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Information on EC 2.3.1.304 - poly[(R)-3-hydroxyalkanoate] polymerase
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2.3.1.304 poly[(R)-3-hydroxyalkanoate] polymeraseIUBMB Comments
This is the key enzyme in the biosynthesis of polyhydroxyalkanoates (PHA), linear polyesters produced by bacteria as a means of carbon and energy storage . The enzyme catalyses the stereoselective, covalent linkage of (3R)-3-hydroxyacyl-CoA thioesters in a transesterification reaction with concomitant release of coenzyme A. The growing polymer is attached to a conserved active site L-cysteine residue. Three types of PHA synthases have been proposed based on their substrate specificity and enzyme structure. Type I and type III synthases preferentially polymerize short chain hydroxyalkanoate monomers containing 3-5 carbon atoms [1,2]. The difference between these two types is that type I synthases are composed of only a single subunit (PhaC), whereas type III synthases are composed of two different subunits, PhaC and PhaE [3,5]. Type II synthases are also composed of a single subunit (PhaC), but preferentially polymerize monomers containing more than 5 carbon atoms .
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Word Map
- 2.3.1.304
-
eutropha
-
ralstonia
-
copolymer
-
medium-chain-length
-
poly3-hydroxybutyrate
-
polyester
- acetoacetyl-coa
-
aeromonas
-
cupriavidus
-
necator
- beta-ketothiolase
-
depolymerase
- 3-hydroxyhexanoate
-
phasins
-
mcl-phas
- octanoate
-
homopolymer
-
copolyesters
-
caviae
- 3-hydroxyvalerate
- propionyl-coa
-
pha-producing
-
poly3-hydroxybutyrate-co-3-hydroxyhexanoate
-
short-chain-length
-
pha-negative
- enoyl-coa
- synthesis
- 3-hydroxyoctanoate
- 3-hydroxybutyryl-coa
-
poly3-hydroxyalkanoate
-
granule-associated
-
phaps
-
polylactic
-
bioplastic
-
vinosum
-
r-specific
-
poly3-hydroxybutyrate-co-3-hydroxyvalerate
-
thermoplastic
-
petroleum-based
-
acetoacetyl
-
acetoacetyl-coenzyme
-
propionicum
-
chromatium
- dodecanoate
-
phbhhx
-
mendocina
-
oleovorans
-
allochromatium
- 3-ketothiolase
-
r-3-hydroxybutyrate
-
3-hydroxydodecanoate
- biotechnology
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
poly[(R)-3-hydroxyalkanoate]n
=
+
poly[(R)-3-hydroxyalkanoate]n+1
Synonyms
pha synthase, phac1, phb synthase, phac2, polyhydroxyalkanoate (pha) synthase, polyhydroxyalkanoate synthase, pha polymerase, phacac, phacre, class i pha synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
class I PHA synthase
Class I PhaC
class I PHB synthase
Class I poly(R)-hydroxyalkanoic acid synthase
UniProt
class I polyhydroxyalkanoate synthase
class I polyhydroxybutyrate synthase
Class I synthase
Class II PHA polymerizing enzyme
class II PHA synthase
Class II PhaC
class III PHA synthase
class IV PHA synthase
HPTL0263
intracellular polyhydroxyalkanoate synthase
P(3HB) synthase
PHA synthase
PHA synthase 1
PHA synthase I
-
-
-
-
PHA synthase II
-
-
-
-
PHA synthase III
-
-
-
-
PhaC
PhaC type II
PhaC1
PhaC1P-5
PhaC2
PhaC2P-5
PhaC2Ps
PhaCAc
PhaCRe
PhaE
PhaEC
PhaRCBm
PhaRCYB4
PHB synthase
PhbC
phbE
poly-beta-hydroxybutyrate synthase
polyhydroxyalkanoate (PHA) synthase
polyhydroxyalkanoate synthase
polyhydroxyalkanoate synthase 1
polyhydroxyalkanoic synthase I
-
-
-
-
polyhydroxyalkanoic synthase II
-
-
-
-
polyhydroxyalkanoic synthase III
-
-
-
-
polyhydroxybutyrate synthase
Q667_12980
type I polyhydroxyalkanoate synthase
type II PHA synthase
type II PhaC1
type II Pseudomonas PHA synthase 1
type III PHA synthase
type-III PHA synthase
class I polyhydroxybutyrate synthase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
PHA synthase
-
-
-
-
PhaC
-
-
-
-
PhaE
-
-
-
-
poly-beta-hydroxybutyrate synthase
UniProt
poly-beta-hydroxybutyrate synthase
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n = CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n = [(R)-3-hydroxybutanoate]n+1 + CoA
Tyr36 is catalytically essential
-
-
-
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n = [(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n = [(R)-3-hydroxyacyl]n+1 + CoA
specific for medium-chain acyl-CoA with a chain length of 6-14 carbon atoms. The enzyme is composed of a single subunit.
-
-
-
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n = [(R)-3-hydroxyacyl]n+1 + CoA
can use short- and medium-chain acyl-CoA with a chain length of 3-14 carbon atoms. The enzyme is composed of two nonidentical subunits.
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
poly(R)-3-hydroxyalkanoate (3R)-3-hydroxyacyltransferase
This is the key enzyme in the biosynthesis of polyhydroxyalkanoates (PHA), linear polyesters produced by bacteria as a means of carbon and energy storage [6]. The enzyme catalyses the stereoselective, covalent linkage of (3R)-3-hydroxyacyl-CoA thioesters in a transesterification reaction with concomitant release of coenzyme A. The growing polymer is attached to a conserved active site L-cysteine residue. Three types of PHA synthases have been proposed based on their substrate specificity and enzyme structure. Type I and type III synthases preferentially polymerize short chain hydroxyalkanoate monomers containing 3-5 carbon atoms [1,2]. The difference between these two types is that type I synthases are composed of only a single subunit (PhaC), whereas type III synthases are composed of two different subunits, PhaC and PhaE [3,5]. Type II synthases are also composed of a single subunit (PhaC), but preferentially polymerize monomers containing more than 5 carbon atoms [4].
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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
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
Burkholderia sp. USM (JCM 15050)
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxy-4-methylvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxy-4-methylvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyalkanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyalkanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
(3R)-3-hydroxybutyryl-CoA + poly[5-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-5-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
(3R)-3-hydroxyvaleryl-CoA + poly[(R)-3-hydroxyvalerate]n
CoA + poly[(R)-3-hydroxyvalerate]n+1
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
?
(R)-lactoyl-CoA + (3R)-3-hydroxybutyryl-CoA
CoA + poly(lactate-co-3-hydroxybutyrate)
-
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyhexanoate
poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
3-hydroxybutyryl-CoA + 3-hydroxyvaleryl-CoA
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
mutant enzymes
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[3-hydroxybutyrate](n+1) + CoA
-
-
-
?
3-hydroxypropanoyl-CoA + (3-hydroxypropanoate)n
[(R)-3-hydroxypropanoate](n+1) + CoA
-
the value of the number-average molecular weight of the polymer obtained at a molar ratio of monomer-to-enzyme of 5000 is 25000 while the polydispersity is 4.7
-
-
?
3-hydroxypropanoyl-CoA + 3-hydroxybutanoyl-CoA
poly(3-hydroxypropanoate-co-3-hydroxybutanoate) + CoA
-
-
-
-
?
3-hydroxyvaleryl-CoA + [3-hydroxyvalerate]n
[3-hydroxyvalerate](n+1) + CoA
-
-
-
?
4-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[4-hydroxybutanoate](n+1) + CoA
-
-
-
?
DL-3-beta-hydroxybutyryl-CoA + poly[DL-3-hydroxybutyrate]n
CoA + poly[DL-3-hydroxybutyrate]n+1
-
-
-
-
?
DL-3-hydroxbutyryl-CoA + poly[DL-3-hydroxybutyrate]n
CoA + poly[DL-3-hydroxybutyrate]n+1
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
Hydrogenophaga pseudoflava NBRC-102513
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxybutyrate]n
CoA + poly[(R)-3-hydroxybutyrate]n+1
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
Aeromonas hydrophila CGMCC 0911
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyhexanoate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyhexanoate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
Hydrogenophaga pseudoflava NBRC-102513
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[(R)-3-hydroxyvalerate]
CoA + poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
-
-
-
-
?
(3R)-3-hydroxybutyryl-CoA + poly[4-hydroxybutyrate]
CoA + poly[(R)-3-hydroxybutyrate-co-4-hydroxybutyrate]
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyhexanoyl-CoA + poly[(R)-3-hydroxyhexanoate]n
CoA + poly[(R)-3-hydroxyhexanoate]n+1
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
substrate HBCoA
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
substrate HBCoA
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
substrate HBCoA
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
Hydrogenophaga pseudoflava NBRC-102513
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
an inherent property of the synthase is chain termination and reinitiation. Class III PhaCPhaEAv synthase initiates polymerization through selfpriming. The primed synthase, species I, can serve as a substrate for further polyhydroxybutanoate elongation. Since hydroxybutyryl units can be added onto the existing polymers when HB-CoA is introduced into a reaction mixture containing preformed intermediate species, the reaction catalyzed by PhaCPhaEAv is nonprocessive. When enough (R)-3-hydroxybutyryl-CoA (S/E ratio is high) is available to load all of the enzyme present, the polymerization may be processive such that no intermediates can be detected and preformed oligomers cannot be extended
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
D2Z0B8; D2Z0B6
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
D2Z0B8; D2Z0B6
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
rate of elongation is much faster than the rate of initiation. The protein is uniformly loaded by a a single CoA/PhaC. Priming with the artificial primer sTCoA, i.e. a trimer of (R)-3-hydroxybutyryl-CoA in which the terminal OH group is replaced with a 3H, increases the uniformity of elongation, allowing distinct polymerization species to be observed. In the absence of (R)-3-hydroxybutyryl-CoA, a dimer of (R)-3-hydroxybutyryl-CoA is formed with a rate constant of 0.017 per s. The dimer forms via attack of CoA on the oxoester of the trimer of (R)-3-hydroxybutyryl-CoA-enzyme chain, leaving the synthase attached to a single (R)-3-hydroxybutyryl unit
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
I3R9Z3; I3R9Z4
-
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
PHB synthase exhibits positive cooperativity
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
PHB synthase exhibits positive cooperativity
-
-
?
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HCCoA
-
-
?
(R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HCCoA
-
-
?
(R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HCCoA
-
-
?
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
[(R)-3-hydroxypentanoate](n+1)
-
activity is 43% of the reaction with 3-hydroxybutyryl-CoA
-
-
?
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
[(R)-3-hydroxypentanoate](n+1)
-
activity is 10% of the reaction with 3-hydroxybutyryl-CoA
-
-
?
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
[(R)-3-hydroxypentanoate](n+1)
-
-
-
?
(R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HVCoA
-
-
?
(R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HVCoA
-
-
?
(R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HVCoA
-
-
?
3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HHxeCoA
-
-
?
3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxeCoA, low activity
-
-
?
3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxeCoA
-
-
?
3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HHxyCoA
-
-
?
3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxyCoA, low activity
-
-
?
3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HHxyCoA
-
-
?
3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
-
substrate HABCoA
-
-
?
3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HABCoA, low activity
-
-
?
3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n
? + CoA
substrate HABCoA
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
incubation of D302A-PhaCPhaE with [14C]-hydroxybutanoyl-CoA results in detection of oligomeric HBs covalently bound to PhaC, at hydroxybutanoyl-CoA to enzyme ratios between 5 and 100
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
the PhaC-(His)6 protein catalyzes polymerization with a specific activity of 0.9 unit/mg. The PhaE-(His)6 protein is inactive. Addition of PhaE-(His)6 to PhaC-(His)6 increases the activity several 100fold. PhaC contains all the elements essential for catalysis and the polymerization proceeds by covalent catalysis using C149 and potentially C130
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
acylation of C319 causes a shift of the monomeric form of the synthase to its dimeric form, and this shift is accompanied by a substantial increase in its specific activity and a substantial decrease in the lag phase of polymer formation
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
Ralstonia eutropha synthase possesses an essential catalytic dyad (C319-H508) in which the C319 is involved in covalent catalysis. A conserved Asp, D480, is not required for acylation of C319 by sT-CoA and is proposed to function as a general base catalyst to activate the hydroxyl of HBCoA for ester formation
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a low-molecular-weight, Mn = 20000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a low-molecular-weight, Mn = 20000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a relatively high molecular weight, Mn = 890000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a relatively high molecular weight, Mn = 890000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutyrate](n+1) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
[3-hydroxybutanoate](n+1) + CoA
-
-
-
?
additional information
?
-
-
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
-
less than 2% of the activity with 3-hydroxybutyryl-CoA: (R)-3-hydroxyhexanoyl-CoA, 3-hydroxypropionyl-CoA, (2R,3R)-2-methyl-3-hydroxylbutyryl-CoA, (R)-3-hydroxybutyryl (D)-pantetheine thioester, (R)-lactyl-CoA
-
-
?
additional information
?
-
-
synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class I PHA synthases, overview. The HHxyCoA and HABCoA can be efficiently incorporated into the polymers produced by enzyme PhaECAv. HHxCoA can be metabolically generated from 3-(R)-hydroxy-5-hexynoic acid. The activity of PhaECAv drops significantly with increasing length of the side chain in substrates. For example, the polymerization rates of HVCoA, HHxCoA, and HCCoA catalyzed by PhaECAv are measured at 23%, 0.38%, and 0.005% rate of HBCoA, respectively. No or poor activity with 3-(R)-hydroxy-4-phenylbutyryl-CoA (HPBCoA). Class III PhaECAv can polymerize HABCoA 6.5fold faster than HHxyCoA
-
-
-
additional information
?
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
D2Z0B8; D2Z0B6
enzyme shows alcoholytic cleavage of PHA chains induced by endogenous ethanol
-
-
?
additional information
?
-
-
enzyme shows alcoholytic cleavage of PHA chains induced by endogenous ethanol
-
-
?
additional information
?
-
D2Z0B8; D2Z0B6
enzyme shows both PHA polymerization and alcoholysis activities. For alcoholysis, PhaRC utilizes various alcohols other than ethanol for alcoholysis, leading to the PHA carboxy terminus modified with thiol, alkynyl, hydroxy, and benzyl groups
-
-
?
additional information
?
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
D2Z0B8; D2Z0B6
enzyme shows alcoholytic cleavage of PHA chains induced by endogenous ethanol
-
-
?
additional information
?
-
D2Z0B8; D2Z0B6
enzyme shows both PHA polymerization and alcoholysis activities. For alcoholysis, PhaRC utilizes various alcohols other than ethanol for alcoholysis, leading to the PHA carboxy terminus modified with thiol, alkynyl, hydroxy, and benzyl groups
-
-
?
additional information
?
-
Burkholderia sp. USM (JCM 15050)
-
the transformant Cupriavidus necator PHB-4 harbouring Burkholderia sp. enzyme gene accumulates poly(3-hydroxybutyrate-co-4-hydroxybutyrate) with 4-hydroxybutyrate monomer as high as up to 87 mol% from sodium 4-hydroxybutyrate. The wild type Burkholderia sp. does not have the ability to produce this copolymer
-
-
-
additional information
?
-
synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. PhaCCc displays 2.5fold lower activity with HABCoA than with HHxyCoA
-
-
-
additional information
?
-
-
synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. PhaCCc displays 2.5fold lower activity with HABCoA than with HHxyCoA
-
-
-
additional information
?
-
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. Priming of PhaCCc with saturated trimeric HBCoA (named sTCoA) demonstrates that approximately one equivalent CoA per PhaC is released during enzyme assay. This is quite different from other reported class I synthases. Wild-type PhaCCs has similar activities toward HHxyCoA and HABCoA
-
-
-
additional information
?
-
-
no or less than 1% of the activity with 3-hydroxybutyryl-CoA: (R)-3-hydroxyhexanoyl-CoA, 3-hydroxypropionyl-CoA, (S)-3-hydroxybutyryl-CoA, (2R,3R)-2-methyl-3-hydroxylbutyryl-CoA, (R)-3-hydroxybutyryl (D)-pantetheine thioester, 4-hydroxybutyryl-CoA, (R)-lactyl-CoA
-
-
?
additional information
?
-
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
-
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
Cupriavidus necator 17699
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
-
the 3-hydroxyvalerate molar fraction in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) is significantly affected by the type of the precursor used and their respective feeding time
-
-
?
additional information
?
-
-
the 3-hydroxyvalerate molar fraction in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) is significantly affected by the type of the precursor used and their respective feeding time
-
-
?
additional information
?
-
I3R9Z3; I3R9Z4
the enzyme is responsible for synthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
additional information
?
-
-
the enzyme is responsible for synthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
additional information
?
-
-
3-hydroxyvaleryl-CoA, 4-hydroxybutyryl-CoA, and 3-hydroxydecanoyl-CoA are not accepted as substrates
-
-
?
additional information
?
-
-
3-hydroxyvaleryl-CoA, 4-hydroxybutyryl-CoA, and 3-hydroxydecanoyl-CoA are not accepted as substrates
-
-
?
additional information
?
-
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile atty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview
-
-
-
additional information
?
-
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
Hydrogenophaga pseudoflava NBRC-102513
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
Hydrogenophaga pseudoflava NBRC-102513
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
-
PHA biosynthesis and in vitro PhaC enzymatic assay results show that the uncharacterized putative PHA synthase from Janthinobacterium sp. UMAB-58 is not funtional
-
-
-
additional information
?
-
-
PHA biosynthesis and in vitro PhaC enzymatic assay results show that the uncharacterized putative PHA synthase from Janthinobacterium sp. UMAB-60 is funtional
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
-
-
-
additional information
?
