reveals 50% reduction in cell wall thickness in the interfascicular fibres of transgenic plants, and FT-IR microspectroscopy of interfascicular fibre walls indicates reduction in lignin cross-linking in plants overexpressing PcGCE. These characteristics can be correlated with improved xylose recovery in transgenic plants, up to 15%. The promotion of glucuronoyl esterase activity in plants can alter the extent of intermolecular cross-linking within plant cell walls. Phenotype, detailed overview
additional information
-
recombinant expression of enzyme PcGE in Arabidopsis thaliana strain Col-0 results in 3 transgenic lines (PcGCE6, PcGCE7, and PcGCE13) consistently displaying a leaf-yellowing phenotype, as well as reduced glucose and xylose content by as much as 30% and 35%, respectively. Histological analysis reveals 50% reduction in cell wall thickness in the interfascicular fibres of transgenic plants, and FT-IR microspectroscopy of interfascicular fibre walls indicates reduction in lignin cross-linking in plants overexpressing PcGCE. These characteristics can be correlated with improved xylose recovery in transgenic plants, up to 15%. The promotion of glucuronoyl esterase activity in plants can alter the extent of intermolecular cross-linking within plant cell walls. Phenotype, detailed overview
-
additional information
use of a constitutive PGAP-Pichia pastoris (glyceraldehyde-3-phosphate dehydrogenase promoter) expression system to produce Hypocrea jecorina glucuronoyl esterase (GE) at bioreactor scale: glycerol fed-batch fermentation kinetics of the recombinant enzyme, enzymatic yields, kinetics and productivity for bioreactor cultivations of recombinant Pichia pastoris at the end of the glycerol fed-batch stage, and comparisons to previous expression attempts, method evaluation, overview
additional information
-
use of a constitutive PGAP-Pichia pastoris (glyceraldehyde-3-phosphate dehydrogenase promoter) expression system to produce Hypocrea jecorina glucuronoyl esterase (GE) at bioreactor scale: glycerol fed-batch fermentation kinetics of the recombinant enzyme, enzymatic yields, kinetics and productivity for bioreactor cultivations of recombinant Pichia pastoris at the end of the glycerol fed-batch stage, and comparisons to previous expression attempts, method evaluation, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
3 - 9
purified recombinant enzyme, 30°C, 30 min, over 40% of maximal activity remaining within this range, 80% at pH 5.0
749697
4 - 10
4 - 7
purified recombinant enzyme NcGE is stable in the relatively broad pH range of pH 4.0-7.0
751237
5 - 11
purified recombinant His6-tagged enzyme, 4°C, 1 week, over 80% activity remaining
749690
3 - 10
purified isozyme TtGE1 is relatively stable at pH between 4.0 and 6.0, with approximately 60-80% activity remaining. The enzyme is almost inactivated after incubation for12 h at a range of pH 9-10, profile overview
760415
3 - 10
purified isozyme TtGE2 retains 60-80% of its initial activity after preincubation at pH 3.0-6.0 for 12 h, but the residue activity decreases rapidly when treated with alkaline buffers at pH 7.0-10.0
760415
4
30°C, 30 min, activity is significantly lost after pre-incubation in pHs lower than 4
749697
4 - 10
recombinant purified esterase displays broad pH range stability between 4-10
741731
8
30°C, 30 min, activity is significantly lost after pre-incubation in pHs higher than 8
749697
8
-
purified esterase, 6 h, 50°C, over 90% activity remaining at pH 8.0, 40% activity at pH 5.0 and pH 10.0, 20% at pH 11.0, and 10% at pH 4.0, inactivation after 6 h at pH 3.0
761097
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
purified recombinant His6-tagged enzyme, pH 6.0, 6 h, loss of 20% activity
30 - 50
30 - 70
purified recombinant enzyme NcGE is stable at 30°C, but it completely loses its activity when preincubated at 70°C for 30 min
35 - 55
purified isozyme TtGE1 exhibits high stability at 35°C and 45°C, and over 90% of the initial activity is retained after 100 min of incubation residual activity of about 60% is retained after incubation at 55°C for 12 h
40
45 - 55
-
purified esterase, 50% activity is retained after 430 and 286 min at 50°C and 55°C, and over 90% of maximal activity at 45°C after 6 h, inactivation after 6 h at 60°C
45 - 65
purified isozyme TtGE2 is completely stable at 45°C and 55°C for 100 min, more than 70% of the initial activity is retained after 100 min of incubation at 65°C
50
52 - 54
differential scanning fluorimetry confirms similar melting temperatures (Tm) for the Phe174 variant as 52-54°C, and for the wild-type enzyme as 52°C
55 - 60
recombinant purified enzyme, pH 7.0, 55°C for 24 h, loss of 53% activity, inactivation above 60°C, half-lives are 22.5 h and 0.5 h at 55°C and 60°C, respectively
60
70
30 - 50
purified recombinant enzyme, pH 7.0, 30 min, completely stable at
40
purified recombinant His6-tagged enzyme, pH 6.0, stable up to for 6 h
50
purified recombinant His6-tagged enzyme, pH 6.0, 6 h, loss of 20% activity
50
purified recombinant His6-tagged enzyme, pH 6.0, 6 h, loss of 20% activity
50
recombinant purified enzyme, pH 7.0, stable up to for 24 h
50
purified recombinant His6-tagged enzyme, pH 6.0, 6 h, loss of 70% activity
60
purified recombinant His6-tagged enzyme, pH 6.0, 6 h, inactivation
60
purified recombinant His6-tagged enzyme, pH 6.0, 6 h, inactivation
70
purified recombinant enzyme, pH 7.0, 30 min, loss of 60% activity
70
purified recombinant His6-tagged enzyme, pH 6.0, 6 h, inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme PeGE exhibits high tolerance toward several denaturing agents
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 110.5fold from Schizophyllum commune strain ATCC 38548 cell culture medium by anion exchange chromatography, desalting gel filtration, and two steps of hydrophobic interaction chromatography
-
native extracellular enzyme 74fold from culture broth, by ultrafiltration, two different steps of anion exchange chromatography, again ultrafiltration, and two different steps of gel filtration, followed by hydrophobic interaction chromatography
-
recombinant c-myc-/His-tagged enzyme from Pichia pastoris strain GS115 by nickel affinity chromatography to over 95% homogeneity
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Pichia pastoris strain X-33 by nickel affinity chromatography