-
analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA)
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
-
the monomer composition of the wild-type cells contains more medium-chain length monomer in the PHAs, with highest content for 3-hydroxyoctanoate, overview. The enzyme mutants show a shift in substrate specificity and produce PHAs with a higher content of 3-hydroxybutanoate
-
-
?
additional information
?
-
structure-function relationship of PhaCs, and substrate specificity, overview
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
-
no activity with (R)-3-hydroxypropionate and (R)-3-hydroxyvalerate
-
-
-
additional information
?
-
-
recombinant enzyme, expressed in phaC-deficient Cupriavidus necator, is able to accumulate PHA homopolymers and copolymers including poly(3-hydroxybutyrate) [P(3HB)], poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [P(3HB-co-3HV)], poly(3-hydroxybutyrate-co-5-hydroxyvalerate) [P(3HB-co-5HV)], poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)], poly(3-hydroxybutyrate-co-3-hydroxy-4-methylvalerate) [P(3HB-co-3H4MV)], and poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) [P(3HB-co-3HHx)], when suitable precursors are provided
-
-
-
additional information
?
-
-
the polyhydroxyalkanoate (PHA) synthase (PhaC) from a mangrove soil metagenome possesses a very wide substrate specificity. The enzyme shows the ability to incorporate six types of PHA monomers, 3-hydroxybutyrate (3HB), 3-hydroxyvalerate (3HV), 4-hydroxybutyrate (4HB), 3-hydroxy-4-methylvalerate (3H4MV), 5-hydroxyvalerate (5HV) and 3-hydroxyhexanoate (3HHx) in the presence of suitable precursors
-
-
-
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
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(3R)-3-hydroxyacyl-CoA + poly[(R)-3-hydroxyalkanoate]n
CoA + poly[(R)-3-hydroxyalkanoate]n+1
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate](n+1) + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
?
(R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
Hydrogenophaga pseudoflava NBRC-102513
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
-
?
3-hydroxyacyl-CoA + [(R)-3-hydroxyacyl]n
[(R)-3-hydroxyacyl]n+1 + CoA
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + 3-hydroxyvalerate
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a low-molecular-weight, Mn = 20000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a low-molecular-weight, Mn = 20000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a relatively high molecular weight, Mn = 890000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
PhaRCBm synthesizes (R)-3-hydroxybutanoate, P(3HB), with a relatively high molecular weight, Mn = 890000
-
-
?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
[(R)-3-hydroxybutanoate]n+1 + CoA
-
-
-
-
?
additional information
?
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
-
the PhaC from BAcillus cereus also shows a polyhydroxybutanoate hydrolyzing activity, time-dependent change in inverse of degree of polymerization during intracellular P(3HB) degradation at a culture temperature of 37°C, overview
-
-
?
additional information
?
-
-
the 3-hydroxyvalerate molar fraction in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) is significantly affected by the type of the precursor used and their respective feeding time
-
-
?
additional information
?
-
-
the 3-hydroxyvalerate molar fraction in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) is significantly affected by the type of the precursor used and their respective feeding time
-
-
?
additional information
?
-
I3R9Z3; I3R9Z4
the enzyme is responsible for synthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
additional information
?
-
-
the enzyme is responsible for synthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
additional information
?
-
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile atty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview
-
-
-
additional information
?
-
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
Hydrogenophaga pseudoflava NBRC-102513
-
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
Hydrogenophaga pseudoflava NBRC-102513
the bacteria produce homo-polymer [poly-3-hydroxybutyrate (P3HB)] when only acetate is used as carbon source, and it produces co-polymer [poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) P(3HB-co-3HV)] by addition of co-substrate propionate. Evaluation of PHA production by Pseudomonas pseudoflava strain NBRC-102513 from wastewater containing diverse volatile fatty acids (VFA), common products of various wastewaters. Analysis of the PHA spectrum produced from different carbon sources, NMR study, overview. MW and polydispersity index (PDI, Mw/Mn) of the P3HB produced by Pseudomonas pseudoflava is 17.63 kDa and 3.3 respectively. MW and PDI of the co-polymer P(3HB-co-3HV) produced by Pseudomonas pseudoflava is 52.33 kDa and 5.7 respectively. The Mw of the standard P(3HB-co-3HV) is 110 kDa, and PDI is 4.3. Pseudomonas pseudoflava can produce biopolymers with relatively lower dispersity
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors
-
-
-
additional information
?
-
-
recombinant enzyme, expressed in phaC-deficient Cupriavidus necator, is able to accumulate PHA homopolymers and copolymers including poly(3-hydroxybutyrate) [P(3HB)], poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [P(3HB-co-3HV)], poly(3-hydroxybutyrate-co-5-hydroxyvalerate) [P(3HB-co-5HV)], poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)], poly(3-hydroxybutyrate-co-3-hydroxy-4-methylvalerate) [P(3HB-co-3H4MV)], and poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) [P(3HB-co-3HHx)], when suitable precursors are provided
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
in the absence of salts the granule-bound PHB synthase still exhibits about 40% of the maximum activity. Enzyme activity is strongly enhanced by slightly increasing the ionic strength independent of the salt
Mg2+
-
addition of Mg2+ shows the strongest activation effect. However, high enzyme activity without Mg2+ ions is observed, when other ions are present, suggesting that Mg2+ ions do not serve as cofactors
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethyl-maleimide
-
1 mM N-ethyl-maleimide for 15 min inhibits the enzyme by 56%
CoA
-
very effective competitive inhibitor for the polymerization of 3-hydroxypropionyl-CoA
HBCH2CoA
-
substrate analogue, in which the S-atom in hydroxybutanoyl-CoA is replaced with a CH2 group. HBCH2CoA is a competitive inhibitor of class I and class III PHB synthases. Upon incubation with a synthase acylated with a [3H]-saturated trimer-CoA, i.e. sTCoA, products are the methylene analogue of [3H]-sTCoA, [3H]-sT-CH2-CoA, saturated dimer-[3H]-sD-CO2H, and trimer-acid [3H]-sT-CO2H. HBCH2CoA may be reporting on the termination and repriming process of the synthases, rather than elongation
HBCH2CoA
-
substrate analogue, in which the S-atom in hydroxybutanoyl-CoA is replaced with a CH2 group. HBCH2CoA is a competitive inhibitor of class I and class III PHB synthases. Upon incubation with a synthase acylated with a [3H]-saturated trimer-CoA, i.e. sTCoA, products are the methylene analogue of [3H]-sTCoA, [3H]-sT-CH2-CoA, saturated dimer-[3H]-sD-CO2H, and trimer-acid [3H]-sT-CO2H. HBCH2CoA may be reporting on the termination and repriming process of the synthases, rather than elongation
additional information
no inhibition by bovine serum albumin
-
additional information
no inhibition by bovine serum albumin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl phosphate
-
activates the enzyme and the level of activation is dependent on the concentration of acetyl phosphate supplementation
acetyl phosphate
-
10 mM acetyl phosphate activates both the native and the dephosphorylated enzyme 6fold and 2fold, respectively
bovine serum albumin
-
leads to an activity increase of severalfold when BSA is added to a concentration of 0.5 mg/mL (0.0075 mM) in the assay mixture
-
bovine serum albumin
addition of BSA increases the specific activity of enzyme PhaCCs with HBCoA about 2fold
-
additional information
-
upion growth in in N2 deficient medium, cell biomass remains almost steady from 0 h after transfer to production medium till the end of fermentation (120 h), while polyhydroxybutanoate yield shows an increase from 0.533 g/l at 0 h to 4g/l by 48 h and later gradually decreases, with increase in polyhydroxybutanoate accumulation increase from 11% to 77% by 96 h
-
additional information
no significant activation of enzyme PhaCCc by bovine serum albumin, molecular activation mechanism, overview
-
additional information
-
no significant activation of enzyme PhaCCc by bovine serum albumin, molecular activation mechanism, overview
-
additional information
molecular activation mechanism, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Colonic Neoplasms
A multi-functional polyhydroxybutyrate nanoparticle for theranostic applications.
Neoplasms
Enzymatic synthesis of a drug delivery system based on polyhydroxyalkanoate-protein block copolymers.
Starvation
Requirement of the nitrogen starvation-induced protein Sll0783 for polyhydroxybutyrate accumulation in Synechocystis sp. strain PCC 6803.
Virus Diseases
Expression and analysis of a bacterial poly(hydroxyalkanoate) synthase in insect cells using a baculovirus system.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
(3R)-3-hydroxybutyryl-CoA
-
at pH 7.0, temperature not specified in the publication
0.66
(3R)-3-hydroxybutyryl-CoA
-
at pH 7.0, temperature not specified in the publication
0.29
(R)-3-hydroxybutanoyl-CoA
recombinant enzyme, pH 7.8, 30°C
0.19
(R)-3-hydroxybutyryl-CoA
-
25°C, pH 7.0, wild-type enzyme, based on one catalytic site in a dimeric enzyme
0.32
(R)-3-hydroxybutyryl-CoA
-
25°C, pH 7.0, mutant enzyme G4D, based on one catalytic site in a dimeric enzyme
2.07
(R)-3-hydroxyvaleryl-CoA
recombinant enzyme, pH 7.8, 30°C
3.22
3-(R)-hydroxhex-5-enoyl-CoA
recombinant enzyme, pH 7.8, 30°C
1.54
3-(R)-hydroxyhex5-ynoyl-CoA
recombinant enzyme, pH 7.8, 30°C
0.07
3-(S)-hydroxy-4-azidobutyryl-CoA
-
recombinant enzyme, pH 7.8, 30°C
9.46
3-(S)-hydroxy-4-azidobutyryl-CoA
recombinant enzyme, pH 7.8, 30°C
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics. Caulobacter crescentus class I PHA synthase uniquely lacks of a lag phase in its polymerization kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics. Caulobacter crescentus class I PHA synthase uniquely lacks of a lag phase in its polymerization kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
297
4-hydroxybutyryl-CoA
based on the assumption that 2 PhaC and 2 PhaE subunits comprise one catalytic site
75
(R)-3-hydroxybutanoyl-CoA
recombinant enzyme, pH 7.8, 30°C
26
(R)-3-hydroxybutyryl-CoA
-
25°C, pH 7.0, mutant enzyme G4D, based on one catalytic site in a dimeric enzyme
44
(R)-3-hydroxybutyryl-CoA
-
25°C, pH 7.0, wild-type enzyme, based on one catalytic site in a dimeric enzyme
320
(R)-3-hydroxybutyryl-CoA
based on the assumption that 2 PhaC and 2 PhaE subunits comprise one catalytic site
14.4
(R)-3-hydroxyvaleryl-CoA
recombinant enzyme, pH 7.8, 30°C
122
(R)-3-hydroxyvaleryl-CoA
based on the assumption that 2 PhaC and 2 PhaE subunits comprise one catalytic site
0.06
3-(R)-hydroxhex-5-enoyl-CoA
recombinant enzyme, pH 7.8, 30°C
0.13
3-(R)-hydroxyhex5-ynoyl-CoA
recombinant enzyme, pH 7.8, 30°C
0.19
3-(S)-hydroxy-4-azidobutyryl-CoA
recombinant enzyme, pH 7.8, 30°C
20
3-(S)-hydroxy-4-azidobutyryl-CoA
-
recombinant enzyme, pH 7.8, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
258.6
(R)-3-hydroxybutanoyl-CoA
recombinant enzyme, pH 7.8, 30°C
6.96
(R)-3-hydroxyvaleryl-CoA
recombinant enzyme, pH 7.8, 30°C
0.019
3-(R)-hydroxhex-5-enoyl-CoA
recombinant enzyme, pH 7.8, 30°C
0.084
3-(R)-hydroxyhex5-ynoyl-CoA
recombinant enzyme, pH 7.8, 30°C
0.02
3-(S)-hydroxy-4-azidobutyryl-CoA
recombinant enzyme, pH 7.8, 30°C
285.7
3-(S)-hydroxy-4-azidobutyryl-CoA
-
recombinant enzyme, pH 7.8, 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.243
Burkholderia sp. USM (JCM 15050)
-
recombinant enzyme expressed in Cupriavidus necator PHB-4, at pH 8.0 and 30°C
2.5
-
mutant enzyme S324T/Q480K of isoform PhaC1SG, at pH 8.0 and 30°C
3 - 8
-
pooled monomeric and dimeric fractions of Strep2-PhaCRe, 30°C, pH not specified in the publication
36
-
purified recombinant Strep2-PhaCRe, 30°C, pH not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
pH 6.5: about 30% of maximal activity, pH 8.5: about 85% of maximal activity
7 - 8.8
-
pH 7.0: about 40% of maximal activity, pH 8.8: about 65% of maximal activity, Tris/HCl buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
20°C: about 50% of maximal activity, 70°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Phb synthase subunits PhaC and PhaE
A0A1E8EW93; A0A1E8EW64
UniProt
brenda
Phb synthase subunits PhaC and PhaE
A0A1E8EW93; A0A1E8EW64
UniProt
brenda
i.e. Ralstonia eutropha
UniProt
brenda
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
i.e. Ralstonia eutropha
UniProt
brenda
a PHA-producing strain isolated from a soil sample from western peninsular Malaysia, gene phaCUSMAA2-4
-
-
brenda
a PHA-producing strain isolated from a soil sample from western peninsular Malaysia, gene phaCUSMAA2-4
-
-
brenda
gene is a biomarker for microorganisms that contain class III PHA synthase
UniProt
brenda
gene is a biomarker for microorganisms that contain class III PHA synthase
UniProt
brenda
Hydrogenophaga pseudoflava NBRC-102513
isolated in Malaysia, gene phbC encoded in the phb operon
UniProt
brenda
isolated as a PHA producer from the polluted soil in Kitakyushu City, Japan
UniProt
brenda
isolated as a PHA producer from the polluted soil in Kitakyushu City, Japan
UniProt
brenda
-
684590, 684662, 685059, 685312, 685486, 685487, 685729, 687271, 688783, 689122, 714539, 718922, 735350
-
-
brenda
isolated in Malaysia, gene phbC encoded in the phb operon
UniProt
brenda
isolated from mangrove soil collected in the mangrove forest at Balik Pulau, Penang, Malaysia
-
-
brenda
uncultured bacterium from Balik Pulau (Penang, Malaysia) mangrove soil
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
highest P(3HB) production of 2.38 g/l at 68 wt% attained with crude palm kernel oil as the sole carbon source
brenda
-
highest P(3HB) production of 2.38 g/l at 68 wt% attained with crude palm kernel oil as the sole carbon source
-
brenda
additional information
two-phase culture of strain TH-1 for PHB production under autotrophic and heterotrophic condition, overview
brenda
additional information
two-phase culture of strain TH-1 for PHB production under autotrophic and heterotrophic condition, overview
brenda
additional information
-
two-phase culture of strain TH-1 for PHB production under autotrophic and heterotrophic condition, overview
brenda
additional information
Hydrogenophilus thermoluteolus DSM 6765
-
two-phase culture of strain TH-1 for PHB production under autotrophic and heterotrophic condition, overview
-
brenda
additional information
-
two-phase culture of strain TH-1 for PHB production under autotrophic and heterotrophic condition, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
I3R9Z3; I3R9Z4
PhaEHme and PhaCHme proteins are strongly bound to the granules
-
brenda
-
PHB synthase can not be released from the PHB granules, indicating a covalent attachment to the PHB core
-
brenda
-
PHB synthase can not be released from the PHB granules, indicating a covalent attachment to the PHB core
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
28 strains belonging to 15 genera in the family Halobacteriaceae, sequence comparisons, phylogenetic analysis, and analyses of conserved regions of type III PHA synthases, overview
evolution
-
PHA synthases have been assigned to three classes based on their substrate specificity and subunit composition. The class I PHA synthases are composed of a single type of polypeptide chain and use mainly short chain length hydroxyalkanoic acid CoA thioesters as substrates. The class III PHA synthases are composed by two different subunits, each of approximately 40 kDa. Substrate specificity is the main difference between class II and both class I and class III PHA synthases. Class II PHA synthases integrate specially 3-hydroxyfatty acids of medium chain length (C6-C14) into PHA, and the resulting product is a latex-like polymer. Class I PHA synthases synthesize higher molecular weight PHAs compared with class II PHA synthases
evolution
PHA synthases have been assigned to three classes based on their substrate specificity and subunit composition. The class I PHA synthases are composed of a single type of polypeptide chain and use mainly short chain length hydroxyalkanoic acid CoA thioesters as substrates. The class III PHA synthases are composed by two different subunits, each of approximately 40 kDa. Substrate specificity is the main difference between class II and both class I and class III PHA synthases. Class II PHA synthases integrate specially 3-hydroxyfatty acids of medium chain length (C6-C14) into PHA, and the resulting product is a latex-like polymer. Class I PHA synthases synthesize higher molecular weight PHAs compared with class II PHA synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
PhaC synthases are grouped into four classes based on substrate specificity, and the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce principally scl-PHAs, while Class II PhaC synthesize mcl-PHAs. Class II PhaC synthases are widely distributed in bacteria. Class II PhaCPhaC enzymes differ from PhaCCn, as prototype of Class I PHA synthases, by about 28 amino acids, reaching the C-terminal (1-559) with a sequence shorter by about 30 amino acids. The catalytic triad has been renumbered as Cys296, Asp452, His453 and His480 in Pseudomonas spp., prototype for Class II PHA synthases. Tyr412 in PhaCCs, and Tyr446 in the 6-helix in PhaCCn, are residues conserved in Class I, III and IV PHA synthases, while Phe occupies this position in Class II synthases
evolution
-
Pseudomonas isolates are found to carry PHA synthase genes which fall into two different PHA gene clusters, namely Class I and Class II, which are involved in the biosynthesis of short-chain-length-PHA (SCL-PHA) and medium-chain-length-PHA (MCL-PHA), respectively
evolution
-
Pseudomonas isolates are found to carry PHA synthase genes which fall into two different PHA gene clusters, namely Class I and Class II, which are involved in the biosynthesis of short-chain-length-PHA (SCL-PHA) and medium-chain-length-PHA (MCL-PHA), respectively
evolution
-
the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. No other gene involved in PHA synthesis is detected in close proximity to the uncharacterized putative PHA synthase gene in the Janthinobacterium isolates, therefore it falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Both of the antarctic Janthinobacterium isolates (UMAB-56 and UMAB-60) have a similar Class I PHA gene cluster as the Jantinobactarium spp. SCL-PHA producers
evolution
-
the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. No other gene involved in PHA synthesis is detected in close proximity to the uncharacterized putative PHA synthase gene in the Janthinobacterium isolates, therefore it falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Both of the antarctic Janthinobacterium isolates (UMAB-56 and UMAB-60) have a similar Class I PHA gene cluster as the Jantinobactarium spp. SCL-PHA producers
evolution
-
the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. The uncharacterized putative PHA synthase gene in the Janthinobacterium isolates falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Multiple sequence alignment shows that the uncharacterized putative PHA synthase gene contains all the highly conserved amino acid residues and the proposed catalytic triad of PHA synthase. Proposal of the uncharacterized PHA synthase as the new Class V PhaC
evolution
-
the Janthinobacterium isolates carry a Class I and an uncharacterized putative PHA synthase genes. The uncharacterized putative PHA synthase gene in the Janthinobacterium isolates falls into a separate clade from the ordinary Class I, II, III and IV clades of PHA synthase (PhaC) phylogenetic tree. Multiple sequence alignment shows that the uncharacterized putative PHA synthase gene contains all the highly conserved amino acid residues and the proposed catalytic triad of PHA synthase. Proposal of the uncharacterized PHA synthase as the new Class V PhaC
evolution
A0A1E8EW93; A0A1E8EW64