recombinant enzyme
recombinant enzyme Cip2 from overexpressing Hypocrea jecorina strain Rut C-30 to homogeneity by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography
recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, dialysis, immobilized metal-ion affinity chromatography, and again ultrafiltration and dialysis
recombinant enzyme partially from Pichia pastoris strain SMD1168H by ultrafiltration
recombinant extracellular c-myc/His6-tagged NcGE from Pichia pastoris, cell culture supernatant by nickel affinity and anion exchange chromatography
recombinant His-tagged enzyme CuGE from Pichia pastoris by nickel affinity chromatography and ultrafiltration
recombinant His-tagged enzyme from Pichia pastoris by nickel affinity chromatography
recombinant His-tagged enzyme from Pichia pastoris by nickel affinity chromatography and gel filtration
recombinant His-tagged TtGE1 isozyme from Pichia pastoris strain GS115 by dialysis and nickel affinity chromatography
recombinant His-tagged TtGE2 isozyme from Pichia pastoris strain GS115 by dialysis and nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Pichia pastoris by nickel affinity chromatography
recombinant His6-tagged enzyme from Pichia pastoris by nickel affinity chromatography to homogeneity
recombinant His6-tagged enzyme from Pichia pastoris strain SMD1168H by nickel affinity and anion exchange chromatography
recombinant His6-tagged enzyme from Pichia pastoris strain SMD1168H by nickel affinity chromatography
recombinant His6-tagged His6-tagged full-length enzyme and catalytic domain (residues 108-429) of enzyme PeGE from Pichia pastoris strain X-33 by ultrafiltration, nickel affinity chromatography, and again ultrafiltration
recombinant His6-tagged His6-tagged full-length enzyme and catalytic domain (residues 25-352) of enzyme CsGE from Pichia pastoris strain X-33 by ultrafiltration, nickel affinity chromatography, and again ultrafiltration
recombinant His6-tagged isozymes from Pichia pastoris strain SMD1168H by nickel affinity chromatography
-
recombinant Myc-His-tagged enzyme AfGE from Aspergillus oryzae strain RIB40 by nickel affinity chromatography, and anion exchange chromatography
recombinant His-tagged enzyme from Pichia pastoris by nickel affinity chromatography
recombinant His-tagged enzyme from Pichia pastoris by nickel affinity chromatography
recombinant His-tagged enzyme from Pichia pastoris by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Pichia pastoris by nickel affinity chromatography and gel filtration
recombinant His6-tagged enzyme from Pichia pastoris by nickel affinity chromatography to homogeneity
recombinant His6-tagged enzyme from Pichia pastoris by nickel affinity chromatography to homogeneity
recombinant His6-tagged enzyme from Pichia pastoris strain SMD1168H by nickel affinity chromatography
recombinant His6-tagged enzyme from Pichia pastoris strain SMD1168H by nickel affinity chromatography
recombinant His6-tagged enzyme from Pichia pastoris strain SMD1168H by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally c-myc and hexahistidine-tagged enzyme is heterologously expressed in the methylotrophic yeast Pichia pastoris
CE15 phylogenetic analysis and tree, overview
CE15 phylogenetic analysis and tree, overview. Quantitative reverse transcription PCR (RT-qPCR) enzyme expression analysis relative to the RNA polymerase sigma factor rpoD
-
cloned into the expression vector pDAU109 and recombinantly expressed in the host Aspergillus oryzae MT3568
DNA and amino acid sequence determination and analysis, peptide pattern recognition (PPR) analysis, phylogenetic analysis
expression in Pichia pastoris
gene Afu6g14390, recombinant expression of Myc-His-tagged enzyme AfGE in Aspergillus oryzae strain RIB40 from vector pUNA-AfGE-Myc-His under the control of a strong promoter of alpha-amylase (amyB), subcloning of the enzyme in Escherichia coli strain DH5alpha and of the vector in Aspergillus oryzae strain niaD300, the recombinant enzyme is secreted into the medium. Recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain KM71H
gene cesA, recombinant expression of the C-terminal domain of a multidomain protein CesA in Escherichia coli strain BL21(DE3)
gene cip2, DNA and amino acid sequence determination and analysis, sequence comparison with Cip2 from Hypocrea jecorina (UniProt ID G0RV93), recombinant expression of C-terminally c-myc- and His6-tagged NcGE from shuttle vector pPICZalphaA in the methylotrophic yeast Pichia pastoris strain KM71H, the enzyme is secreted, enzyme subcloning in Escherichia coli strain DH5alpha
gene cip2, recombinant expression of the isolated C-terminal domain (corresponding to amino acids 90-460) in Hypocrea jecorina cells, the protein is secreted into culture medium
gene cip2, sequence and domain comparisons, functional recombinant overexpression of enzyme Cip2 under cellulase-induction conditions in Hypocrea jecorina strain Rut C-30 using the cel7A promoter, the cel5A signal peptide and carbohydrate-binding module (CBM)-coding region, and the Escherichia coli hygromycin B phosphotransferase gene. The recombinant enzyme is secreted
gene cip2, the enzyme is homologously overexpressed using a cellobiohydrolase promoter and secreted to the growth medium
gene csge, functional recombinant expression of His6-tagged full-length enzyme and catalytic domain (residues 25-352) of enzyme CsGE in Pichia pastoris strain X-33, the recombinant enzyme is secreted to the culture medium
gene ge1 or e_gwh2.18.77.1, sequence analysis of the promoter region of gene ge1 reveals several putative regulatory sites, a TATA box is located -62 bp and a CCAAT-box -72 bp, upstream of ge1 translation initial site, sequence comparisons and phylogenetic analysis, functional recombinant heterologous expression of the extracellular glucuronoyl esterase in Aspergillus niger, Aspergillus vadensis strain NW282 (under control of the glucoamylase glaA promoter), Pycnoporus cinnabarinus strain BMR44 (under control of the GPD promoter), and Schizophyllum commune strain 4.8B (under control of the SC3 promoter), the enzyme expressed in Schizophyllum commune is secreted to the culture medium, the enzyme expressed in Aspergillus niger is inactive