the three genes phaJ (CLAOCE_21160) and phaEC (CLAOCE_21150 and CLAOCE_21140) are clustered in Clostridium acetireducens and encode a (R)-enoyl-CoA hydratase as well as a type III PHA synthase. The genes phaJ and phaEC from Clostridium acetireducens share high sequence similarity compared to genes encoding enzymes involved in PHB formation such as phaJ from Rhodospirillum rubrum or Haloferax mediterranei (Rru_A2964, HFX_1483) and phaEC from Synechocystis sp. PCC 6803
evolution
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHA-SCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHA-MCL which contains 6-14 carbons in the monomer unit
evolution
-
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
evolution
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
evolution
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
evolution
-
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
-
evolution
Cupriavidus necator 17699
-
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
-
evolution
-
the three genes phaJ (CLAOCE_21160) and phaEC (CLAOCE_21150 and CLAOCE_21140) are clustered in Clostridium acetireducens and encode a (R)-enoyl-CoA hydratase as well as a type III PHA synthase. The genes phaJ and phaEC from Clostridium acetireducens share high sequence similarity compared to genes encoding enzymes involved in PHB formation such as phaJ from Rhodospirillum rubrum or Haloferax mediterranei (Rru_A2964, HFX_1483) and phaEC from Synechocystis sp. PCC 6803
-
evolution
-
there is a total of four classes of PhaCs, where class I, III, and IV prefer to synthesize PHASCL containing 3-5 carbons in the monomer unit, while class II PhaC prefers to synthesize PHAMCL which contains 6-14 carbons in the monomer unit
-
evolution
Hydrogenophaga pseudoflava NBRC-102513
-
PHA synthases have been assigned to three classes based on their substrate specificity and subunit composition. The class I PHA synthases are composed of a single type of polypeptide chain and use mainly short chain length hydroxyalkanoic acid CoA thioesters as substrates. The class III PHA synthases are composed by two different subunits, each of approximately 40 kDa. Substrate specificity is the main difference between class II and both class I and class III PHA synthases. Class II PHA synthases integrate specially 3-hydroxyfatty acids of medium chain length (C6-C14) into PHA, and the resulting product is a latex-like polymer. Class I PHA synthases synthesize higher molecular weight PHAs compared with class II PHA synthases
-
malfunction
mutation of residues S320, F333, S475, A479, Y492, and L506 affects the positioning of the catalytic triad residues, while mutation of F387 affects the enzyme's dimerization
malfunction
mutation of residues S325, F338, S477, Q481, Y494, and Q508 affects the positioning of the catalytic triad residues, while mutation of F392 affects the enzyme's dimerization
malfunction
mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
malfunction
-
mutation of residues T349, F362, S501, A505, F518, and L532 affects the positioning of the catalytic triad residues, while mutation of F416 affects the enzyme's dimerization
malfunction
-
mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
-
malfunction
Cupriavidus necator 17699
-
mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
-
malfunction
-
mutation of residues T348, F361, S506, A510, H523, and L537 affects the positioning of the catalytic triad residues, while mutation of class I/II-conserved Phe420 of PhaCCn to serine greatly reduced the lag phase and affects the enzyme's dimerization
-
metabolism
-
PhaC is involved in the biosynthetic pathway for generation of (R)-3-hydroxybutyrate monomers from two acetyl-CoA molecules, and further of short-chain length polyhydroxyalkanoates, PHAs. The malonyl-CoA availability is a limiting factor to synthesis of poly(3-hydroxybutyrate), P(3HB), thus acetoacetyl-CoA synthetase, which is controlling the malonyl-CoA pool, is an important enzyme for increasing the P(3HB) production
metabolism
Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% (w/w) of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
metabolism
Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% w/w of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
metabolism
-
PHA synthase is the critical enzyme in PHA biosynthesis
metabolism
PHA synthase is the critical enzyme in PHA biosynthesis
metabolism
-
polyhydroxyalkanoate synthase is not the rate limiting enzyme of polyhydroxyalkanoate biosynthesis in Synechocystis sp. PCC6803
metabolism
Hydrogenophilus thermoluteolus DSM 6765
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Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% (w/w) of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
-
metabolism
Hydrogenophilus thermoluteolus DSM 6765
-
Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% w/w of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
-
metabolism
-
Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% (w/w) of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
-
metabolism
-
Hydrogenophilus thermoluteolus strain TH-1 is a thermophilic hydrogen-oxidizing microorganism that has the highest growth rate among autotrophs. Genomic analysis reveals that this strain comprises the complete gene set for poly-beta-hydroxybutyrate (PHB) synthesis, i.e. three copies of acetyl-CoA acetyltransferase and polyhydroxyalkanoate synthase and one copy of acetoacetyl-CoA reductase and 3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase. PHB accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions. This strain accumulates up to 430.4 mg LL1 PHB during a 3-h incubation under nitrogen-limited heterotrophic conditions. The highest PHB accumulation rates under autotrophic and heterotrophic conditions are 38.6% w/w of the dry cells after a 6-h induction and 53.8% after 3 h, respectively. Although PHB granules start to accumulate after 15 min of nitrogen limitation under heterotrophic conditions, a drastic decrease of PHB is observed after 9 h of induction. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
-
metabolism
Hydrogenophaga pseudoflava NBRC-102513
-
PHA synthase is the critical enzyme in PHA biosynthesis
-
physiological function
-
class I PHB synthase, PhaC, from Ralstonia eutropha catalyzes the formation of PHB from (R)-3-hydroxybutyryl-CoA, ultimately resulting in the formation of insoluble granules, the polymer elongation rate is much faster than the initiation rate
physiological function
P(3HB) synthase catalyzes polymerization of the 3-hydroxybutyryl-CoA monomers, Pseudomonas sp. USM 4-55 is a soil isolated bacterium that possesses the ability to produce polyhydroxyalkanoates consisting of both poly(3-hydroxybutyrate) homopolymer and medium-chain length monomers (6 to 14 carbon atoms) when sugars or fatty acids are utilized as the sole carbon source
physiological function
-
PHA accumulation rates in the differnt strains harboring type III PHA synthases, overview
physiological function
enzyme is able to produce poly(3-hydroxybutyrate) in recombinant Cupriavidus necator PHB-negative mutant under the control of the phaC1 promoter from Cupriavidus necator H16
physiological function
gene expression in a Cupriavidus necator polyhydroxyalkanoate-negative mutant results in the accumulation of significant amount of polyhydroxyalkanoate
physiological function
-
heterologous expression of foreign PHA synthases in the single mutant lacking isoform PhaC2 and in a double mutant lacking both isoforms PhaC1 and PhaC2 results in a significant accumulation of polyhydroxybutanoate in all generated strains. Six of the thirteen generated phaC hybrid vectors lead to an increased polyhydroxybutanoate accumulation in the single mutant in comparison to the wild type strain. All recombinant strains of Rthe double mutant harboring heterologous phaC genes accumulate significantly less polyhydroxybutanoate than the recombinant single mutants and the wild type strain. Recombinant strains with higher content of accumulated polyhydroxybutanoate are linked to higher growth rates and higher maximum ODs, due to the light scattering effect of polyhydroxybutanoate granules. All recombinant strains of the double mutant show significantly decreased growth rates and maximum ODs
physiological function
D2Z0B8; D2Z0B6
recombinant Escherichia coli expressing PHA synthase from Bacillus cereus shows a reduction of the molecular weight of PHA produced during the stationary phase of growth. Its carboxy end structure is capped by ethanol, as the result of alcoholytic cleavage of PHA chains by PhaRC induced by endogenous ethanol. This scission reaction is also induced by exogenous ethanol in both in vivo and in vitro assays. In addition, PhaRC has alcoholysis activity for PHA chains synthesized by other synthases
physiological function
-
Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA)
physiological function
-
Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA)
physiological function
-
Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA). The ability of UMAB-40 to produce SCL-MCL-PHA copolymers is likely due to the presence of both Class I and II PHA synthases in its genome
physiological function
-
Class I PHA synthases are involved in the biosynthesis of short-chain-length-polyhydroxyalkanoates (SCL-PHA). The PHA produced by UMAB-60 is a homopolymer containing C4 repeating units
physiological function
-
Class II PHA synthases are involved in the biosynthesis of medium-chain-length-polyhydroxyalkanoates (MCL-PHA). Pseudomonas sp. UMAB-08 PHA gene cluster is very well conserved among the MCL-PHA producers
physiological function
-
Class II PHA synthases are involved in the biosynthesis of medium-chain-length-polyhydroxyalkanoates (MCL-PHA). Pseudomonas sp. UMAB-08 PHA gene cluster is very well conserved among the MCL-PHA producers. Although UMAB-40 does not produce any homopolymer (PHA having only one type of monomeric unit), small peaks of the C4 position [3-hydroxybutyrate (3HB) monomer] in addition to larger peaks at C6 to C14 are detected. The ability of UMAB-40 to produce SCL-MCL-PHA copolymers is likely due to the presence of both Class I and II PHA synthases in its genome
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaCPhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaCPhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors, Class II PhaC enzymes synthesize mcl-polymers depending on 3-hydroxyhexanoate (3HH), 3-hydroxyheptanoate (3HHp), 3-hydroxyoctanoate (3HO), 3-hydroxydecanoate (3HD), 3-hydroxyundecanoate (3HUD), 3-hydroxydodecanoate (3HDD) (C6 to C12), and availability of the corresponding CoA thioester substrates, originating from three different metabolic pathways. In Pseudomonas spp., there are two PhaCPhaC genes, of which PhaC1 is the active enzyme under physiological conditions
physiological function
-
different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group
physiological function
different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group
physiological function
different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group. Specifically, the specific activity of PhaCCs toward propynyl analogue (HHxyCoA) is only 5fold less than that toward the classical substrate HBCoA
physiological function
-
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
physiological function
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
physiological function
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
physiological function
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs). Structure comparisons and structure-function relationship of PhaCs, overview
physiological function
-
PHA synthase is the critical enzyme in polyhydroxyalkanoates (PHA) biosynthesis, and R-3-hydroxyacyl-coenzyme A (CoA) is the substrate. Poly-3-hydroxybutyrate (P3HB) is one type of PHA produced by many bacteria
physiological function
PHA synthase is the critical enzyme in polyhydroxyalkanoates (PHA) biosynthesis, and R-3-hydroxyacyl-coenzyme A (CoA) is the substrate. Poly-3-hydroxybutyrate (P3HB) is one type of PHA produced by many bacteria
physiological function
-
PhaC can polymerize high molecular weight hydrophobic PHA chains in the hydrophilic environment of the cell cytoplasm
physiological function
poly-beta-hydroxybutyrate accumulation in the moderately thermophilic hydrogen-oxidizing bacterium Hydrogenophilus thermoluteolus TH-1 by induction of the poly-beta-hydroxybutyrate (PHB) synthesis pathway enzymes, including the PHB synthase. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
physiological function
A0A1E8EW93; A0A1E8EW64
species that do contain type III PHA synthases (phaEC) are able to produce butyrate and possess in addition an (R)-enoyl-CoA hydratase (phaJ), suggesting that (R)-3-hydroxybutyryl-CoA is the starting point for PHB synthesis, whereas the (S)-isomer is used for butyrate formation
physiological function
-
recombinant Escherichia coli expressing PHA synthase from Bacillus cereus shows a reduction of the molecular weight of PHA produced during the stationary phase of growth. Its carboxy end structure is capped by ethanol, as the result of alcoholytic cleavage of PHA chains by PhaRC induced by endogenous ethanol. This scission reaction is also induced by exogenous ethanol in both in vivo and in vitro assays. In addition, PhaRC has alcoholysis activity for PHA chains synthesized by other synthases
-
physiological function
-
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
-
physiological function
Cupriavidus necator 17699
-
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
-
physiological function
-
enzyme is able to produce poly(3-hydroxybutyrate) in recombinant Cupriavidus necator PHB-negative mutant under the control of the phaC1 promoter from Cupriavidus necator H16
-
physiological function
Hydrogenophilus thermoluteolus DSM 6765
-
poly-beta-hydroxybutyrate accumulation in the moderately thermophilic hydrogen-oxidizing bacterium Hydrogenophilus thermoluteolus TH-1 by induction of the poly-beta-hydroxybutyrate (PHB) synthesis pathway enzymes, including the PHB synthase. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
-
physiological function
-
gene expression in a Cupriavidus necator polyhydroxyalkanoate-negative mutant results in the accumulation of significant amount of polyhydroxyalkanoate
-
physiological function
-
species that do contain type III PHA synthases (phaEC) are able to produce butyrate and possess in addition an (R)-enoyl-CoA hydratase (phaJ), suggesting that (R)-3-hydroxybutyryl-CoA is the starting point for PHB synthesis, whereas the (S)-isomer is used for butyrate formation
-
physiological function
-
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs)
-
physiological function
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
class I PHB synthase, PhaC, from Ralstonia eutropha catalyzes the formation of PHB from (R)-3-hydroxybutyryl-CoA, ultimately resulting in the formation of insoluble granules, the polymer elongation rate is much faster than the initiation rate
-
physiological function
-
poly-beta-hydroxybutyrate accumulation in the moderately thermophilic hydrogen-oxidizing bacterium Hydrogenophilus thermoluteolus TH-1 by induction of the poly-beta-hydroxybutyrate (PHB) synthesis pathway enzymes, including the PHB synthase. Among these synthetic genes, polyhydroxyalkanoate synthase (phbC) is the key enzyme for the polymerization
-
physiological function
-
P(3HB) synthase catalyzes polymerization of the 3-hydroxybutyryl-CoA monomers, Pseudomonas sp. USM 4-55 is a soil isolated bacterium that possesses the ability to produce polyhydroxyalkanoates consisting of both poly(3-hydroxybutyrate) homopolymer and medium-chain length monomers (6 to 14 carbon atoms) when sugars or fatty acids are utilized as the sole carbon source
-
physiological function
Hydrogenophaga pseudoflava NBRC-102513
-
PHA synthase is the critical enzyme in polyhydroxyalkanoates (PHA) biosynthesis, and R-3-hydroxyacyl-coenzyme A (CoA) is the substrate. Poly-3-hydroxybutyrate (P3HB) is one type of PHA produced by many bacteria
-
additional information
-
comparison of P(3HB) biosynthesis by recombinant Cupriavidus necator PHB-4 harboring the synthase gene of Cupriavidus sp. USMAA2-4 from various plant oils
additional information
in the class II PhaC1 from Pseudomonas sp. 61-3 (PhaC1Ps), Ser325 stabilizes the catalytic cysteine through hydrogen bonding. Another residue, Gln508 of PhaC1Ps is located in a conserved hydrophobic pocket which is next to the catalytic Asp and His. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
-
residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the Balpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. Closed form PhaCCs-CAT blocks the substrates from entering the catalytic pocket by covering the active site within the CAP subdomain, in particular, a short stretch of highly dynamic amino acids named LID region. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
-
structure comparisons and structure-function relationship of PhaCs, overview. Phe362 and Phe518 of PhaC from Aeromonas caviae (PhaCAc) are assisting the dimer formation and maintaining the integrity of the core beta-sheet, respectively. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
the region Leu402-Asn415 forming the alpha4-helix in PhaCCn-CAT is conserved among Class I and II PHA synthases, whereas the corresponding segment, Leu369-Lys382 of PhaCCs-CAT, displays a disordered structure. Catalytic mechanism, overview
additional information
-
residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
-
additional information
Cupriavidus necator 17699
-
residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
-
additional information
-
residue Ala510 of PhaCCn is near catalytic His508 and may be involved in the open-close regulation, which presumably play an important role in substrate specificity and activity. Class I/II-conserved Phe420 of PhaCCn is one of the residues involved in dimerization. Structure comparisons and structure-function relationship of PhaCs, overview. A flexible CAP subdomain is observed covering the alpha/beta core subdomain from the top. The conformation of the CAP subdomain is the key indicator of the enzyme's active status. A short stretch of highly dynamic amino acids named LID region in the partially opened PhaCCn-CAT undergoes structural changes to allow substrate entry. The catalytic triad residues come together in the core, forming a catalytic pocket, indicating the involvement of the catalytic triad in the catalysis. Ala510 of PhaCCn and its corresponding residues in other PhaCs are important in regulating the enzymes' substrate specificities
-
additional information
-
comparison of P(3HB) biosynthesis by recombinant Cupriavidus necator PHB-4 harboring the synthase gene of Cupriavidus sp. USMAA2-4 from various plant oils
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2Z6DVS4_HYDTE
610
0
69119
TrEMBL
-
A0A2Z6DWT1_HYDTE
570
0
64457
TrEMBL
-
B7KDE2_GLOC7
Gloeothece citriformis (strain PCC 7424)
364
0
41639
TrEMBL
-
G0LKV7_HALWC
Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23)
184
0
20853
TrEMBL
-
H6VX88_PSEAI
559
0
62582
TrEMBL
other Location (Reliability: 2)
O87110_DELAC
630
0
69069
TrEMBL
other Location (Reliability: 1)
PHAC_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
589
0
64317
Swiss-Prot
-
PHAC_ALLVD
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
355
0
39775
Swiss-Prot
-
Q9F4K5_CAUVI
587
0
64888
TrEMBL
other Location (Reliability: 4)
Q9F5P9_ECTSH
371
0
42049
TrEMBL
Secretory Pathway (Reliability: 3)
PHAC_CHRVO
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
568
0
63270
Swiss-Prot
-
U7P2T8_9GAMM
599
0
67973
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40600
41700
64000
66000
-
x * 66000, (His)6-tagged wild-type and G4D mutant PhaCRe, SDS-PAGE
40600
3 * 41700 (PhaE) + 3 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE
40600
6 * 41700 (PhaE) + 6 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE
41700
3 * 41700 (PhaE) + 3 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE
41700
6 * 41700 (PhaE) + 6 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
6 * 41700 (PhaE) + 6 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE
hexamer
3 * 41700 (PhaE) + 3 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE
monomer
additional information
dimer
-
homodimer is the active form of the enzyme. Two identical thiol groups from C319 residues on each subunit of the homodimer are required to form the catalytic site for the initiation and propagation reactions. A dimer synthase that has initiated the polymerization reaction (primed synthase) is significantly more stable against dissociation than the unprimed (unreacted) dimer synthase
dimer
-
it is suggested that a dimeric form of the enzyme is involved in elongation
additional information
-
Phe362 and Phe518 of PhaC from Aeromonas caviae (PhaCAc) are assisting the dimer formation and maintaining the integrity of the core beta-sheet, respectively. Structure analysis and comparison. Monomer-dimer equilibration of PhaC
additional information
-
the synthase is composed of a 1:1 mixture of two subunits, PhaC and PhaE. Size-exclusion chromatography indicates that in solution PhaC and PhaE exist as large molecular weight aggregates. The PhaC-(His)6 protein catalyzes polymerization with a specific activity of 0.9 unit/mg. The PhaE-(His)6 protein is inactive. Addition of PhaE-(His)6 to PhaC-(His)6 increases the activity several 100fold
additional information
structure analysis and comparison. Domain organization of class I PhaCCs from Chromobacterium sp. USM2. Monomer-dimer equilibration of PhaC
additional information
structure analysis and comparison. Domain organization of class I PhaCCn from Cupriavidus necator. Monomer-dimer equilibration of PhaC
additional information
-
structure analysis and comparison. Domain organization of class I PhaCCn from Cupriavidus necator. Monomer-dimer equilibration of PhaC
additional information
Cupriavidus necator 17699
-
structure analysis and comparison. Domain organization of class I PhaCCn from Cupriavidus necator. Monomer-dimer equilibration of PhaC
-
additional information
-
structure analysis and comparison. Domain organization of class I PhaCCn from Cupriavidus necator. Monomer-dimer equilibration of PhaC
-
additional information
-
structure analysis and comparison. Domain organization of class I PhaCCn from Cupriavidus necator. Monomer-dimer equilibration of PhaC
-
additional information
I3R9Z3; I3R9Z4
PHA synthase is composed of PhaC and PhaE subunits
additional information
-
PHA synthase is composed of PhaC and PhaE subunits
additional information
Classes I and II PHA synthases are formed by a single protein (PhaC), of about 60 kDa
additional information
Classes I and II PHA synthases are formed by a single protein (PhaC), of about 60 kDa
additional information
Classes I and II PHA synthases are formed by a single protein (PhaC), of about 60 kDa
additional information
Classes I and II PHA synthases are formed by a single protein (PhaC), of about 60 kDa
additional information
structure analysis and comparison. Monomer-dimer equilibration of PhaC
additional information
Classes I and II PHA synthases are formed by a single protein (PhaC), of about 60 kDa
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
sequence has potential N-glycosylation, myristoylation, protein kinase C and casein kinase II type phosphorylation domains
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain, vapor diffusion method, using 50 mM Bis-Tris (pH 5.5), 60 mM ammonium sulfate and 5% (w/v) PEG4000. Full-length enzyme, vapor diffusion method, using 0.2 M lithium sulfate, 0.1 M Bis-Tris (pH 6.5) and 25% (w/v) PEG3350
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D171G
-
the mutation leads to an 8-10fold increase in polyhydroxyalkanoate content in the T1 transgenic Arabidopsis thaliana, compared to plants harboring the wild type enzyme gene
D459V/A513C
-
the mutant shows a 1.1fold increase in specific enzyme activity and polyhydroxyalkanoate accumulation increases by 26% as compared with the wild type enzyme
F326I/F518I
-
the mutant shows a 1.06fold increase in specific enzyme activity and polyhydroxyalkanoate accumulation increases by 11% as compared with the wild type enzyme
F362I/F518I
-
the double mutation of Phe362Ile and Phe518Ile of PhaCAc causes a 6% increment in the specific synthase activity and an 11% increment of PHA accumulation compared to wild-type synthase
F518I
N149S
-
the mutation leads to an 8-10fold increase in polyhydroxyalkanoate content in the T1 transgenic Arabidopsis thaliana, compared to plants harboring the wild type enzyme gene
S103C/F518I
-
the mutant shows a decrease in specific enzyme activity (to 74%) and polyhydroxyalkanoate accumulation decreases by 45% as compared with the wild type enzyme
V214G
-
the mutant shows a 2.16fold increase in specific enzyme activity and polyhydroxyalkanoate accumulation increases by 7% as compared with the wild type enzyme
C130A
C130S
-
121% of wild-type activity in the initial phase of reaction, 16% of wild-type activity in tghe second phase of reaction
C149S
-
0.1% of wild-type activity in the initial phase of reaction, 0.09% of wild-type activity in tghe second phase of reaction
D302A
-
incubation of D302A-PhaCPhaE with [14C]-hydroxybutanoyl-CoA results in detection of oligomeric HBs covalently bound to PhaC, at hydroxybutanoyl-CoA to enzyme ratios between 5 and 100
D302N
-
0.012% of wild-type activity in the initial phase of reaction, 0.29% of wild-type activity in tghe second phase of reaction
H303Q
-
0.25% of wild-type activity in the initial phase of reaction, 1.6% of wild-type activity in tghe second phase of reaction
H331Q
-
51% of wild-type activity in the initial phase of reaction, 73% of wild-type activity in tghe second phase of reaction
A479S
A510S
mutant is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
A510X
mutation corresponds to position 481 in the class II lactate polymerizing polyhydroxyalkanoate synthase PhaC1PsSTQK, in which Gln481Lys is essential to its lactate polymerizing activity. Among 19 A510X mutants, 15 synthesize lactate-3-hydroxybutanoate copolymers
C319A
F396L
-
about 40% of the poly(3-hydroxybutyrate) content compared to wild-type
F420S
-
F420S enzyme has a significant decrease in its lag phase compared to that of the wild-type enzyme. Poly(3-hydroxybutyrate) content is about 85% of wild-type value
G4A
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 14% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4C
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 24% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4D
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 58% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4D/F420S
-
mutant shows a higher poly(3-hydroxybutyrate) content and in vivo concentration of PhaCRe enzyme than the F420S mutant, the molecular weight of the poly(3-hydroxybutyrate) polymer of the double mutant is similar to that of the F420S mutant
G4E
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 58% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4F
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 45% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4H
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4I
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4K
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 58% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4L
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 2% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4M
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 24% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4N
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 57% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4P
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 54% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4Q
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 55% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4R
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 54% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4S
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4T
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 56% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has rather similar molecular weights with that of the wild-type
G4V
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 12% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4W
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 13% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
G4Y
-
poly(3-hydroxybutyrate) content of Escherichia coli harboring mutant PhaCRe is 54% of Ralstonia eutropha wild-type value. Poly(3-hydroxybutyrate) produced by mutant has higher molecular weights with that of the wild-type
N208D
-
about 40% of the poly(3-hydroxybutyrate) content compared to wild-type
A510S
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
mutant is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
-
A510X
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
mutation corresponds to position 481 in the class II lactate polymerizing polyhydroxyalkanoate synthase PhaC1PsSTQK, in which Gln481Lys is essential to its lactate polymerizing activity. Among 19 A510X mutants, 15 synthesize lactate-3-hydroxybutanoate copolymers
-
E130D/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
Q482K
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
S326T
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
S326T/Q482K
site-directed mutagenesis, the double mutant grown on nonanoic acid in Pseudomonas putida strain GPp104 or grown on valeric acid in Ralstonia eutropha strain PHB-4 shows a 2.5fold higher copolymer content with 3.8fold increased 3-hydroxyalkanoate fraction compared to wild-type
Q482K
-
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
-
S326T
-
site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type
-
S326T/Q482K
-
site-directed mutagenesis, the double mutant grown on nonanoic acid in Pseudomonas putida strain GPp104 or grown on valeric acid in Ralstonia eutropha strain PHB-4 shows a 2.5fold higher copolymer content with 3.8fold increased 3-hydroxyalkanoate fraction compared to wild-type
-
E130D/S325T/S477G/Q481K
E130D/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
L484V
-
mutation remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis
Q481M
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
S482G
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
L484V
Pseudomonas putida GPo1 / ATCC29347
-
mutation remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis
-
Q481M
Pseudomonas putida GPo1 / ATCC29347
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
-
S482G
Pseudomonas putida GPo1 / ATCC29347
-
mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
-
E130D/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D/S325T/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D/S325T/S477G/Q481K
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
E130D/S477F/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D/S325T/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D/S325T/S477G/Q481K
E130D/S477F/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D
-
recombinant Escherichia coli strain JM109 harboring the E130D mutant gene accumulates 10fold higher (1.0 wt%) poly(3-hydroxybutyrate) from glucose, compared to recombinant Escherichia coli harboring the wild-type PHA synthase gene (0.1 wt%). Recombinant Escherichia coli strain LS5218 harboring the E130D PHA synthase gene grown on dodecanoate produces more poly(3-hydroxybutanoate-co-3-hydroxyalkanoate) (20 wt%) copolymer than an LS5218 strain harboring the wild-type PHA synthase gene (13 wt%). The E130D mutation also results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase. Mutation results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase. In vitro enzyme activities of the E130D PHA synthase toward various 3-hydroxyacyl-CoAs (4-10 carbons in length) are all higher than those of the wild-type enzyme. Mutation decreases the molecular weight of poly(3-hydroxybutyrate)
E130D/Q481K
E130D/Q481M
-
the double mutant shows much higher poly(3-hydroxybutyrate) accumulation (29-34 wt%) compared to poly(3-hydroxybutyrate) accumulation in cells harboring PHA synthase with the individual mutations E130D or Q481M alone
E130D/Q481R
-
the double mutant shows much higher poly(3-hydroxybutyrate) accumulation (29-34 wt%) compared to poly(3-hydroxybutyrate) accumulation in cells harboring PHA synthase with the individual mutations E130D or Q481R alone
E130D/S325C
-
the double mutants of E130D with either the S325T or the S325C mutations exhibits strong synergistic increases in poly(3-hydroxybutyrate) content, up to 39 wt%
E130D/S325T
-
the double mutants of E130D with either the S325T or the S325C mutations exhibits strong synergistic increases in poly(3-hydroxybutyrate) content, up to 39 wt%
E130D/S325T/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
E130D/S477F/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
Q481K
Q481K/Q508L
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Q481M
Q481M/Q508L
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Q481R
Q481R/Q508L
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Q508L
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
S325T
S325T/Q481K
-
S325T mutation decreases the molecular weight of poly(3-hydroxybutyrate). If the mutation is combined with the Q481K mutation, the enzyme can produce poly(3-hydroxybutyrate) with higher molecular weight
S325T/Q508L
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
S477R
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
S477R/Q508L
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
E130D/S477R
-
the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 27 wt %) and an alteration of substrate specificity
Q481K
in class II PhaC1Ps, the mutations Gln481Met/Lys/Arg allow the incorporation of non-native substrates, such as smaller 3-hydroxybutyrate fractions into the copolymer
Q481M
in class II PhaC1Ps, the mutations Gln481Met/Lys/Arg allow the incorporation of non-native substrates, such as smaller 3-hydroxybutyrate fractions into the copolymer
Q481R
in class II PhaC1Ps, the mutations Gln481Met/Lys/Arg allow the incorporation of non-native substrates, such as smaller 3-hydroxybutyrate fractions into the copolymer
S325C
the mutation causes a significant increase in the incorporation of short-chain-length (SCL) in the PHA synthesized
S325C/S477R
-
the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 21 wt %) and an alteration of substrate specificity
S325T
the mutation causes a significant increase in the incorporation of short-chain-length (SCL) in the PHA synthesized
S325T/Q481K
the mutat shows significantly increased incorporation of short-chain-length (SCL) substrates in the polymer synthesized by class II PhaCs
S325T/S477R
-
the double mutant exhibits synergistic effects on both an increase in polyhydroxyalkanoate production (from 9 wt % to 17 wt %) and an alteration of substrate specificity
S477A
-
the mutation results in a shift in substrate specificity to smaller monomer units
S477F
-
the mutation results in a shift in substrate specificity to smaller monomer units
S477G
S477H
-
the mutation results in a shift in substrate specificity to smaller monomer units
S477R
S477R/Q481K
-
the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 1 wt %) and an alteration of substrate specificity
S477R/Q481M
-
the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 6 wt %) and an alteration of substrate specificity
S477R/Q481R
-
the double mutant exhibits synergistic effects on both a decrease in polyhydroxyalkanoate production (from 9 wt % to 0.2 wt %) and an alteration of substrate specificity
S477Y
-
the mutation results in a shift in substrate specificity to smaller monomer units
E130D/S325T/S477G/Q481K
-
engineered polyhydroxybutanoate synthase able to accept 2-hydroxyacyl-CoAs as substrates
-
S324T/Q480K
-
the mutant shows increased activity compared to the wild type enzyme
S326T/Q482K
additional information
F518I
-
in broad-range class I PhaCAc, mutation of Phe518Ile increases the relative activity to 480% in the in vitro synthase activity assay, and 120% in the in vivo PHA accumulation
F518I
-
the mutant shows a 4.8fold increase in specific enzyme activity, whereas the corresponding mediated polyhydroxyalkanoate accumulation increases by 20%, as compared with the wild type enzyme
C130A
-
89% of wild-type activity in the initial phase of reaction, 39% of wild-type activity in tghe second phase of reaction
A479S
site-directed mutagenesis, while mutant A479S-PhaCCs displays the same order as the wild-type enzyme with regard to chain length, it exhibits higher activity for both HBCoA and HVCoA and lower activity for HHxCoA compared to wild-type
A479S
the mutant shows an increased activity towards short-chain length (SCL) PHA, but a decreased activity towards medium-chain length (MCL) PHA
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S325T/S477G/Q481K
the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S325T/S477G/Q481K
-
the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
-
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
-
E130D/S325T/S477G/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
-
E130D/S325T/S477G/Q481K
-
site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
-
E130D/Q481K
-
E130D mutation decreases the molecular weight of poly(3-hydroxybutyrate). If the mutation is combined with the Q481K mutation, the enzyme can produce poly(3-hydroxybutyrate) with higher molecular weight
E130D/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
site-directed mutagenesis, the mutation leads to production of high molecular weights of P(3HB-co-LA)
E130D/S325T/S477G/Q481K
site-directed mutagenesis, the type II PHA synthase 1 is engineered to accept short-chain-length hydroxyacyl-CoAs including lactyl-CoA and 3-hydroxybutyryl-CoA as substrates and support the synthesis of P(3HB-co-LA) by site-directed mutagenesis of four sites, i.e. E130, S325, S477, and Q481
E130D/S325T/S477G/Q481K
-
engineered polyhydroxybutanoate synthase able to accept 2-hydroxyacyl-CoAs as substrates
Q481K
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Q481M
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
Q481R
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
S325T
-
site-directed mutagenesis, the mutant shows an altered substrate specificity shifted to short-chain acyl-CoAs, corresponding to the reaction of a type I PHA synthase, compared to the wild-type enzyme, which is more specific for medium-chain substrates as a type II PHA synthase
S477G
the mutant of PhaC1Ps shows enhancement in the in vitro activity with both short-chain-length (SCL) and medium-chain-length (MCL) substrates
S477G
-
the mutation greatly enhances activity toward all different sizes of substrates with carbon numbers ranging from 4 to 12
S477R
-
the mutation contributes to a shift in substrate specificity to smaller monomers containing a 3-hydroxybutyrate unit rather than to an enhancement in catalytic activity
S477R
-
the mutation results in a shift in substrate specificity to smaller monomer units
S326T/Q482K
-
the mutations increase the enzyme substrate specificity toward 3-hydroxybutyrate enhance synthase activity for more PHA production
S326T/Q482K
-
the mutations increase the enzyme substrate specificity toward 3-hydroxybutyrate enhance synthase activity for more PHA production
-
additional information
engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Valine supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview
additional information
-
engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Valine supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview
additional information
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
additional information
-
mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes
additional information
-
the enzyme is used for in vitro synthesis of polyhydroxyalkanoates on a hydrophobic support, i.e. highly oriented pyrolytic graphite. Using PhaECAv and 3-hydroxyoctanoyl-CoA at room temperature, a poly(3-hydroxyoctanoate) [P(3HO)] film is formed on the hydrophobic support with a thickness of a few nanometers, as revealed by atomic force microscopy
additional information
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
additional information
-
deletion of 13 amino acids from the C-terminus greatly affects the catalytic activity of the enzyme, retaining 1.1-7.4% of the total activity
additional information
construction of enzyme hybrids of PhaC from Bacillus megaterium and Bacillus cereus, i.e. PhaRBmCYB4 and PhaRYB4CBm. The molecular weight of P(3HB) synthesized by PhaRCYB4 decreased with increasing culture time and temperature, time-dependent behavior is observed for hybrid synthase PhaRBmCYB4, but not for PhaRYB4CBm, thus the molecular weight change is caused by the PhaCYB4 subunit
additional information
-
construction of enzyme hybrids of PhaC from Bacillus megaterium and Bacillus cereus, i.e. PhaRBmCYB4 and PhaRYB4CBm. The molecular weight of P(3HB) synthesized by PhaRCYB4 decreased with increasing culture time and temperature, time-dependent behavior is observed for hybrid synthase PhaRBmCYB4, but not for PhaRYB4CBm, thus the molecular weight change is caused by the PhaCYB4 subunit