gene ge2 or fgenesh1_pg.C_scaffold_11000167, sequence analysis of the promoter region of gene ge2 reveals several putative regulatory sites, the ge2 promoter contains a TATA box at position -62, sequence comparisons and phylogenetic analysis, functional recombinant heterologous expression of the extracellular glucuronoyl esterase in Schizophyllum commune strain 4.8B, the enzyme is secreted to the culture medium
gene ge2, DNA and amino acid sequence determination and analysis, sequence comparisons, gene ge2 from the genomic DNA is successfully cloned in frame with the sequence for the Saccharomyces cerevisiae alpha-factor secretion signal under the transcriptional control of alcohol oxidase (AOX1) promoter and integrated in Pichia pastoris strain X-33
gene ge2, functional recombinant expression of C-terminally His6-tagged enzyme in Pichia pastoris strain X-33 under transcriptional control of alcohol oxidase (AOX1) promoter
gene ge2, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Pichia pastoris
gene page1, functional recombinant expression of C-terminally His6-tagged enzyme in Pichia pastoris strain X-33 under transcriptional control of alcohol oxidase (AOX1) promoter
gene pege, functional recombinant expression of His6-tagged His6-tagged full-length enzyme and catalytic domain (residues 108-429) of enzyme PeGE in Pichia pastoris strain X-33, recombinant enzyme is secreted to the culture medium
gene THITE_2055580, phylogenetic tree, recombinant expression of His-tagged TtGE2 isozyme in Pichia pastoris strain GS115, subcloning in Escherichia coli strain DH5alpha
gene THITE_2117593, phylogenetic tree, recombinant expression of His-tagged TtGE1 isozyme in Pichia pastoris strain GS115, subcloning in Escherichia coli strain DH5alpha
heterologous expression in Pichia pastoris SMD1168H
heterologously expressed in Aspergillus oryzae RIB40 strain (ATCC42149) under the control of a strong promoter of alpha-amylase (amyB)
overexpression of a glucuronoyl esterase from Phanerochaete carnosa, PcGCE, in hybrid aspen (Populus tremula L. x tremuloides Michx.) on the wood composition and the saccharification efficiency. The recombinant enzyme, which is targeted to the plant cell wall using the signal peptide from hybrid aspen cellulase PttCel9B3, is constitutively expressed resulting in the appearance of glucuronoyl esterase activity in protein extracts from developing wood. Whereas PcGCE expression in hybrid aspen increases lignin deposition, the inhibitory effects of lignin are efficiently removed during acid pretreatment, and the extent of wood cellulose conversion during hydrolysis after acid pretreatment is improved in the transgenic lines possible due to reduced cell wall cross-links between cell wall biopolymers by PcGCE
phylogenetic analysis, recombinant expression of His-tagged enzyme in protease-deficient Pichia pastoris strain SMD1168H, subcloning in Escherichia coli strain DH5alpha
phylogenetic analysis, recombinant expression of His-tagged isozymes in protease-deficient Pichia pastoris strain SMD1168H, subcloning in Escherichia coli strain DH5alpha
-
phylogenetic analysis, recombinant expression of His6-tagged enzyme in protease-deficient Pichia pastoris strain SMD1168H, subcloning in Escherichia coli strain DH5alpha
recombinant expression in Pichia pastoris strain DSMZ 70382 (CBS704), the recombinant enzyme is secreted
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Pichia pastoris strain X-33
recombinant expression of enzyme PcGE in Arabidopsis thaliana strain Col-0 under control of constitutive cauliflower mosaic virus 35S promoter, semiquantitative RT-PCR enzyme expression analysis, recombinant expression of c-myc-/His-tagged enzyme in Pichia pastoris strain GS115
recombinant expression of His-tagged enzyme CuGE in Pichia pastoris
recombinant expression of His-tagged enzyme from codon-optimized gene in Pichia pastoris
recombinant expression of His-tagged wild-type and mutant enzymes
recombinant expression of the enzyme in Pichia pastoris strain SMD1168H
cloned into the expression vector pDAU109 and recombinantly expressed in the host Aspergillus oryzae MT3568
cloned into the expression vector pDAU109 and recombinantly expressed in the host Aspergillus oryzae MT3568
cloned into the expression vector pDAU109 and recombinantly expressed in the host Aspergillus oryzae MT3568
DNA and amino acid sequence determination and analysis, peptide pattern recognition (PPR) analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, peptide pattern recognition (PPR) analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, peptide pattern recognition (PPR) analysis, phylogenetic analysis
phylogenetic analysis, recombinant expression of His-tagged enzyme in protease-deficient Pichia pastoris strain SMD1168H, subcloning in Escherichia coli strain DH5alpha
phylogenetic analysis, recombinant expression of His-tagged enzyme in protease-deficient Pichia pastoris strain SMD1168H, subcloning in Escherichia coli strain DH5alpha
phylogenetic analysis, recombinant expression of His-tagged enzyme in protease-deficient Pichia pastoris strain SMD1168H, subcloning in Escherichia coli strain DH5alpha
recombinant expression of His-tagged enzyme from codon-optimized gene in Pichia pastoris
recombinant expression of His-tagged enzyme from codon-optimized gene in Pichia pastoris
recombinant expression of His-tagged enzyme from codon-optimized gene in Pichia pastoris
recombinant expression of His-tagged enzyme from codon-optimized gene in Pichia pastoris
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
the cip2 gene of Hypocrea jecorina is upregulated under conditions of induction of cellulolytic and hemicellulolytic enzymes
the expressions of the SlCE15A-, B-, and C-encoding genes are thus apparently regulated by different biological cues. Grown on glucose, xylose, corn cob xylan, and milled corn cob biomass. Gene slce15b is constitutively expressed in all growth conditions, expression of slce15a is similar for glucose, xylose, and xylan, but increases twofold on milled corn cob, and slce15c shows a three to fourfold increase in response to any xylose-containing carbon source compared to glucose
-
up-regulated under conditions of induction of cellulolytic and hemicellulolytic enzymes
expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
Phanerodontia chrysosporium ATCC MYA-4764
-
-
expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
Phanerodontia chrysosporium FGSC 9002
-
-
expression of genes encoding GE1 and GE2 isozymes appears to be mediated by different forms of regulatory control
-
-
the cip2 gene of Hypocrea jecorina is upregulated under conditions of induction of cellulolytic and hemicellulolytic enzymes
the cip2 gene of Hypocrea jecorina is upregulated under conditions of induction of cellulolytic and hemicellulolytic enzymes
-
-
up-regulated under conditions of induction of cellulolytic and hemicellulolytic enzymes
up-regulated under conditions of induction of cellulolytic and hemicellulolytic enzymes
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
biotechnology
degradation
industry
molecular biology
synthesis
additional information
biofuel production
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
biofuel production
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
biofuel production
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
biofuel production
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
biofuel production
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
biofuel production
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
biofuel production
decomposition of wood polymers in biorefinery processes
biofuel production
efficient and complete enzymatic degradation is an essential prerequisite in the utilization of lignocellulosic material for production of energy and value-added biorefinery products. Glucuronoyl esterase CE15 is a candidate for polishing lignin for residual carbohydrates to achieve pure, native lignin fractions after minimal pretreatment
biofuel production
inclusion of glucuronoyl-esterases in the enzymatic digestion of lignocellulosic biomass
biofuel production
inclusion of glucuronoyl-esterases in the enzymatic digestion of lignocellulosic biomass
biofuel production
inclusion of glucuronoyl-esterases in the enzymatic digestion of lignocellulosic biomass
biofuel production
the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass
biofuel production
the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass
biofuel production
the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass
biofuel production
glucuronoyl esterase (GE) has potential for production of biofuels and biomaterials in lignocellulose biorefineries. GE cleaves alkali-labile bonds from the lignincarbohydrate complexes at acidic pH. Removal of glucuronic acid branches from the hemicellulose significantly improved release of fermentable sugars for biofuels production
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
Phanerodontia chrysosporium ATCC MYA-4764
-
the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass
-
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
Phanerodontia chrysosporium FGSC 9002
-
the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass
-
biofuel production
-
the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass
-
biofuel production
Thermothelomyces thermophilus BCRC 31852
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
-
inclusion of glucuronoyl-esterases in the enzymatic digestion of lignocellulosic biomass
-
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
-
glucuronoyl esterase (GE) has potential for production of biofuels and biomaterials in lignocellulose biorefineries. GE cleaves alkali-labile bonds from the lignincarbohydrate complexes at acidic pH. Removal of glucuronic acid branches from the hemicellulose significantly improved release of fermentable sugars for biofuels production
-
biofuel production
Thermothelomyces thermophilus DSM 1799
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biofuel production
-
the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass
-
biofuel production
-
broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials
-
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
biotechnology
glucuronoyl esterases are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid in plant cell walls. This activity renders glucuronoyl esterases attractive research targets for biotechnological applications. One of the factors impeding the progress in glucuronoyl esterases research is the lack of suitable substrates. A facile preparation is described of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl beta-D-glucuronides for qualitative and quantitative glucuronoyl esterase assay coupled with beta-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of glucuronoyl esterase in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries
biotechnology
glucuronoyl esterases are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid in plant cell walls. This activity renders glucuronoyl esterases attractive research targets for biotechnological applications. One of the factors impeding the progress in glucuronoyl esterases research is the lack of suitable substrates. A facile preparation is described of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl beta-D-glucuronides for qualitative and quantitative glucuronoyl esterase assay coupled with beta-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of glucuronoyl esterase in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries
biotechnology
glucuronoyl esterases are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid in plant cell walls. This activity renders glucuronoyl esterases attractive research targets for biotechnological applications. One of the factors impeding the progress in glucuronoyl esterases research is the lack of suitable substrates. A facile preparation is described of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl beta-D-glucuronides for qualitative and quantitative glucuronoyl esterase assay coupled with beta-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of glucuronoyl esterase in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
Phanerodontia chrysosporium ATCC MYA-4764
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
Phanerodontia chrysosporium FGSC 9002
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
Thermothelomyces thermophilus BCRC 31852