additional information
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
additional information
-
construction of enzyme hybrids of PhaC from Bacillus megaterium and Bacillus cereus, i.e. PhaRBmCYB4 and PhaRYB4CBm. The molecular weight of P(3HB) synthesized by PhaRCYB4 decreased with increasing culture time and temperature, time-dependent behavior is observed for hybrid synthase PhaRBmCYB4, but not for PhaRYB4CBm, thus the molecular weight change is caused by the PhaCYB4 subunit
-
additional information
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
additional information
mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes. Beneficial mutations displayed on PhaCCs-CAT, structure, overview
additional information
A0A1E8EW93; A0A1E8EW64
anaerobic production of the biopolymer poly(3-hydroxybutyrate) (PHB) and the monomer 3-hydroxybutyrate (3-HB) is achieved using recombinant clostridial acetogens supplied with syn-(thesis) gas as the sole carbon and energy source. 3-HB production is successfully accomplished by a synthetic pathway containing the genes thlA (encoding thiolase A), ctfA/B (encoding CoA-transferase A/B), and bdhA (encoding (R)-3-hydroxybutyrate dehydrogenase). The respective recombinant Clostridium coskatii [p83_tcb] strain produces autotrophically and heterotrophically 3-HB. As a proof of concept, production of PHB is achieved using recombinant Clostridium coskatii and Clostridium ljungdahlii strains expressing a synthetic PHB pathway containing the genes thlA (encoding thiolase A), hbd (encoding 3-hydroxybutyryl-CoA dehydrogenase), crt (encoding crotonase), phaJ (encoding (R)-enoyl-CoA hydratase), and phaEC (encoding PHA synthase). The strain Clostridium coskatii [p83_PHB_Scaceti] synthesizes heterotrophically 3.4% PHB per cell dry weight (CDW) and autotrophically 1.12% PHB per CDW
additional information
-
anaerobic production of the biopolymer poly(3-hydroxybutyrate) (PHB) and the monomer 3-hydroxybutyrate (3-HB) is achieved using recombinant clostridial acetogens supplied with syn-(thesis) gas as the sole carbon and energy source. 3-HB production is successfully accomplished by a synthetic pathway containing the genes thlA (encoding thiolase A), ctfA/B (encoding CoA-transferase A/B), and bdhA (encoding (R)-3-hydroxybutyrate dehydrogenase). The respective recombinant Clostridium coskatii [p83_tcb] strain produces autotrophically and heterotrophically 3-HB. As a proof of concept, production of PHB is achieved using recombinant Clostridium coskatii and Clostridium ljungdahlii strains expressing a synthetic PHB pathway containing the genes thlA (encoding thiolase A), hbd (encoding 3-hydroxybutyryl-CoA dehydrogenase), crt (encoding crotonase), phaJ (encoding (R)-enoyl-CoA hydratase), and phaEC (encoding PHA synthase). The strain Clostridium coskatii [p83_PHB_Scaceti] synthesizes heterotrophically 3.4% PHB per cell dry weight (CDW) and autotrophically 1.12% PHB per CDW
-
additional information
-
deleting the first 60 or 78 amino acid residues results in approximately 60% PHB accumulation, similar to that of the recombinant harboring wild-type phbCRe gene, while negligible, polyhydroxybutyrate is accumulated in the recombinant harboring the plasmid encoding PhbCRe with a deletion of N-terminal 88- or 98-amino acid residues. Polyhydroxybutyrate polymerized by mutant PhbCRe with a deletion of N-terminal 78 amino acid residues shows much higher molecular weight compared with that of the wild-type. Polyhydroxybutyrate synthase from Ralstonia eutropha with a deletion on N-terminal 88 amino acid residues shows a significant reduced activity, as reflected by only 1.5% polyhydroxybutyrate accumulation compared with the wild type which produces 58.4% polyhydroxybutyrate of the cell dry weight
additional information
-
fusion proteins composed of an N-terminal class II PHA synthase region (PhaCPa from Pseudomonas aeruginosa) and a C-terminal class I PHA synthase region (PhaCRe from Ralstonia eutropha) are constructed
additional information
engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Val supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview
additional information
-
engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Val supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview
additional information
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
additional information
mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes
additional information
-
mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes
additional information
translationally fusing a target protein to PHA synthase using a self-cleaving intein as linker, intracellular production of PHA beads is achieved. Upon isolation of respective PHA beads the soluble pure target protein is released by a simple pH shift to pH 6.0. The utility of this approach is exemplified by producing six target proteins, including Aequorea victoria green fluorescent protein (GFP), Mycobacterium tuberculosis vaccine candidate Rv1626, the immunoglobulin G (IgG) binding ZZ domain of protein A derived from Staphylococcus aureus, human tumor necrosis factor alpha (TNFalpha), human granulocyte colony-stimulating factor (G-CSF), and human interferon alpha 2beta (IFNalpha2beta)
additional information
Cupriavidus necator 17699
-
mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes
-
additional information
-
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
-
additional information
-
engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Val supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview
-
additional information
-
translationally fusing a target protein to PHA synthase using a self-cleaving intein as linker, intracellular production of PHA beads is achieved. Upon isolation of respective PHA beads the soluble pure target protein is released by a simple pH shift to pH 6.0. The utility of this approach is exemplified by producing six target proteins, including Aequorea victoria green fluorescent protein (GFP), Mycobacterium tuberculosis vaccine candidate Rv1626, the immunoglobulin G (IgG) binding ZZ domain of protein A derived from Staphylococcus aureus, human tumor necrosis factor alpha (TNFalpha), human granulocyte colony-stimulating factor (G-CSF), and human interferon alpha 2beta (IFNalpha2beta)
-
additional information
-
mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes
-
additional information
-
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
-
additional information
-
engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Val supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview
-
additional information
-
translationally fusing a target protein to PHA synthase using a self-cleaving intein as linker, intracellular production of PHA beads is achieved. Upon isolation of respective PHA beads the soluble pure target protein is released by a simple pH shift to pH 6.0. The utility of this approach is exemplified by producing six target proteins, including Aequorea victoria green fluorescent protein (GFP), Mycobacterium tuberculosis vaccine candidate Rv1626, the immunoglobulin G (IgG) binding ZZ domain of protein A derived from Staphylococcus aureus, human tumor necrosis factor alpha (TNFalpha), human granulocyte colony-stimulating factor (G-CSF), and human interferon alpha 2beta (IFNalpha2beta)
-
additional information
-
mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes
-
additional information
-
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
-
additional information
-
engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Val supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview
-
additional information
-
translationally fusing a target protein to PHA synthase using a self-cleaving intein as linker, intracellular production of PHA beads is achieved. Upon isolation of respective PHA beads the soluble pure target protein is released by a simple pH shift to pH 6.0. The utility of this approach is exemplified by producing six target proteins, including Aequorea victoria green fluorescent protein (GFP), Mycobacterium tuberculosis vaccine candidate Rv1626, the immunoglobulin G (IgG) binding ZZ domain of protein A derived from Staphylococcus aureus, human tumor necrosis factor alpha (TNFalpha), human granulocyte colony-stimulating factor (G-CSF), and human interferon alpha 2beta (IFNalpha2beta)
-
additional information
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
additional information
construction of enzyme hybrids of PhaC from Bacillus megaterium and Bacillus cereus, i.e. PhaRBmCYB4 and PhaRYB4CBm. The molecular weight of P(3HB) synthesized by PhaRCYB4 decreased with increasing culture time and temperature, time-dependent behavior is observed for hybrid synthase PhaRBmCYB4, but not for PhaRYB4CBm, thus the molecular weight change is caused by the PhaCYB4 subunit
additional information
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construction of enzyme hybrids of PhaC from Bacillus megaterium and Bacillus cereus, i.e. PhaRBmCYB4 and PhaRYB4CBm. The molecular weight of P(3HB) synthesized by PhaRCYB4 decreased with increasing culture time and temperature, time-dependent behavior is observed for hybrid synthase PhaRBmCYB4, but not for PhaRYB4CBm, thus the molecular weight change is caused by the PhaCYB4 subunit
additional information
establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview
additional information
-
construction of enzyme hybrids of PhaC from Bacillus megaterium and Bacillus cereus, i.e. PhaRBmCYB4 and PhaRYB4CBm. The molecular weight of P(3HB) synthesized by PhaRCYB4 decreased with increasing culture time and temperature, time-dependent behavior is observed for hybrid synthase PhaRBmCYB4, but not for PhaRYB4CBm, thus the molecular weight change is caused by the PhaCYB4 subunit
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additional information
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the enzyme is used for in vitro synthesis of polyhydroxyalkanoates on a hydrophobic support, i.e. highly oriented pyrolytic graphite. Using PhaC1Pp and 3-hydroxyoctanoyl-CoA at room temperature, a poly(3-hydroxyoctanoate) [P(3HO)] film is formed on the hydrophobic support with a thickness of a few nanometers, as revealed by atomic force microscopy
additional information
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sequences derived from SNARE domains efficiently target and integrate the poly-3-hydroxyalkanoate synthase from Pseudomonas putida CA-3 to the membrane of secretory vesicles in Saccharomyces cerevisiae
additional information
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sequences derived from SNARE domains efficiently target and integrate the poly-3-hydroxyalkanoate synthase from Pseudomonas putida CA-3 to the membrane of secretory vesicles in Saccharomyces cerevisiae
-
additional information
the double mutations of Ser325X and Gln481X show further increments in the production of P(3HB), up by 340 to 400fold higher than the wild-type. Mutation of Phe333 may directly impact the geometry of the catalytic Asp447 in the dimer. Since Phe333 and His448 are highly conserved in class I and II PhaC, it is highly possible that this architecture is shared among synthases from different classes
additional information
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recombinant phaC-deficient Cupriavidus necator expressing the enzyme is able to accumulate PHA homopolymers and copolymers including poly(3-hydroxybutyrate) [P(3HB)], poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [P(3HB-co-3HV)], poly(3-hydroxybutyrate-co-5-hydroxyvalerate) [P(3HB-co-5HV)], poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)], poly(3-hydroxybutyrate-co-3-hydroxy-4-methylvalerate) [P(3HB-co-3H4MV)], and poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) [P(3HB-co-3HHx)], when suitable precursors are provided
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 37
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purified PHA synthase exhibits no significant loss of specific activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of specific activity of the PHA synthase is observed during purification at 4°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-cellulose column chromatography, Cibacron Blue column chromatography, omega-amino octyl-agarose column chromatography, and hydroxyapatite column chromatography
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each subunit was cloned, expressed, and purified as a (His)6-tagged construct
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HisTrap column chromatography
HiTrap Q anion-exchange column chromatography, Ni-NTA agarose column chromatography, and Superdex 200 gel filtration
Ni-NTA agarose column chromatography, and HiTrap Q anion-exchange column chromatography
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recombinant His-tagged PhaC1Pp from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged PhaECAv from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
recombinant N-terminally Strep2-tagged PhaC from Ralstonia eutropha by affinity chromatography. Strep2-PhaCRe co-purifies with the phasin protein, PhaP1, and with soluble polyhydroxybutyrate of 350 kDa MW in a high-molecular weight complex and in monomeric/dimeric forms with no associated PhaP1 or polyhydroxybutyrate
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recombinantly expressed in Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
28 strains belonging to 15 genera in the family Halobacteriaceae, sequence comparisons, phylogenetic analysis, overview
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a central region of the phaC gene of Cyanothece sp. strain PCC 8303 is cloned, sequenced and heterologously expressed in Escherichia coli
a synthetic operon for polyhydroxyalkanoate biosynthesis designed to yield high levels of PHA synthase activity in vivo is constructed by positioning a genetic fragment encoding beta-ketothiolase and acetoacetyl-CoA reductase behind a modified synthase gene containing an Escherichia coli promoter and ribosome binding site. Plasmids containing the synthetic operon and the native Alcaligenes eutrophus PHA operon are transformed into Escherichia DH5 alpha and analyzed for polyhydroxybutyrate production. The molecular weight of polymer isolated from recombinant Escherichia coli containing the modified synthase construct is lower than that of the polymer from Escherichia coli containing the native Alcaligenes eutrophus operon. A further decrease in polyester molecular weight is observed with increased induction of the PHA biosynthetic genes in the synthetic operon. Comparison of the enzyme activity levels of PHA biosynthetic enzymes in a strain encoding the native operon with a strain possessing the synthetic operon indicates that the amount of polyhydroxyalkanoate synthase in a host organism plays a key role in controlling the molecular weight and the polydispersity of polymer
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BP-M-CPF4, DNA and amino acid sequence determination and analysis, functional assessment by in vivo PHA biosynthesis in a PHA-negative mutant, recombinant expression in the PHA-negative mutant of Cupriavidus necator under control of phaC1 promoter from Cupriavidus necator, subcloning in Escherichia coli
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cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, functional recombinant heterologous expression in the PHA-negative mutant of Cupriavidus necator PHB-4
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, recombinant expression in the PHA-negative mutant of Cupriavidus necator PHB-4 shows that the enzyme is not functional
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cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, recombinant heterologous expression in the PHA-negative mutant of Cupriavidus necator PHB-4. PHB-4/pBBR1-ProCnJ60 accumulates 18.7% of wild-type polyhydroxybutyrate
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cloning of the gene cluster (phaECHme) encoding a polyhydroxyalkanoate (PHA) synthase in Haloferax mediterranei CGMCC 1.2087 via thermal asymmetric interlaced PCR
I3R9Z3; I3R9Z4
co-expressed with the NADPH-dependent acetoacetyl-CoA reductase gene from Ralstonia eutropha in Arabidopsis thaliana
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co-expression of PhaC with acetoacetyl-CoA synthetase, AACS, from Streptomyces sp. CL190 in Escherichia coli and Corynebacterium glutamicum leading to enhanced production of polyhydroxybutanoates, by cloning the AACS gene into the phaABC operon of Ralstonia eutropha
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construction of (His)6-tagged Ralstonia eutropha PHA synthase gene, expression in Escherichia coli
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construction of a recombinant Ralstonia eutropha PHB-4 harboring Aeromonas caviae biosynthesis genes under the control of a promoter for Ralstonia eutropha phb operon (phbRe promoter), and examination of the polyhydroxyalkanoate producing ability of the recombinants from various alkanoic acids as carbon sources. The polymerization step is not the rate-determining one in PHA biosynthesis by Ralstonia eutropha. The molecular weights of poly(3-hydroxybutyrate) produced by the recombinant strains are also independent of the levels of PHA synthase activity
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construction of an N-terminally Strep2-tagged PhaC, Strep2-PhaCRe, and integration into the Ralstonia eutropha genome in place of wild-type phaC and functional expression without a lag phase of CoA release in the enzyme reaction, functional expression of Strep2-PhaCRe in Escherichia coli strain BL21(DE3) showing a lag phase in CoA release
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constructs of phaCDm alone (pBBRMCS-2::phaCDm) and of phaEDmCDm (pBBRMCS-2::phaEDmCDm) in various vectors are obtained and transferred to several strains of Escherichia coli, as well as to the PHA-negative mutants PHB-4 and GPp104 of Ralstonia eutropha and Pseudomonas putida, respectively. In cells of the recombinant strains harboring phaEDmCDm small but significant amounts (up to 1.7% of cell dry matter) of poly(3-hydroxybutyrate) and of PHA synthase activity (up to 1.5 U/mg protein) are detected. Hybrid synthases consisting of PhaCDm and PhaE of Thiococcus pfennigii or Synechocystis sp. strain PCC 6308 are also constructed and are shown to be functionally active
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each subunit was cloned, expressed, and purified as a (His)6-tagged construct
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entire PHA synthase structural gene of Chlorogloeopsis fritschii PCC 6912 is cloned, sequenced and heterologously expressed in Escherichia coli
entire PHA synthase structural gene of Synechococcus sp. strain MA19 is cloned, sequenced and heterologously expressed in Escherichia coli
expressed in Cupriavidus necator strain PHB-4
expressed in Cupriavidus necator strains PHB-4, Re2058 and Re2160 and Escherichia coli Rosetta2 (DE3) cells
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expressed in Escherichia coli JM109 and BL21(DE3) cells
expressed in Escherichia coli JM109 cells
expressed in polyhydroxyalkanoate synthase negative Aeromonas hydrophila mutant CQ4
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expression in Escherichia coli
expression of PhaRCBm, and as hybrid enzyme PhaRYB4CBm with Bacillus cereus YB-4, PhaRCYB4 in Escherichia coli JM109
expression of PhaRCYB4, and as hybrid enzyme PhaRYB4CBm with Bacillus megaterium NBRC15308, PhaRCBm in Escherichia coli JM109
expression of wild-type and mutant enzymes in Escherichai coli altering its content of polyhydroxyalkanoates
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expression of wild-type and mutant enzymes in Escherichia coli altering its content of polyhydroxyalkanoates
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gene phaC