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid in plant cell walls. This activity renders glucuronoyl esterases attractive research targets for biotechnological applications. One of the factors impeding the progress in glucuronoyl esterases research is the lack of suitable substrates. A facile preparation is described of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl beta-D-glucuronides for qualitative and quantitative glucuronoyl esterase assay coupled with beta-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of glucuronoyl esterase in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are microbial enzymes with potential to cleave the ester bonds between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid in plant cell walls. This activity renders glucuronoyl esterases attractive research targets for biotechnological applications. One of the factors impeding the progress in glucuronoyl esterases research is the lack of suitable substrates. A facile preparation is described of methyl esters of chromogenic 4-nitrophenyl and 5-bromo-4-chloro-3-indolyl beta-D-glucuronides for qualitative and quantitative glucuronoyl esterase assay coupled with beta-glucuronidase as the auxiliary enzyme. The indolyl derivative affording a blue indigo-type product is suitable for rapid and sensitive assay of glucuronoyl esterase in commercial preparations as well as for high throughput screening of microorganisms and genomic and metagenomic libraries
-
biotechnology
Thermothelomyces thermophilus DSM 1799
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
biotechnology
-
glucuronoyl esterases are interesting candidates for biotechnological applications in plant biomass processing and genetic modification of plants
-
degradation
fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization
degradation
fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization
degradation
Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources
degradation
-
Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources
-
degradation
-
Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources
-
industry
the enzyme is a potentially industrially applicable enzyme due to its characteristic as a thermophilic enzyme with the favorable temperature of 40-50°C at pH 5
industry
-
the enzyme is a potentially industrially applicable enzyme due to its characteristic as a thermophilic enzyme with the favorable temperature of 40-50°C at pH 5
-
molecular biology
the enzyme may prove a valuable as research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
molecular biology
the enzyme may prove a valuable as research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
molecular biology
the enzyme may prove a valuable research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
molecular biology
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
molecular biology
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
molecular biology
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
molecular biology
-
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
-
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
-
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
-
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
Thermothelomyces thermophilus BCRC 31852
-
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
-
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
-
the enzyme may prove a valuable as research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
-
the enzyme may prove a valuable as research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
Thermothelomyces thermophilus DSM 1799
-
the enzyme may prove valuable as a research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
molecular biology
-
the enzyme may prove a valuable research tool for the investigation of lignin and lignin to carbohydrates-bond chemistry
-
synthesis
-
due to its thermostability, enzyme CkXyn10C-GE15A is a promising candidate for industrial processes, with both catalytic domains exhibiting melting temperatures over 70°C. Of particular interest is the glucuronoyl esterase domain, as it represents the first studied thermostable enzyme displaying this activity
synthesis
Thermothielavioides terrestris glucoronoyl esterases TtGEs can be used as promising accessory enzymes to improve the hydrolysis efficiency of commercial enzymes in saccharification of lignocellulosic materials due to their thermophilic characteristics
synthesis
-
Thermothielavioides terrestris glucoronoyl esterases TtGEs can be used as promising accessory enzymes to improve the hydrolysis efficiency of commercial enzymes in saccharification of lignocellulosic materials due to their thermophilic characteristics
-
synthesis
-
Thermothielavioides terrestris glucoronoyl esterases TtGEs can be used as promising accessory enzymes to improve the hydrolysis efficiency of commercial enzymes in saccharification of lignocellulosic materials due to their thermophilic characteristics
-
additional information
fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization
additional information
fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization
additional information
glucuronoyl esterases are highly important enzymes for industrial applications that aim for selective lignin recovery in order to obtain a final high-quality lignin product from hardwood
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Charavgi, M.D.; Dimarogona, M.; Topakas, E.; Christakopoulos, P.; Chrysina, E.D.
The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst
Acta Crystallogr. Sect. D
69
63-73
2013
Thermothelomyces thermophilus (G2QJR6), Thermothelomyces thermophilus, Thermothelomyces thermophilus ATCC 42464 (G2QJR6), Thermothelomyces thermophilus DSM 1799 (G2QJR6)
brenda
Topakas, E.; Moukouli, M.; Dimarogona, M.; Vafiadi, C.; Christakopoulos, P.
Functional expression of a thermophilic glucuronyl esterase from Sporotrichum thermophile identification of the nucleophilic serine
Appl. Microbiol. Biotechnol.
87
1765-1772
2010
Thermothelomyces thermophilus (G2QJR6), Thermothelomyces thermophilus, Thermothelomyces thermophilus ATCC 42464 (G2QJR6), Thermothelomyces thermophilus BCRC 31852 (G2QJR6), Thermothelomyces thermophilus DSM 1799 (G2QJR6)
brenda
Katsimpouras, C.; Benarouche, A.; Navarro, D.; Karpusas, M.; Dimarogona, M.; Berrin, J.G.; Christakopoulos, P.; Topakas, E.
Enzymatic synthesis of model substrates recognized by glucuronoyl esterases from Podospora anserina and Myceliophthora thermophila
Appl. Microbiol. Biotechnol.
98
5507-5516
2014
Podospora anserina (B2ABS0), Podospora anserina, Thermothelomyces thermophilus (G2QJR6), Thermothelomyces thermophilus, Thermothelomyces thermophilus ATCC 42464 (G2QJR6), Podospora anserina ATCC MYA-4624 (B2ABS0), Podospora anserina DSM 980 (B2ABS0), Podospora anserina FGSC 10383 (B2ABS0), Thermothelomyces thermophilus BCRC 31852 (G2QJR6), Podospora anserina S (B2ABS0), Thermothelomyces thermophilus DSM 1799 (G2QJR6)
brenda
Li, X.L.; Spanikova, S.; de Vries, R.P.; Biely, P.
Identification of genes encoding microbial glucuronoyl esterases
FEBS Lett.
581
4029-4035
2007
Trichoderma reesei (G0RV93), Trichoderma reesei, Trichoderma reesei QM6a (G0RV93)
brenda
Franova, L.; Puchart, V.; Biely, P.
beta-Glucuronidase-coupled assays of glucuronoyl esterases
Anal. Biochem.
510
114-119
2016
Schizophyllum commune (D8QLP9), Trichoderma reesei (G0RV93), Ruminococcus flavefaciens (Q9RLB8), Schizophyllum commune H4-8 (D8QLP9), Trichoderma reesei QM6a (G0RV93)
brenda
Biely, P.
Microbial glucuronoyl esterases 10 years after discovery
Appl. Environ. Microbiol.
82
7014-7018
2016
Sodiomyces alcalophilus (A0A1D8EJG8), Podospora anserina (B2ABS0), Teredinibacter turnerae (C5BN23), Schizophyllum commune (D8QLP9), Schizophyllum commune, Trichoderma reesei (G0RV93), Thermothelomyces thermophilus (G2QJR6), Phanerochaete carnosa (K5XDZ6), Phanerodontia chrysosporium (P0CT87), Phanerodontia chrysosporium (P0CT88), Ruminococcus flavefaciens (Q9RLB8), Thermothelomyces thermophilus ATCC 42464 (G2QJR6), Podospora anserina ATCC MYA-4624 (B2ABS0), Podospora anserina DSM 980 (B2ABS0), Phanerodontia chrysosporium ATCC MYA-4764 (P0CT87), Phanerodontia chrysosporium ATCC MYA-4764 (P0CT88), Phanerodontia chrysosporium FGSC 9002 (P0CT87), Phanerodontia chrysosporium FGSC 9002 (P0CT88), Thermothelomyces thermophilus BCRC 31852 (G2QJR6), Podospora anserina S (B2ABS0), Schizophyllum commune H4-8 (D8QLP9), Teredinibacter turnerae ATCC 39867 (C5BN23), Trichoderma reesei QM6a (G0RV93), Thermothelomyces thermophilus DSM 1799 (G2QJR6), Schizophyllum commune FGSC 9210 (D8QLP9), Teredinibacter turnerae T7901 (C5BN23), Phanerochaete carnosa HHB-10118-sp (K5XDZ6), Phanerodontia chrysosporium RP-78 (P0CT87), Phanerodontia chrysosporium RP-78 (P0CT88)
brenda
Httner, S.; Klaubauf, S.; de Vries, R.; Olsson, L.
Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds
Appl. Microbiol. Biotechnol.
101
5301-5311
2017
Lentithecium fluviatile, Sodiomyces alcalophilus (A0A1D8EJG8), Sodiomyces alcalophilus, Schizophyllum commune (D8QLP9), Phanerodontia chrysosporium (P0CT87), Phanerodontia chrysosporium, Wolfiporia cocos (P0CU53), Wolfiporia cocos, Phanerodontia chrysosporium ATCC MYA-4764 (P0CT87), Phanerodontia chrysosporium FGSC 9002 (P0CT87), Wolfiporia cocos MD-104 (P0CU53), Schizophyllum commune H4-8 (D8QLP9), Phanerodontia chrysosporium RP-78 (P0CT87)
brenda
Huynh, H.; Ishii, N.; Matsuo, I.; Arioka, M.
A novel glucuronoyl esterase from Aspergillus fumigatus - the role of conserved Lys residue in the preference for 4-O-methyl glucuronoyl esters
Appl. Microbiol. Biotechnol.
102
2191-2201
2018
Aspergillus fumigatus (Q4WL89), Aspergillus fumigatus, Aspergillus fumigatus ATCC MYA-4609 (Q4WL89)
brenda
Lin, M.; Hiyama, A.; Kondo, K.; Nagata, T.; Katahira, M.
Classification of fungal glucuronoyl esterases (FGEs) and characterization of two new FGEs from Ceriporiopsis subvermispora and Pleurotus eryngii
Appl. Microbiol. Biotechnol.
102
9635-9645
2018
Gelatoporia subvermispora (A0A386GY48), Pleurotus eryngii (A0A386GY52)
brenda
Mosbech, C.; Holck, J.; Meyer, A.; Agger, J.
The natural catalytic function of CuGE glucuronoyl esterase in hydrolysis of genuine lignin-carbohydrate complexes from birch
Biotechnol. Biofuels
11
71
2018
Cerrena unicolor (A0A0A7EQR3)
brenda
Arnling Baath, J.; Giummarella, N.; Klaubauf, S.; Lawoko, M.; Olsson, L.
A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin-carbohydrate ester bonds
FEBS Lett.
590
2611-2618
2016
Sodiomyces alcalophilus (A0A1D8EJG8), Sodiomyces alcalophilus
brenda
dErrico, C.; Brjesson, J.; Ding, H.; Krogh, K.; Spodsberg, N.; Madsen, R.; Monrad, R.
Improved biomass degradation using fungal glucuronoyl-esterases-hydrolysis of natural corn fiber substrate
J. Biotechnol.
219
117-123
2016
Cerrena unicolor (A0A0A7EQR3), Schizophyllum commune (D8QLP9), Trichoderma reesei (G0RV93), Schizophyllum commune H4-8 (D8QLP9)
brenda
Huynh, H.; Arioka, M.