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Aeromonas caviae Pha synthase leads to a high secretory production of 3-hydroxybutyrate and a large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Allochromatium vinosum Pha synthase leads to a veryl low secretory production of 3-hydroxybutyrate and a moderate amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type BW25113 strain. In the mutant BW25113 strain, the relative amount of oligomers is reduced compared to wild-type. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Bacillus cereus Pha synthase leads to a moderate secretory production of 3-hydroxybutyrate and a large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Bacillus megaterium Pha synthase leads to a moderate secretory production of 3-hydroxybutyrate and a very low amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type BW25113 strain. In the mutant BW25113 strain, no oligomers are produced. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Bacillus sp. INT005 Pha synthase leads to a low secretory production of 3-hydroxybutyrate, but a large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Cupriavidus necator Pha synthase leads to very lo secretory production and a very low amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Delftia acidovorans Pha synthase leads to a low secretory production of 3-hydroxybutyrate and a very large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene phaC, recombinant expression of the chimeric mutant enzyme PhaCAR in Escherichia coli
gene phaC, sequence comparisons, phylogenetic analysis
gene phaC1Ps6-19 phylogenetic analysis, expression of phaC1Ps6-19 mutants in Escherichia coli strain XL-1 Blue
gene phaC1Ps6-19, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of mutant E130D/S325T/S477G/Q481K in Escherichia coli strain XL-1 Blue
gene phaCUSMAA2-4, DNA and amino acid sequence determination and analysis, expression in and complementation of mutant Cupriavidus necator PHB-4 deficient in PHA synthesis, expression in Escherichia coli strain S17-1
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gene PhaEC, sequence comparisons, construction of a plasmid with genes encoding thiolase A (thlA), 3-hydroxybutyryl-CoA dehydrogenase (hbd), and crotonase (crt) from Clostridium scatologenes strain ATCC 25775 and (R)-enoyl-CoA hydratase (phaJ) and PHA synthase (phaEC) from Clostridium acetireducens strain DSM 10703 under control of promoter Ppta-ack from Clostridium ljungdahlii strain DSM 13583 into pMTL83151 Clostridium-Escherichia coli shuttle plasmid. The clustered genes thlA, hbd, and crt are initially cloned into pMTL83151, together with Ppta-ack promoter, recombinant expression in Escherichia coli
A0A1E8EW93; A0A1E8EW64
gene phbCPs encoded in the phb operon, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, the genetic organization of phb operon shows a putative promoter region, followed by phbBPs-phbAPs-phbCPs, with phbRPs encoding a putative transcriptional activator that is located in the opposite orientation, upstream of phbBACPs. Heterologous expression of phbCPs from pGEM3ABex vector in Escherichia coli JM109 resulting in P(3HB) accumulation of up to 40% of dry cell weight
in vivo studies on a Wautersia eutropha strain in which the class I synthase gene has been replaced with the D302A-PhaCPhaE gene and the organism examined under PHB production conditions by transmission electron microscopy. Very small granules are observed in contrast to the 200-500 nm granules observed with the wild-type strain
-
mutant enzymes expressed in Escherichia coli
PHA synthase genes (phaC and phaE) are cloned by screening a genomic library for PHA accumulation in Escherichia coli cells
recombinant Escherichia coli strain JM109 harboring the E130D mutant gene accumulates 10fold higher (1.0 wt%) poly(3-hydroxybutyrate) from glucose, compared to recombinant Escherichia coli harboring the wild-type PHA synthase gene (0.1 wt%). Recombinant Escherichia coli strain LS5218 harboring the E130D PHA synthase gene grown on dodecanoate produces more poly(3-hydroxybutanoate-co-3-hydroxyalkanoate) (20 wt%) copolymer than an LS5218 strain harboring the wild-type PHA synthase gene (13 wt%). The E130D mutation also results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase
-
recombinant expression of His-tagged PhaC1Pp in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
recombinant expression of His-tagged PhaECAv in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
recombinant expression of PhaC1P-5 in Pseudomonas putida strain Gp104
recombinant expression of PhaC2P-5 in Pseudomonas putida strain Gp104 or in Ralstonia eutropha strain PHB-4
recombinant expression of the enzyme used as a fusion protein with a self-cleaving intein linker for production of the fused proteins, e.g. Aequorea victoria green fluorescent protein (GFP), Mycobacterium tuberculosis vaccine candidate Rv1626, the immunoglobulin G (IgG) binding ZZ domain of protein A derived from Staphylococcus aureus, human tumor necrosis factor alpha (TNFalpha), human granulocyte colony-stimulating factor (G-CSF), and human interferon alpha 2beta (IFNalpha2beta) in the Escherichia coli system. A pH or thiol inducible intein is employed in combination with PHA beads for target protein production and purification, method evaluation, overview
the phaC coding region is subcloned into vector pBBR1-JO2 under lac promoter control. The resulting plasmid, pQQ4, mediates PHB accumulation in the mutant Ralstonia eutropha PHBN4 and recombinant Escherichia coli JM109(pBHR69)
the wild-type and mutated PHA synthase genes from Aeromonas caviae are introduced into Arabidopsis thaliana together with the NADPH-dependentacetoacetyl-CoA reductase gene from Ralstonia eutropha. Expression of the highly active mutated PHA synthase genes, N149S and D171G, leads to an 8-10fold increase in PHA content in the T1 transgenic Arabidopsis, compared to plants harboring the wild-type PHA synthase gene. In homozygous T2 progenies, PHA content is further increased up to 6.1 mg/g cell dry weight. GC/MS analysis of the purified PHA from the transformants revealed that these PHAs are poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymers consisting of 0.2-0.8 mol% 3-hydroxyvalerate
-
While Chromobacterium violaceum accumulates poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) when grown on a fatty acid carbon source, Klebsiella aerogenes and Ralstonia eutropha (formerly Alcaligenes eutrophus), harboring phaCCv, accumulate poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) and, additionally, poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) when even-chain-length fatty acids are utilized as the carbon source. This finding suggests that the metabolic environments of these organisms are sufficiently different to alter the product range of the Chromobacterium violaceum PHA synthase. Neither recombinant Escherichia coli nor recombinant Pseudomonas putida harboring phaCCv accumulate significant levels of polyhydroxyalkanoic acids
wild-type and (His)6-tagged PhaCRe, expression in Escherichia coli. Wild-type enzyme expressed in Escherichia coli shows 35% of the enzyme from Ralstonia eutropha
-
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping
-
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping
-
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, functional recombinant heterologous expression in the PHA-negative mutant of Cupriavidus necator PHB-4
-
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, functional recombinant heterologous expression in the PHA-negative mutant of Cupriavidus necator PHB-4
-
gene phaC, recombinant expression of the chimeric mutant enzyme PhaCAR in Escherichia coli
gene phaC, recombinant expression of the chimeric mutant enzyme PhaCAR in Escherichia coli
gene phaC1Ps6-19 phylogenetic analysis, expression of phaC1Ps6-19 mutants in Escherichia coli strain XL-1 Blue
-
gene phaC1Ps6-19 phylogenetic analysis, expression of phaC1Ps6-19 mutants in Escherichia coli strain XL-1 Blue
-
gene phaC1Ps6-19 phylogenetic analysis, expression of phaC1Ps6-19 mutants in Escherichia coli strain XL-1 Blue
gene phaC1Ps6-19 phylogenetic analysis, expression of phaC1Ps6-19 mutants in Escherichia coli strain XL-1 Blue
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
poly-beta-hydroxybutyrate (PHB) accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions
poly-beta-hydroxybutyrate (PHB) accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions
poly-beta-hydroxybutyrate (PHB) accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions
Hydrogenophilus thermoluteolus DSM 6765
-
-
poly-beta-hydroxybutyrate (PHB) accumulation is induced by nitrogen limitation under autotrophic as well as heterotrophic conditions
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
synthesis
analysis
deveopment of a phaE biosensor as a a biomarker for microorganisms that contain class III PHA synthase. The phaE biosensor has a high specificity for polyhydroxyalkanoate-producing haloarchaea. The lowest amount of genomic DNA of Haloquadratum walsbyi detected by the biosensor is approximately 250 fg. The phaE biosensor can be applied for screening of polyhydroxyalkanoate-producing haloarchaea from environmental samples
analysis
-
deveopment of a phaE biosensor as a a biomarker for microorganisms that contain class III PHA synthase. The phaE biosensor has a high specificity for polyhydroxyalkanoate-producing haloarchaea. The lowest amount of genomic DNA of Haloquadratum walsbyi detected by the biosensor is approximately 250 fg. The phaE biosensor can be applied for screening of polyhydroxyalkanoate-producing haloarchaea from environmental samples
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biotechnology
recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
biotechnology
-
recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
-
biotechnology
-
recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
-
biotechnology
-
recombinant protein production and purification from Escherichia coli is often accompanied with expensive and complicated procedures, especially for therapeutic proteins. By using an intein cleavable polyhydroxyalkanoate synthase fusion, recombinant proteins can be first produced and sequestered on a natural resin, the polyhydroxyalkanoate (PHA) inclusions, then separated from contaminating host proteins via simple PHA bead isolation steps, and finally purified by specific release into the soluble fraction induced by a pH reduction
-
synthesis
-
usage of the enzyme for recombinant high-level production of poly(3-hydroxybutyrate), P(3HB), in Escherichia coli and Corynebacterium glutamicum. P(3HB) is the natural aliphatic polyester that can be processed into a wide variety of consumer products, including plastics, films and fibers
synthesis
a Cupriavidus necator polyhydroxyalkanoate-negative transformant harboring the polyhydroxyalkanoate synthase gene from bacterium SC8 is able to accumulate 55 weight% of polyhydroxyalkanoate of the cell dry weight when crude palm kernel oil is used as the carbon source. It produces 14 weight% of polyhydroxyalkanoate when 10 g per l of fructose is used
synthesis
-
engineering of an in vivo polylactic acid biosynthesis system in Escherichia coli to synthesize 2-hydroxybutyrate-containing polyhydroxyalkanoate. Propionyl-CoA is used as precursor for 2-ketobutyrate that is converted into 2-hydroxybutyrate-CoA by the sequential actions of Lactococcus lactis (D)-2-hydroxybutyrate dehydrogenase (PanE) and PctCp and then 2-hydroxybutyrate-CoA is polymerized by an engineered PhaC1 from Pseudomonas sp. (mutant E130D/S325T/S477G/Q481K). The recombinant Escherichia coli expressing the system can be grown to 0.66 g/l and successfully produces P(70 mol% 3-hydroxybutyrate-co-18 mol% 3-hydroxybutyrate-co-12 mol% lactate) up to the polyhydroxyalkanoate content of 66 weight% from 20 g/l of glucose, 2 g/l of 3-hydroxybutyrate and 1 g/l of sodium propionate
synthesis
D2Z0B8; D2Z0B6
enzyme shows both polyhydroxyalkanoate polymerization and alcoholysis activities, unsing various alcohols other than ethanol for alcoholysis.. Through the use of bifunctional compounds for alcoholysis, the polyhydroxyalkanoate carboxy terminus can be modified with thiol, alkynyl, hydroxy, and benzyl groups, resulting in the functionalization of the polyhydroxyalkanoate carboxy terminus
synthesis
-
expansion of the substrate specificity and enhancment of biosynthesis of polyhydroxyalkanoate by site-specific mutagenesis. Mutated PhaC1s are coexpressed with beta-ketothiolase and acetoacetyl-CoA reductase to supply sufficient short-chain length (R)-3-hydroxyacyl-CoA as a substrate. Mutation L484V remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis. A single mutation at Q481M, S482G and A547V obviously increases polyhydroxyalkanoate yields. Q481M and S482G enhance the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
synthesis
heterologous expression in Escherichia coli with simultaneous overexpression of chaperone proteins. Compared to expression of synthase alone (14.55 mg per liter), coexpression with chaperones results in the production of larger total quantities of enzyme, including a larger proportion in the soluble fraction. The largest increase is seen when the GroEL/GroES system is coexpressed, resulting in approximately 6fold greater enzyme yields (82.37 mg per liter) than in the absence of coexpressed chaperones. The specific activity of the purified enzyme is unaffected by coexpression with chaperones
synthesis
mutant A510S is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
synthesis
-
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics
synthesis
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics
synthesis
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
synthesis
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that could replace some conventional petroleum-based plastics especially the single use plastics. Class II PhaC1 from Pseudomonas sp. 61-3 (PhaC1Ps) is useful in terms of its broad substrate specificity, and engineering of PhaC1Ps successfully increases its short-chain-length (SCL) incorporation into PHA
synthesis
A0A1E8EW93; A0A1E8EW64
poly(3-hydroxyalkanoates) (PHAs) such as poly(3-hydroxybutyrate) (PHB) are suitable biobased and biodegradable candidates to replace petroleum-based nondegradable plastics. Enzyme PhaEC can be used in its biocatalytic production, PHB production in clostridia, method development and evaluation, overview. The successful transfer and expression of phaJ and phaEC in autotrophic gas-fermenting clostridia leading to PHB formation now opens the possibility to establish an economically viable route to biodegradable plastics from waste and greenhouse gases, as the gas fermentation technology has meanwhile matured and is already performed at industrial scale. A novel metabolic pathway leading to 3-hydroxybutyrate has also been engineered that will allow similarly better economic production of this platform chemical
synthesis
-
replacement of conventional plastics by bioplastics. Polyhydroxyalkanoates (PHA) are bio-polyesters accumulated in cells by a wide range of bacteria. Polyhydroxyalkanoates production from synthetic waste using Pseudomonas palleronii polyhydroxyalkanoate synthase enzyme activity
synthesis
replacement of conventional plastics by bioplastics. Polyhydroxyalkanoates (PHA) are bio-polyesters accumulated in cells by a wide range of bacteria. Polyhydroxyalkanoates production from synthetic waste using Pseudomonas pseudoflava polyhydroxyalkanoate synthase enzyme activity
synthesis
the enzyme mutant S326T/Q482K might be useful for production of distinct polyhydroxyalkanoate copolymers with improved material properties
synthesis
-
the PHA synthase is suitable for the biosynthesis of PHAs that can be used in various biomedical applications due to its ability to incorporate the lipase-degradable monomer sequences of 4-hydroxybutyrate (4HB) and 5-hydroxyvalerate (5HV)
synthesis
the enzyme can be used for polyhydroxyalkanoate production from synthetic wastewater
synthesis
-
enzyme shows both polyhydroxyalkanoate polymerization and alcoholysis activities, unsing various alcohols other than ethanol for alcoholysis.. Through the use of bifunctional compounds for alcoholysis, the polyhydroxyalkanoate carboxy terminus can be modified with thiol, alkynyl, hydroxy, and benzyl groups, resulting in the functionalization of the polyhydroxyalkanoate carboxy terminus
-
synthesis
-
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
-
synthesis
-
the enzyme mutant S326T/Q482K might be useful for production of distinct polyhydroxyalkanoate copolymers with improved material properties
-
synthesis
Cupriavidus necator 17699
-
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
-
synthesis
Pseudomonas putida GPo1 / ATCC29347
-
expansion of the substrate specificity and enhancment of biosynthesis of polyhydroxyalkanoate by site-specific mutagenesis. Mutated PhaC1s are coexpressed with beta-ketothiolase and acetoacetyl-CoA reductase to supply sufficient short-chain length (R)-3-hydroxyacyl-CoA as a substrate. Mutation L484V remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis. A single mutation at Q481M, S482G and A547V obviously increases polyhydroxyalkanoate yields. Q481M and S482G enhance the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation
-
synthesis
-
a Cupriavidus necator polyhydroxyalkanoate-negative transformant harboring the polyhydroxyalkanoate synthase gene from bacterium SC8 is able to accumulate 55 weight% of polyhydroxyalkanoate of the cell dry weight when crude palm kernel oil is used as the carbon source. It produces 14 weight% of polyhydroxyalkanoate when 10 g per l of fructose is used
-
synthesis
-
poly(3-hydroxyalkanoates) (PHAs) such as poly(3-hydroxybutyrate) (PHB) are suitable biobased and biodegradable candidates to replace petroleum-based nondegradable plastics. Enzyme PhaEC can be used in its biocatalytic production, PHB production in clostridia, method development and evaluation, overview. The successful transfer and expression of phaJ and phaEC in autotrophic gas-fermenting clostridia leading to PHB formation now opens the possibility to establish an economically viable route to biodegradable plastics from waste and greenhouse gases, as the gas fermentation technology has meanwhile matured and is already performed at industrial scale. A novel metabolic pathway leading to 3-hydroxybutyrate has also been engineered that will allow similarly better economic production of this platform chemical
-
synthesis
-
biodegradable bio-based polyhydroxyalkanoate (PHA) is gaining much attention as a promising biomaterial that can replace some conventional petroleum-based plastics especially the single use plastics. The most studied class I PhaC from Cupriavidus necator (PhaCCn) is often used as a study model to increase its ability to incorporate medium-chain length (MCL) monomers into PHA
-
synthesis
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
heterologous expression in Escherichia coli with simultaneous overexpression of chaperone proteins. Compared to expression of synthase alone (14.55 mg per liter), coexpression with chaperones results in the production of larger total quantities of enzyme, including a larger proportion in the soluble fraction. The largest increase is seen when the GroEL/GroES system is coexpressed, resulting in approximately 6fold greater enzyme yields (82.37 mg per liter) than in the absence of coexpressed chaperones. The specific activity of the purified enzyme is unaffected by coexpression with chaperones
-
synthesis
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
mutant A510S is able to synthesize a lactate-3-hydroxybutanoate copolymer containing 7 mol% lactate and with a averge molecular weight of 320000 Da. The polymer contains a high ratio of an LA-LA-LA triad sequence
-
synthesis
-
engineering of an in vivo polylactic acid biosynthesis system in Escherichia coli to synthesize 2-hydroxybutyrate-containing polyhydroxyalkanoate. Propionyl-CoA is used as precursor for 2-ketobutyrate that is converted into 2-hydroxybutyrate-CoA by the sequential actions of Lactococcus lactis (D)-2-hydroxybutyrate dehydrogenase (PanE) and PctCp and then 2-hydroxybutyrate-CoA is polymerized by an engineered PhaC1 from Pseudomonas sp. (mutant E130D/S325T/S477G/Q481K). The recombinant Escherichia coli expressing the system can be grown to 0.66 g/l and successfully produces P(70 mol% 3-hydroxybutyrate-co-18 mol% 3-hydroxybutyrate-co-12 mol% lactate) up to the polyhydroxyalkanoate content of 66 weight% from 20 g/l of glucose, 2 g/l of 3-hydroxybutyrate and 1 g/l of sodium propionate
-
synthesis
Hydrogenophaga pseudoflava NBRC-102513
-
the enzyme can be used for polyhydroxyalkanoate production from synthetic wastewater
-
synthesis
Hydrogenophaga pseudoflava NBRC-102513
-
replacement of conventional plastics by bioplastics. Polyhydroxyalkanoates (PHA) are bio-polyesters accumulated in cells by a wide range of bacteria. Polyhydroxyalkanoates production from synthetic waste using Pseudomonas pseudoflava polyhydroxyalkanoate synthase enzyme activity
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kolibachuk, D.; Miller, A.; Dennis, D.