Functional expression and characterization of a glucuronoyl esterase from the fungus Neurospora crassa Identification of novel consensus sequences containing the catalytic triad
J. Gen. Appl. Microbiol.
62
217-224
2016
Neurospora crassa (Q7S1X0), Neurospora crassa, Neurospora crassa 74-OR23-1A (Q7S1X0), Neurospora crassa ATCC 24698 (Q7S1X0), Neurospora crassa CBS 708.71 (Q7S1X0), Neurospora crassa DSM 1257 (Q7S1X0), Neurospora crassa FGSC 987 (Q7S1X0)
brenda
Sunner, H.; Charavgi, M.; Olsson, L.; Topakas, E.; Christakopoulos, P.
Glucuronoyl esterase screening and characterization assays utilizing commercially available benzyl glucuronic acid ester
Molecules
20
17807-17817
2015
Cerrena unicolor (A0A0A7EQR3), Podospora anserina (B2ABS0), Schizophyllum commune (D8QLP9), Trichoderma reesei (G0RV93), Thermothelomyces thermophilus (G2QJR6), Phanerodontia chrysosporium (P0CT87), Phanerodontia chrysosporium (P0CT88), Thermothelomyces thermophilus ATCC 42464 (G2QJR6), Podospora anserina ATCC MYA-4624 (B2ABS0), Podospora anserina DSM 980 (B2ABS0), Podospora anserina FGSC 10383 (B2ABS0), Thermothelomyces thermophilus BCRC 31852 (G2QJR6), Podospora anserina S (B2ABS0), Schizophyllum commune H4-8 (D8QLP9), Trichoderma reesei QM6a (G0RV93), Thermothelomyces thermophilus DSM 1799 (G2QJR6), Phanerodontia chrysosporium RP-78 (P0CT87)
brenda
Dilokpimol, A.; Mkel, M.; Cerullo, G.; Zhou, M.; Varriale, S.; Gidijala, L.; Bras, J.; Jtten, P.; Piechot, A.; Verhaert, R.; Faraco, V.; Hilden, K.; de Vries, R.
Fungal glucuronoyl esterases Genome mining based enzyme discovery and biochemical characterization
N. Biotechnol.
40
282-287
2018
Ascobolus immersus, Parastagonospora nodorum, Stereum hirsutum, Botryosphaeria dothidea, Apiospora arundinis, Hypholoma sublateritium (A0A0D2LPD9), Piromyces sp. E2 (A0A1Y3N892), Podospora anserina (B2ABS0), Podospora anserina (B2API8), Penicillium rubens (B6H3U7), Schizophyllum commune (D8QLP9), Leptosphaeria maculans (E4ZH04), Trichoderma reesei (G0RV93), Thermothelomyces thermophilus (G2QJR6), Serendipita indica (G4TU99), Phanerochaete carnosa (K5XDZ6), Dichomitus squalens (R7SXC9), Thermothelomyces thermophilus ATCC 42464 (G2QJR6), Dichomitus squalens LYAD-421 (R7SXC9), Hypholoma sublateritium FD-334 SS-4 (A0A0D2LPD9), Podospora anserina FGSC 10383 (B2ABS0), Podospora anserina FGSC 10383 (B2API8), Serendipita indica DSM 11827 (G4TU99), Schizophyllum commune H4-8 (D8QLP9), Trichoderma reesei QM6a (G0RV93), Penicillium rubens ATCC 28089 (B6H3U7), Phanerochaete carnosa HHB-10118-sp (K5XDZ6)
brenda
Gandla, M.; Derba-Maceluch, M.; Liu, X.; Gerber, L.; Master, E.; Mellerowicz, E.; Jnsson, L.
Expression of a fungal glucuronoyl esterase in populus Effects on wood properties and saccharification efficiency
Phytochemistry
112
210-220
2015
Phanerochaete carnosa (K5XDZ6), Phanerochaete carnosa, Phanerochaete carnosa HHB-10118-sp (K5XDZ6)
brenda
Wood, S.J.; Li, X.L.; Cotta, M.A.; Biely, P.; Duke, N.E.; Schiffer, M.; Pokkuluri, P.R.
Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina
Acta Crystallogr. Sect. F
64
255-257
2008
Trichoderma reesei (G0RV93), Trichoderma reesei
brenda
Tang, J.; Long, L.; Cao, Y.; Ding, S.
Expression and characterization of two glucuronoyl esterases from Thielavia terrestris and their application in enzymatic hydrolysis of corn bran
Appl. Microbiol. Biotechnol.
103
3037-3048
2019
Thermothielavioides terrestris (G2R8B5), Thermothielavioides terrestris (G2RCM8), Thermothielavioides terrestris, Thermothielavioides terrestris ATCC 38088 (G2R8B5), Thermothielavioides terrestris ATCC 38088 (G2RCM8), Thermothielavioides terrestris NRRL 8126 (G2R8B5), Thermothielavioides terrestris NRRL 8126 (G2RCM8)
brenda
Mosbech, C.; Holck, J.; Meyer, A.; Agger, J.
Enzyme kinetics of fungal glucuronoyl esterases on natural lignin-carbohydrate complexes
Appl. Microbiol. Biotechnol.
103
4065-4075
2019
Cerrena unicolor (A0A0A7EQR3), Punctularia strigosozonata (A0A4D6BQ82), Thermothielavioides terrestris (A0A4D6BS73), Armillaria fuscipes (A0A4D6BT21)
brenda
Spanikova, S.; Polakova, M.; Joniak, D.; Hirsch, J.; Biely, P.