Cloning, molecular analysis, and expression of the polyhydroxyalkanoic acid synthase (phaC) gene from Chromobacterium violaceum
Appl. Environ. Microbiol.
65
3561-3565
1999
Chromobacterium violaceum (Q9ZHI2), Chromobacterium violaceum
brenda
Hai, T.; Lange, D.; Rabus, R.; Steinbuchel, A.
Polyhydroxyalkanoate (PHA) accumulation in sulfate-reducing bacteria and identification of a class III PHA synthase (PhaEC) in Desulfococcus multivorans
Appl. Environ. Microbiol.
70
4440-4448
2004
Desulfococcus multivorans
brenda
Zheng, Z.; Li, M.; Xue, X.J.; Tian, H.L.; Li, Z.; Chen, G.Q.
Mutation on N-terminus of polyhydroxybutyrate synthase of Ralstonia eutropha enhanced PHB accumulation
Appl. Microbiol. Biotechnol.
72
896-905
2006
Cupriavidus necator
brenda
Yuan, W.; Jia, Y.; Tian, J.; Snell, K.D.; Muh, U.; Sinskey, A.J.; Lambalot, R.H.; Walsh, C.T.; Stubbe, J.
Class I and III polyhydroxyalkanoate synthases from Ralstonia eutropha and Allochromatium vinosum: characterization and substrate specificity studies
Arch. Biochem. Biophys.
394
87-98
2001
Cupriavidus necator, Allochromatium vinosum
brenda
Hezayen, F.F.; Steinbuchel, A.; Rehm, B.H.
Biochemical and enzymological properties of the polyhydroxybutyrate synthase from the extremely halophilic archaeon strain 56
Arch. Biochem. Biophys.
403
284-291
2002
Halopiger aswanensis, Halopiger aswanensis DSM 13151
brenda
Dai, D.; Reusch, R.N.
Poly-3-hydroxybutyrate synthase from the periplasm of Escherichia coli
Biochem. Biophys. Res. Commun.
374
485-489
2008
Escherichia coli
brenda
Mh, U.; Sinskey, A.J.; Kirby, D.P.; Lane, W.S.; Stubbe, J.
PHA synthase from chromatium vinosum: cysteine 149 is involved in covalent catalysis
Biochemistry
38
826-837
1999
Allochromatium vinosum
brenda
Jia, Y.; Kappock, T.J.; Frick, T.; Sinskey, A.J.; Stubbe, J.
Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: characterization of the functional residues in Chromatium vinosum PHB synthase
Biochemistry
39
3927-3936
2000
Allochromatium vinosum
brenda
Jia, Y.; Yuan, W.; Wodzinska, J.; Park, C.; Sinskey, A.J.; Stubbe, J.
Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: class I and III synthases share a similar catalytic mechanism
Biochemistry
40
1011-1019
2001
Cupriavidus necator
brenda
Tian, J.; Sinskey, A.J.; Stubbe, J.
Detection of intermediates from the polymerization reaction catalyzed by a D302A mutant of class III polyhydroxyalkanoate (PHA) synthase
Biochemistry
44
1495-1503
2005
Allochromatium vinosum
brenda
Tian, J.; Sinskey, A.J.; Stubbe, J.
Class III polyhydroxybutyrate synthase: involvement in chain termination and reinitiation
Biochemistry
44
8369-8377
2005
Allochromatium vinosum
brenda
Rehm, B.H.; Antonio, R.V.; Spiekermann, P.; Amara, A.A.; Steinbuchel, A.
Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: in vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model
Biochim. Biophys. Acta
1594
178-190
2002
Cupriavidus necator
brenda
Song, J.J.; Zhang, S.; Lenz, R.W.; Goodwin, S.
In vitro polymerization and copolymerization of 3-hydroxypropionyl-CoA with the PHB synthase from Ralstonia eutropha
Biomacromolecules
1
433-439
2000
Cupriavidus necator
brenda
Zhang, S.; Kolvek, S.; Lenz, R.W.; Goodwin, S.
Mechanism of the polymerization reaction initiated and catalyzed by the polyhydroxybutyrate synthase of Ralstonia eutropha
Biomacromolecules
4
504-509
2003
Cupriavidus necator
brenda
Zhang, S.; Kolvek, S.; Goodwin, S.; Lenz, R.W.
Poly(hydroxyalkanoic acid) biosynthesis in Ectothiorhodospira shaposhnikovii: characterization and reactivity of a type III PHA synthase
Biomacromolecules
5
40-48
2004
Ectothiorhodospira shaposhnikovii (Q9F5P8 and Q9F5P9), Ectothiorhodospira shaposhnikovii (Q9F5P9), Ectothiorhodospira shaposhnikovii
brenda
Matsumoto, K.; Nagao, R.; Murata, T.; Arai, Y.; Kichise, T.; Nakashita, H.; Taguchi, S.; Shimada, H.; Doi, Y.
Enhancement of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) production in the transgenic Arabidopsis thaliana by the in vitro evolved highly active mutants of polyhydroxyalkanoate (PHA) synthase from Aeromonas caviae
Biomacromolecules
6
2126-2130
2005
Aeromonas caviae
brenda
Matsumoto, K.; Takase, K.; Aoki, E.; Doi, Y.; Taguchi, S.
Synergistic effects of Glu130Asp substitution in the type II polyhydroxyalkanoate (PHA) synthase: enhancement of PHA production and alteration of polymer molecular weight
Biomacromolecules
6
99-104
2005
Pseudomonas sp.
brenda
Normi, Y.M.; Hiraishi, T.; Taguchi, S.; Sudesh, K.; Najimudin, N.; Doi, Y.
Site-directed saturation mutagenesis at residue F420 and recombination with another beneficial mutation of Ralstonia eutropha polyhydroxyalkanoate synthase
Biotechnol. Lett.
27
705-712
2005
Cupriavidus necator
brenda
Liebergesell, M.; Sonomoto, K.; Madkour, M.; Mayer, F.; Steinbuchel, A.
Purification and characterization of the poly(hydroxyalkanoic acid) synthase from Chromatium vinosum and localization of the enzyme at the surface of poly(hydroxyalkanoic acid) granules
Eur. J. Biochem.
226
71-80
1994
Allochromatium vinosum
brenda
Kichise, T.; Fukui, T.; Yoshida, Y.; Doi, Y.
Biosynthesis of polyhydroxyalkanoates (PHA) by recombinant Ralstonia eutropha and effects of PHA synthase activity on in vivo PHA biosynthesis
Int. J. Biol. Macromol.
25
69-77
1999
Aeromonas caviae
brenda
Wodzinska, J.; Snell, K.D.; Rhomberg, A.; Sinskey, A.J.; Biemann, K.; Stubbe, J.
Polyhydroxybutyrate synthase: Evidence for covalent catalysis
J. Am. Chem. Soc.
118
6319-6320
1996
Cupriavidus necator
-
brenda
Lu, Q.; Han, J.; Zhou, L.; Zhou, J.; Xiang, H.
Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthase in Haloferax mediterranei
J. Bacteriol.
190
4173-4180
2008
Haloferax mediterranei (I3R9Z3 and I3R9Z4), Haloferax mediterranei
brenda
Takase, K.; Taguchi, S.; Doi, Y.
Enhanced synthesis of poly(3-hydroxybutyrate) in recombinant Escherichia coli by means of error-prone PCR mutagenesis, saturation mutagenesis, and in vitro recombination of the type II polyhydroxyalkanoate synthase gene
J. Biochem.
133
139-145
2003
Pseudomonas sp.
brenda
Sharma, L.; Panda, B.; Singh, A.K.; Mallick, N.
Studies on poly-beta-hydroxybutyrate synthase activity of Nostoc muscorum
J. Gen. Appl. Microbiol.
52
209-214
2006
Desmonostoc muscorum
brenda
Normi, Y.M.; Hiraishi, T.; Taguchi, S.; Abe, H.; Sudesh, K.; Najimudin, N.; Doi, Y.
Characterization and properties of G4X mutants of Ralstonia eutropha PHA synthase for poly(3-hydroxybutyrate) biosynthesis in Escherichia coli
Macromol. Biosci.
5
197-206
2005
Cupriavidus necator
brenda
Hai, T.; Hein, S.; Steinbuchel, A.
Multiple evidence for widespread and general occurrence of type-III PHA synthases in cyanobacteria and molecular characterization of the PHA synthases from two thermophilic cyanobacteria: Chlorogloeopsis fritschii PCC 6912 and Synechococcus sp. strain MA19
Microbiology
147
3047-3060
2001
Anabaena cylindrica, Gloeocapsa sp., Synechococcus sp., Synechococcus sp. (Q8RT55), Crocosphaera subtropica ATCC 51142, Crocosphaera subtropica ATCC 51142 (B7KDE2), no activity in Stanieria cyanosphaera, no activity in Cyanothece sp., no activity in Gloeothece membranacea, Chlorogloeopsis fritschii (Q8RTL8), no activity in Cyanothece sp. PCC 8955, no activity in Gloeothece membranacea PCC 6501, no activity in Stanieria cyanosphaera PCC 7437, Anabaena cylindrica SAG 1403-2
brenda
Qi, Q.; Rehm, B.H.
Polyhydroxybutyrate biosynthesis in Caulobacter crescentus: molecular characterization of the polyhydroxybutyrate synthase
Microbiology
147
3353-3358
2001
Caulobacter vibrioides (Q9F4K5), Caulobacter vibrioides
brenda
Sim, S.J.; Snell, K.D.; Hogan, S.A.; Stubbe, J.; Rha, C.; Sinskey, A.J.
PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo
Nat. Biotechnol.
15
63-67
1997
Cupriavidus necator
brenda
Matsumoto, K.; Yamada, M.; Leong, C.; Jo, S.; Kuzuyama, T.; Taguchi, S.
A new pathway for poly(3-hydroxybutyrate) production in Escherichia coli and Corynebacterium glutamicum by functional expression of a new acetoacetyl-coenzyme A synthase
Biosci. Biotechnol. Biochem.
75
364-366
2011
Cupriavidus necator
brenda
Han, J.; Hou, J.; Liu, H.; Cai, S.; Feng, B.; Zhou, J.; Xiang, H.
Wide distribution among halophilic archaea of a novel polyhydroxyalkanoate synthase subtype with homology to bacterial type III synthases
Appl. Environ. Microbiol.
76
7811-7819
2010
Halobacteriaceae
brenda
Yang, T.H.; Jung, Y.K.; Kang, H.O.; Kim, T.W.; Park, S.J.; Lee, S.Y.
Tailor-made type II Pseudomonas PHA synthases and their use for the biosynthesis of polylactic acid and its copolymer in recombinant Escherichia coli
Appl. Microbiol. Biotechnol.
90
603-614
2011
Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas chlororaphis (C0LD26), Pseudomonas chlororaphis, Pseudomonas resinovorans (Q9X5X7), Pseudomonas resinovorans, Pseudomonas sp. (Q9Z3Y1), Pseudomonas sp., Pseudomonas chlororaphis KCTC 12349 (C0LD26), Pseudomonas putida KT 2240, Pseudomonas resinovorans KCTC 12498 (Q9X5X7)
brenda
Cho, M.; Brigham, C.J.; Sinskey, A.J.; Stubbe, J.
Purification of polyhydroxybutyrate synthase from its native organism, Ralstonia eutropha: implications for the initiation and elongation of polymer formation in vivo
Biochemistry
51
2276-2288
2012
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Tomizawa, S.; Hyakutake, M.; Saito, Y.; Agus, J.; Mizuno, K.; Abe, H.; Tsuge, T.
Molecular weight change of polyhydroxyalkanoate (PHA) caused by the PhaC subunit of PHA synthase from Bacillus cereus YB-4 in recombinant Escherichia coli
Biomacromolecules
12
2660-2666
2011
Bacillus cereus (D2Z0B8), Bacillus cereus, Priestia megaterium (D2Z0B9), Priestia megaterium, Bacillus cereus YB-4 (D2Z0B8), Bacillus cereus YB-4, Priestia megaterium NBRC15308 (D2Z0B9)
brenda
Shozui, F.; Sun, J.; Song, Y.; Yamada, M.; Sakai, K.; Matsumoto, K.; Takase, K.; Taguchi, S.
A new beneficial mutation in Pseudomonas sp. 61-3 polyhydroxyalkanoate (PHA) synthase for enhanced cellular content of 3-hydroxybutyrate-based PHA explored using its enzyme homolog as a mutation template
Biosci. Biotechnol. Biochem.
74
1710-1712
2010
Pseudomonas sp.
brenda
Tan, Y.; Neo, P.C.; Najimudin, N.; Sudesh, K.; Muhammad, T.S.; Othman, A.S.; Samian, R.
Cloning and characterization of poly(3-hydroxybutyrate) biosynthesis genes from Pseudomonas sp. USM 4-55
J. Basic Microbiol.
50
179-189
2010
Pseudomonas sp. (C0KTZ0), Pseudomonas sp., Pseudomonas sp. USM4-55 (C0KTZ0)
brenda
Sato, S.; Minato, M.; Kikkawa, Y.; Abe, H.; Tsuge, T.
In vitro synthesis of polyhydroxyalkanoate catalyzed by class II and III PHA synthases: A useful technique for surface coatings of a hydrophobic support with PHA
J. Chem. Technol. Biotechnol.
85
779-782
2010
Allochromatium vinosum, Pseudomonas putida
-
brenda
Kek, Y.; Chang, C.; Amirul, A.; Sudesh, K.
Heterologous expression of Cupriavidus sp. USMAA2-4 PHA synthase gene in PHB-4 mutant for the production of poly(3-hydroxybutyrate) and its copolymers
World J. Microbiol. Biotechnol.
26
1595-1603
2010
Cupriavidus sp., Cupriavidus sp. USMAA2-4
brenda
Zhang, W.; Shrestha, R.; Buckley, R.M.; Jewell, J.; Bossmann, S.H.; Stubbe, J.; Li, P.
Mechanistic insight with HBCH2CoA as a probe to polyhydroxybutyrate (PHB) synthases
ACS Chem. Biol.
9
1773-1779
2014
Cupriavidus necator, Allochromatium vinosum
brenda
Thomson, N.; Saika, A.; Ushimaru, K.; Sangiambut, S.; Tsuge, T.; Summers, D.; Sivaniah, E.
Efficient production of active polyhydroxyalkanoate synthase in Escherichia coli by coexpression of molecular chaperones
Appl. Environ. Microbiol.
79
1948-1955
2013
Cupriavidus necator (P23608), Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (P23608)
brenda
Hyakutake, M.; Tomizawa, S.; Mizuno, K.; Abe, H.; Tsuge, T.
Alcoholytic cleavage of polyhydroxyalkanoate chains by class IV synthases induced by endogenous and exogenous ethanol
Appl. Environ. Microbiol.
80
1421-1429
2014
Bacillus cereus (D2Z0B8 and D2Z0B6), Bacillus cereus, Bacillus cereus YB-4 (D2Z0B8 and D2Z0B6)
brenda
Ochi, A.; Matsumoto, K.; Ooba, T.; Sakai, K.; Tsuge, T.; Taguchi, S.
Engineering of class i lactate-polymerizing polyhydroxyalkanoate synthases from Ralstonia eutropha that synthesize lactate-based polyester with a block nature
Appl. Microbiol. Biotechnol.
97
3441-3447
2013
Cupriavidus necator (P23608), Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (P23608)
brenda
Buckley, R.M.; Stubbe, J.
Chemistry with an artificial primer of polyhydroxybutyrate synthase suggests a mechanism for chain termination
Biochemistry
54
2117-2125
2015
Caulobacter vibrioides
brenda
Edkie, G.; Prasad, D.
Bacillus PHA synthase III C gene showed regulatory functions: An in-silico analysis
Biotechnology
13
143-151
2014
Bacillus subtilis (I4EBJ0)
-
brenda
Foong, C.; Lau, N.; Deguchi, S.; Toyofuku, T.; Taylor, T.; Sudesh, K.; Matsui, M.
Whole genome amplification approach reveals novel polyhydroxyalkanoate synthases (PhaCs) from Japan Trench and Nankai Trough seawater
BMC Microbiol.
14
318
2014
Marinobacter sp. (U7P2T8), Marinobacter sp. C1S70 (U7P2T8)
brenda
Klask, C.; Raberg, M.; Heinrich, D.; Steinbchel, A.
Heterologous expression of various PHA synthase genes in Rhodospirillum rubrum
Chem. Biochem. Eng. Q.
29
75-85
2015
Rhodospirillum rubrum
-
brenda
Chen, Y.J.; Tsai, P.C.; Hsu, C.H.; Lee, C.Y.
Critical residues of class II PHA synthase for expanding the substrate specificity and enhancing the biosynthesis of polyhydroxyalkanoate
Enzyme Microb. Technol.
56
60-66
2014
Pseudomonas putida, Pseudomonas putida GPo1 / ATCC29347
brenda
Gowda, V.; Shivakumar, S.
Poly(3)hydroxybutyrate (PHB) production in Bacillus thuringiensis IAM 12077 under varied nutrient limiting conditions and molecular detection of class IV PHA synthase gene by PCR
Int. J. Pharm. Bio Sci.
4
B794-B802
2013
Bacillus thuringiensis, Bacillus thuringiensis IAM 12077
-
brenda
Tai, Y.T.; Foong, C.P.; Najimudin, N.; Sudesh, K.
Discovery of a new polyhydroxyalkanoate synthase from limestone soil through metagenomic approach
J. Biosci. Bioeng.
121
355-364
2015
uncultured bacterium (A0A0F6WBG5), uncultured bacterium, uncultured bacterium SC8 (A0A0F6WBG5)
brenda
Park, S.J.; Kang, K.H.; Lee, H.; Park, A.R.; Yang, J.E.; Oh, Y.H.; Song, B.K.; Jegal, J.; Lee, S.H.; Lee, S.Y.
Propionyl-CoA dependent biosynthesis of 2-hydroxybutyrate containing polyhydroxyalkanoates in metabolically engineered Escherichia coli
J. Biotechnol.
165
93-98
2013
Pseudomonas sp., Pseudomonas sp. MBEL 619
brenda
Muniasamy, G.; Perez-Guevara, F.
Use of SNAREs for the immobilization of poly-3-hydroxyalkanoate polymerase type II of Pseudomonas putida CA-3 in secretory vesicles of Saccharomyces cerevisiae ATCC 9763
J. Biotechnol.
172
77-79
2014
Pseudomonas putida, Pseudomonas putida CA-3
brenda
Muangsuwan, W.; Ruangsuj, P.; Chaichanachaicharn, P.; Yasawong, M.
A novel nucleic lateral flow assay for screening of PHA-producing haloarchaea
J. Microbiol. Methods
116
8-14
2015
Haloquadratum walsbyi (G0LKV7), Haloquadratum walsbyi DSM 16854 (G0LKV7)
brenda
Hyakutake, M.; Tomizawa, S.; Sugahara, I.; Murata, E.; Mizuno, K.; Abe, H.; Tsuge, T.
Carboxy-terminal modification of polyhydroxyalkanoate (PHA) via alcoholysis reaction catalyzed by class IV PHA synthase
Polym. Degrad. Stab.
117
90-96
2015
Bacillus cereus (D2Z0B8 and D2Z0B6), Bacillus cereus YB-4 (D2Z0B8 and D2Z0B6)
-
brenda
Chek, M.F.; Hiroe, A.; Hakoshima, T.; Sudesh, K.; Taguchi, S.
PHA synthase (PhaC) interpreting the functions of bioplastic-producing enzyme from a structural perspective
Appl. Microbiol. Biotechnol.
103
1131-1141
2019
Aeromonas caviae, Chromobacterium sp. USM2 (E1APK1), Cupriavidus necator (P23608), Cupriavidus necator, Pseudomonas sp. 61-3 (Q9Z3Y1), Cupriavidus necator Stanier 337 (P23608), Cupriavidus necator 17699 (P23608), Cupriavidus necator DSM 428 (P23608)
brenda
Jia, K.; Cao, R.; Hua, D.H.; Li, P.
Study of class I and class III polyhydroxyalkanoate (PHA) synthases with substrates containing a modified side chain
Biomacromolecules
17
1477-1485
2016
Allochromatium vinosum, Caulobacter vibrioides (A0A290N3S7), Caulobacter vibrioides, Chromobacterium sp. USM2 (E1APK1)
brenda
Fluechter, S.; Follonier, S.; Schiel-Bengelsdorf, B.; Bengelsdorf, F.R.; Zinn, M.
Anaerobic production of poly(3-hydroxybutyrate) and its precursor 3?hydroxybutyrate from synthesis gas by autotrophic clostridia
Biomacromolecules
20
3271-3282
2019
Clostridium acetireducens (A0A1E8EW93 AND A0A1E8EW64), Clostridium acetireducens DSM 10703 (A0A1E8EW93 AND A0A1E8EW64)
brenda
Venkateswar Reddy, M.; Mawatari, Y.; Onodera, R.; Nakamura, Y.; Yajima, Y.; Chang, Y.
Polyhydroxyalkanoates (PHA) production from synthetic waste using Pseudomonas pseudoflava PHA synthase enzyme activity analysis from P. pseudoflava and P. palleronii
Biores. Technol.
234
99-105
2017
Hydrogenophaga palleronii, Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava (A0A4P6X2C3), Hydrogenophaga pseudoflava NBRC-102513, Hydrogenophaga pseudoflava NBRC-102513 (A0A4P6X2C3)
brenda
Miyahara, Y.; Hiroe, A.; Tsuge, T.; Taguchi, S.
Microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases
Biotechnol. J.
14
e1900201
2019
Bacillus cereus (D2Z0B8), Aeromonas caviae (O32471), Delftia acidovorans (O87110), Cupriavidus necator (P23608), Allochromatium vinosum (P45370), Bacillus sp. INT005 (Q8GI81), Priestia megaterium (Q9ZF92), Cupriavidus necator Stanier 337 (P23608), Cupriavidus necator DSM 428 (P23608), Cupriavidus necator ATCC 17699 (P23608)
brenda
Nguyen, T.H.; Ishizuna, F.; Sato, Y.; Arai, H.; Ishii, M.
Physiological characterization of poly-beta-hydroxybutyrate accumulation in the moderately thermophilic hydrogen-oxidizing bacterium Hydrogenophilus thermoluteolus TH-1
J. Biosci. Bioeng.
127
686-689
2019
Hydrogenophilus thermoluteolus (A0A2Z6DVS4), Hydrogenophilus thermoluteolus (A0A2Z6DWT1), Hydrogenophilus thermoluteolus, Hydrogenophilus thermoluteolus DSM 6765 (A0A2Z6DVS4), Hydrogenophilus thermoluteolus DSM 6765 (A0A2Z6DWT1), Hydrogenophilus thermoluteolus TH-1 (A0A2Z6DVS4), Hydrogenophilus thermoluteolus TH-1 (A0A2Z6DWT1)
brenda
Sudo, M.; Hori, C.; Ooi, T.; Mizuno, S.; Tsuge, T.; Matsumoto, K.
Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase
J. Biosci. Bioeng.
129
302-306
2020
Aeromonas caviae (O32471), Aeromonas caviae, Cupriavidus necator (P23608), Cupriavidus necator, Cupriavidus necator Stanier 337 (P23608), Cupriavidus necator DSM 428 (P23608), Cupriavidus necator ATCC 17699 (P23608)
brenda
Tan, I.K.P.; Foong, C.P.; Tan, H.T.; Lim, H.; Zain, N.A.; Tan, Y.C.; Hoh, C.C.; Sudesh, K.
Polyhydroxyalkanoate (PHA) synthase genes and PHA-associated gene clusters in Pseudomonas spp. and Janthinobacterium spp. isolated from Antarctica
J. Biotechnol.
313
18-28
2020
Janthinobacterium sp. UMAB-56, Janthinobacterium sp. UMAB-60, Pseudomonas sp. UMAB-08, Pseudomonas sp. UMAB-40, Janthinobacterium sp. UMAB-58
brenda
Foong, C.; Lakshmanan, M.; Abe, H.; Taylor, T.; Foong, S.; Sudesh, K.
A novel and wide substrate specific polyhydroxyalkanoate (PHA) synthase from unculturable bacteria found in mangrove soil
J. Polym. Res.
25
23
2018
uncultured bacterium
-
brenda
Woo, S.; Lee, S.; Rhee, Y.
Substrate chain-length specificities of polyhydroxyalkanoate synthases PhaC1 and PhaC2 from Pseudomonas aeruginosa P-5
Korean J. Microbiol.
52
455-462
2016
Pseudomonas aeruginosa (H6VX88), Pseudomonas aeruginosa (H6VX89), Pseudomonas aeruginosa P-5 (H6VX88), Pseudomonas aeruginosa P-5 (H6VX89)
-
brenda
Du, J.; Rehm, B.
Purification of target proteins from intracellular inclusions mediated by intein cleavable polyhydroxyalkanoate synthase fusions
Microb. Cell Fact.
16
184
2017
Cupriavidus necator (P23608), Cupriavidus necator Stanier 337 (P23608), Cupriavidus necator DSM 428 (P23608), Cupriavidus necator ATCC 17699 (P23608)
brenda
Mezzolla, V.; D'Urso, O.; Poltronieri, P.
Role of PhaC type I and type II enzymes during PHA biosynthesis
Polymers (Basel)
10
910
2018
Pseudomonas aeruginosa (Q51513), Pseudomonas mendocina (Q2PMY5), Pseudomonas oleovorans (P26494), Pseudomonas putida (A0A1Y5KN65), Pseudomonas stutzeri (Q848R9)
brenda
Lau, N.S.; Sudesh, K.
Revelation of the ability of Burkholderia sp. USM (JCM 15050) PHA synthase to polymerize 4-hydroxybutyrate monomer
AMB Express
2
41
2012
Burkholderia sp. USM (JCM 15050)
brenda
Amara, A.A.; Steinbuechel, A.; Rehm, B.H.
In vivo evolution of the Aeromonas punctata polyhydroxyalkanoate (PHA) synthase isolation and characterization of modified PHA synthases with enhanced activity
Appl. Microbiol. Biotechnol.
59
477-482
2002
Aeromonas caviae
brenda
Shen, X.W.; Shi, Z.Y.; Song, G.; Li, Z.J.; Chen, G.Q.
Engineering of polyhydroxyalkanoate (PHA) synthase PhaC2Ps of Pseudomonas stutzeri via site-specific mutation for efficient production of PHA copolymers
Appl. Microbiol. Biotechnol.
91
655-665
2011
Pseudomonas stutzeri, Pseudomonas stutzeri 1317
brenda
Tajima, K.; Han, X.; Satoh, Y.; Ishii, A.; Araki, Y.; Munekata, M.; Taguchi, S.
In vitro synthesis of polyhydroxyalkanoate (PHA) incorporating lactate (LA) with a block sequence by using a newly engineered thermostable PHA synthase from Pseudomonas sp. SG4502 with acquired LA-polymerizing activity
Appl. Microbiol. Biotechnol.
94
365-376
2012
Pseudomonas sp. SG4502
brenda
Qin, L.; Gao, X.; Liu, Q.; Wu, Q.; Chen, G.
Biosynthesis of polyhydroxyalkanoate copolyesters by Aeromonas hydrophila mutant expressing a low-substrate-specificity PHA synthase PhaC2Ps
Biochem. Eng. J.
37
144-150
2007
Pseudomonas stutzeri, Pseudomonas stutzeri 1317
-
brenda
Matsumoto, K.; Nagao, R.; Murata, T.; Arai, Y.; Kichise, T.; Nakashita, H.; Taguchi, S.; Shimada, H.; Doi, Y.
Enhancement of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) production in the transgenic Arabidopsis thaliana by the in vitro evolved highly active mutants of polyhydroxyalkanoate (PHA) synthase from Aeromonas caviae
Biomacromolecules
6
2126-2130
2005
Aeromonas caviae
brenda
Matsumoto, K.; Aoki, E.; Takase, K.; Doi, Y.; Taguchi, S.
In vivo and in vitro characterization of Ser477X mutations in polyhydroxyalkanoate (PHA) synthase 1 from Pseudomonas sp. 61-3 effects of beneficial mutations on enzymatic activity, substrate specificity, and molecular weight of PHA
Biomacromolecules
7
2436-2442
2006
Pseudomonas sp. 61-3
brenda
Liu, C.H.; Chen, H.Y.; Chen, Y.L.; Sheu, D.S.
The polyhydroxyalkanoate (PHA) synthase 1 of Pseudomonas sp. H9 synthesized a 3-hydroxybutyrate-dominant hybrid of short- and medium-chain-length PHA
Enzyme Microb. Technol.
143
109719
2021
Pseudomonas sp. H9 (A0A4R5K593)
brenda
Qi, Q.; Rehm, B.H.; Steinbuechel, A.
Synthesis of poly(3-hydroxyalkanoates) in Escherichia coli expressing the PHA synthase gene phaC2 from Pseudomonas aeruginosa comparison of PhaC1 and PhaC2
FEMS Microbiol. Lett.
157
155-162
1997
Pseudomonas aeruginosa
brenda
Tan, H.T.; Chek, M.F.; Lakshmanan, M.; Foong, C.P.; Hakoshima, T.; Sudesh, K.
Evaluation of BP-M-CPF4 polyhydroxyalkanoate (PHA) synthase on the production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from plant oil using Cupriavidus necator transformants
Int. J. Biol. Macromol.
159
250-257
2020
Chromobacterium sp. USM2
brenda
Lim, H.; Chuah, J.A.; Chek, M.F.; Tan, H.T.; Hakoshima, T.; Sudesh, K.
Identification of regions affecting enzyme activity, substrate binding, dimer stabilization and polyhydroxyalkanoate (PHA) granule morphology in the PHA synthase of Aquitalea sp. USM4
Int. J. Biol. Macromol.
186
414-423
2021
Aquitalea sp. USM4
brenda
Sudesh, K.; Taguchi, K.; Doi, Y.
Effect of increased PHA synthase activity on polyhydroxyalkanoates biosynthesis in Synechocystis sp. PCC6803
Int. J. Biol. Macromol.
30
97-104
2002
Synechocystis sp. PCC 6803
brenda
Chee, J.Y.; Lau, N.S.; Samian, M.R.; Tsuge, T.; Sudesh, K.
Expression of Aeromonas caviae polyhydroxyalkanoate synthase gene in Burkholderia sp. USM (JCM15050) enables the biosynthesis of SCL-MCL PHA from palm oil products
J. Appl. Microbiol.
112
45-54
2012
Aeromonas caviae
brenda
Hiroe, A.; Ushimaru, K.; Tsuge, T.
Characterization of polyhydroxyalkanoate (PHA) synthase derived from Delftia acidovorans DS-17 and the influence of PHA production in Escherichia coli
J. Biosci. Bioeng.
115
633-638
2013
Cupriavidus necator, Delftia acidovorans, Delftia acidovorans DS-17
brenda
Hu, F.; You, S.
Inactivation of type I polyhydroxyalkanoate synthase in Aeromonas hydrophila resulted in discovery of another potential PHA synthase
J. Ind. Microbiol. Biotechnol.
34
255-260
2007
Aeromonas hydrophila, Aeromonas hydrophila CGMCC 0911
brenda
Pantazaki, A.A.; Tambaka, M.G.; Langlois, V.; Guerin, P.; Kyriakidis, D.A.
Polyhydroxyalkanoate (PHA) biosynthesis in Thermus thermophilus purification and biochemical properties of PHA synthase
Mol. Cell. Biochem.
254
173-183
2003
Thermus thermophilus
brenda
Mok, P.S.; Chuah, J.A.; Najimudin, N.; Liew, P.W.; Jong, B.C.; Sudesh, K.
In vivo characterization and application of the PHA synthase from Azotobacter vinelandii for the biosynthesis of polyhydroxyalkanoate containing 4-hydroxybutyrate
Polymers (Basel)
13
1576
2021
Azotobacter vinelandii, Azotobacter vinelandii ATCC 12837
brenda
Chek, M.F.; Kim, S.Y.; Mori, T.; Arsad, H.; Samian, M.R.; Sudesh, K.; Hakoshima, T.
Structure of polyhydroxyalkanoate (PHA) synthase PhaC from Chromobacterium sp. USM2, producing biodegradable plastics
Sci. Rep.
7
5312
2017
Chromobacterium sp. USM2 (E1APK1)
brenda
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