Synthetic esters recognized by glucuronoyl esterase from Schizophyllum commune
Arch. Microbiol.
188
185-189
2007
Schizophyllum commune, Schizophyllum commune ATCC 38548
brenda
Duranova, M.; Spanikova, S.; Woesten, H.A.; Biely, P.; de Vries, R.P.
Two glucuronoyl esterases of Phanerochaete chrysosporium
Arch. Microbiol.
191
133-140
2009
Phanerodontia chrysosporium (P0CT87), Phanerodontia chrysosporium (P0CT88), Phanerodontia chrysosporium, Phanerodontia chrysosporium ATCC MYA-4764 (P0CT87), Phanerodontia chrysosporium ATCC MYA-4764 (P0CT88), Phanerodontia chrysosporium FGSC 9002 (P0CT87), Phanerodontia chrysosporium FGSC 9002 (P0CT88), Phanerodontia chrysosporium RP-78 (P0CT87), Phanerodontia chrysosporium RP-78 (P0CT88)
brenda
Arnling Baath, J.; Mazurkewich, S.; Knudsen, R.M.; Poulsen, J.N.; Olsson, L.; Lo Leggio, L.; Larsbrink, J.
Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion
Biotechnol. Biofuels
11
213
2018
Candidatus Solibacter usitatus, Opitutus terrae, Spirosoma linguale, Candidatus Solibacter usitatus Ellin6076
brenda
Krska, D.; Larsbrink, J.
Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme from Caldicellulosiruptor kristjanssonii incorporating multiple carbohydrate-binding modules
Biotechnol. Biofuels
13
68
2020
Caldicellulosiruptor acetigenus
brenda
Conacher, C.G.; Garcia-Aparicio, M.P.; Coetzee, G.; van Zyl, W.H.; Goergens, J.F.
Scalable methanol-free production of recombinant glucuronoyl esterase in Pichia pastoris
BMC Res. Notes
12
596
2019
Trichoderma reesei (G0RV93), Trichoderma reesei QM6a (G0RV93)
brenda
Spanikova, S.; Biely, P.
Glucuronoyl esterase - novel carbohydrate esterase produced by Schizophyllum commune
FEBS Lett.
580
4597-4601
2006
Schizophyllum commune, Schizophyllum commune ATCC 38548
brenda
Biely, P.; Malovikova, A.; Uhliarikova, I.; Li, X.L.; Wong, D.W.
Glucuronoyl esterases are active on the polymeric substrate methyl esterified glucuronoxylan
FEBS Lett.
589
2334-2339
2015
Schizophyllum commune (D8QLP9), Trichoderma reesei (G0RV93), Ruminococcus flavefaciens (Q9RLB8), Schizophyllum commune H4-8 (D8QLP9), Trichoderma reesei QM6a (G0RV93), Schizophyllum commune FGSC 9210 (D8QLP9)
brenda
Vafiadi, C.; Topakas, E.; Biely, P.; Christakopoulos, P.
Purification, characterization and mass spectrometric sequencing of a thermophilic glucuronoyl esterase from Sporotrichum thermophile
FEMS Microbiol. Lett.
296
178-184
2009
Thermothelomyces thermophilus, Thermothelomyces thermophilus ATCC 34628
brenda
Agger, J.W.; Busk, P.K.; Pilgaard, B.; Meyer, A.S.; Lange, L.
A new functional classification of glucuronoyl esterases by peptide pattern recognition
Front. Microbiol.
8
309
2017
Ganoderma lucidum, Armillaria fuscipes (A0A4D6BT21), Wolfiporia cocos (P0CU53), Wolfiporia cocos MD-104 (P0CU53)
brenda
Mazurkewich, S.; Poulsen, J.N.; Lo Leggio, L.; Larsbrink, J.
Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components
J. Biol. Chem.
294
19978-19987
2019
Opitutus terrae
brenda
Arnling Baath, J.; Mazurkewich, S.; Poulsen, J.N.; Olsson, L.; Lo Leggio, L.; Larsbrink, J.
Structure-function analyses reveal that a glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds
J. Biol. Chem.
294
6635-6644
2019
Teredinibacter turnerae (C5BN23), Teredinibacter turnerae, Teredinibacter turnerae ATCC 39867 (C5BN23), Teredinibacter turnerae T7901 (C5BN23)
brenda
Ernst, H.A.; Mosbech, C.; Langkilde, A.E.; Westh, P.; Meyer, A.S.; Agger, J.W.; Larsen, S.
The structural basis of fungal glucuronoyl esterase activity on natural substrates
Nat. Commun.
11
1026
2020
Cerrena unicolor (A0A0A7EQR3), Cerrena unicolor
brenda
Tsai, A.Y.; Canam, T.; Gorzsas, A.; Mellerowicz, E.J.; Campbell, M.M.; Master, E.R.
Constitutive expression of a fungal glucuronoyl esterase in Arabidopsis reveals altered cell wall composition and structure
Plant Biotechnol. J.
10
1077-1087
2012
Phanerochaete carnosa (K5XDZ6), Phanerochaete carnosa, Phanerochaete carnosa HHB-10118-sp (K5XDZ6)
brenda
Pokkuluri, P.R.; Duke, N.E.; Wood, S.J.; Cotta, M.A.; Li, X.L.; Biely, P.; Schiffer, M.
Structure of the catalytic domain of glucuronoyl esterase Cip2 from Hypocrea jecorina
Proteins
79
2588-2592
2011
Trichoderma reesei (G0RV93), Trichoderma reesei, Trichoderma reesei QM6a (G0RV93)
brenda
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