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Information on EC 2.4.1.131 - GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase
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2.4.1.131 GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferaseIUBMB Comments
The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
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Word Map
- 2.4.1.131
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lipid-linked
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n-glycosylation
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n-linked
- glycosyltransferase
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dolichol-linked
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asparagine-linked
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man5glcnac2-pp-dolichol
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alpha1,2-linked
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single-subunit
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oligosaccharyltransferase
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man5glcnac2-pp-dol
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microcephaly
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
alg11, halg11, gdp-man:man3glcnac2-pp-dolichol-alpha1,2-mannosyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alg11
GDP-mannose-oligosaccharide-lipid mannosyltransferase
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guanosine diphosphomannose-oligosaccharide-lipid mannosyltransferase
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mannosyltransferase, guanosine diphosphomannose-oligosaccharide-lipid
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oligosaccharide-lipid mannosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 GDP-alpha-D-mannose + alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = 2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
GDP-alpha-D-mannose:D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 2-alpha-D-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
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CAS REGISTRY NUMBER
COMMENTARY
74506-43-7
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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
2 GDP-alpha-D-mannose + alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 UDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
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-
-
?
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP-mannose + lipid-linked Manalpha(1-3)Manbeta-GlcNAcbeta-GlcNAc
GDP + lipid-linked Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta-GlcNAcbeta-GlcNAc
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reaction via penta- and hexasaccharide intermediates to a lipid-linked heptasaccharide, presumably multiple mannosyltransferases involved
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?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
2 GDP-alpha-D-mannose + alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
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-
-
?
2 GDP-alpha-D-mannose + alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
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?
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
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?
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
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-
?
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side
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?
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
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?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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acceptors can be mannose or Man-(GlcNAc)2 to (Man)5-(GlcNAc)2, lipid-linked tetrasaccharide Manalpha(1-3)Manbeta-GlcNAcbeta-GlcNAc, presumably multiple mannosyltransferases involved
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?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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acceptor isolated from baby hamster kidney cells, i.e. BHK cells
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?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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oligosaccharide-P-P-lipid: major oligosaccharide component is Man2GlcNAc2
penta-, hexa-, and heptasaccharide as oligosaccharide portion, formed by the stepwise addition of mannose to the growing oligosaccharide chain
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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acceptor isolated from pig liver
presumably a heptasaccharide with a 1,6-linked branched glycosyl unit with 65% of the newly added mannosyl units in a terminal nonreducing position, structure may be Manalpha(1-2)Man-Man(Man(1-6))Man-GlcNAc-GlcNAc
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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acceptor isolated from pig liver
penta-, hexa-, and heptasaccharide as oligosaccharide portion, formed by the stepwise addition of mannose to the growing oligosaccharide chain
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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oligosaccharide portion: a mixture of trisaccharide and pentasaccharide, acceptor lipids are probably Manbeta-GlcNAc-GlcNAc-pyrophosphoryldolichol and Man2alpha-Manbeta-GlcNAc-GlcNAc-pyrophosphoryldolichol
heptasaccharide-lipid as product, probably Man5GlcNAc2 as heptasaacharide
?
GDP-mannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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acceptor isolated from pig liver
heptasaccharide-lipid as product, probably Man5GlcNAc2 as heptasaacharide
?
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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involved in biosynthesis of lipid-linked oligosaccharides up to (Man)5-(GlcNAc)2, involved in the production of two 1,2-linked mannosyl residues in mammalian lipid-linked tetradecasaccharide of the structure (Glc)3(Man)9(GlcNAc)2, the major precursor for eukaryotic en-bloc-glycosylation of asparagin-linked glycoproteins
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?
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
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biosynthesis of oligosaccharide-lipids
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?
additional information
?
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involved in asparagine-linked glycosylation, reaction proceeds in the endoplasmatic reticulum, role of the ALG9 step in downstream ER and Golgi N-glycan processing events
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?
additional information
?
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Alg11 mannosyltransferase shows no activity with Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
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?
additional information
?
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Alg11 mannosyltransferase shows no activity with Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
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?
additional information
?
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chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins. Comparison to the reaction of dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3A (EC 2.4.99.18)
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additional information
?
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chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins. Comparison to the reaction of dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3A (EC 2.4.99.18)
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additional information
additional information
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no sugar donor: mannosylphosphorylretinol
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?
additional information
additional information
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no substrate: dolichol-phosphat
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?
additional information
additional information
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(Man)6-(GlcNAc)2 precursor of enzyme
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-2)Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcalpha/beta is the product of the middle-arm terminal alpha1,2-mannosyltransferase Alg9p
?
additional information
additional information
-
-
no substrate: dolichol-phosphat
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?
additional information
additional information
-
-
no sugar donor: mannosylphosphoryldolichol
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?
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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
2 GDP-alpha-D-mannose + alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
additional information
?
-
-
involved in asparagine-linked glycosylation, reaction proceeds in the endoplasmatic reticulum, role of the ALG9 step in downstream ER and Golgi N-glycan processing events
-
-
?
2 GDP-alpha-D-mannose + alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
-
-
-
?
2 GDP-alpha-D-mannose + alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
-
-
-
?
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
-
-
?
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side
-
-
?
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
-
involved in biosynthesis of lipid-linked oligosaccharides up to (Man)5-(GlcNAc)2, involved in the production of two 1,2-linked mannosyl residues in mammalian lipid-linked tetradecasaccharide of the structure (Glc)3(Man)9(GlcNAc)2, the major precursor for eukaryotic en-bloc-glycosylation of asparagin-linked glycoproteins
-
-
?
GDPmannose + oligosaccharide-lipid acceptor
GDP + alpha-mannosyl-1,2-oligosaccharide-lipid
-
biosynthesis of oligosaccharide-lipids
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
reaction is independent of the addition of divalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
less than 15% inhibition at 2 mM: ADP, ATP, UDP, UDP-glucose, UDP-galactose and UDP-N-acetylglucosamine; not inhibited by EDTA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital Disorders of Glycosylation
A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip.
Intellectual Disability
Improved diagnostics lead to identification of three new patients with congenital disorder of glycosylation-Ip.
Lipoma
Gene expression and single nucleotide polymorphism array analyses of spindle cell lipomas and conventional lipomas with 13q14 deletion.
Metabolic Diseases
A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip.
Seizures
Improved diagnostics lead to identification of three new patients with congenital disorder of glycosylation-Ip.
Strabismus
Improved diagnostics lead to identification of three new patients with congenital disorder of glycosylation-Ip.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00064
D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
pH 7.0, 37°C
0.00064
oligosaccharide-lipid acceptor
-
based on the assumption of incorporation of only a single mannosyl unit into the product
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
a deletion of the ALG11 gene leads to poor growth and temperature-sensitive lethality, disruption of the ALG11 locus results in Underglycosylation of proteins
malfunction
a patient with muscular hypotonia, convulsions, developmental retardation, dysmorphic signs and death in infancy, a deficiency of GDP-Man:Man3GlcNAc2-PP-dolichol mannosyltransferase, the human ortholog of Alg11 from yeast, is identified as the molecular cause. The enzymatic malfunction leads to impairment in the elongation of lipid-linked oligosaccharides at the outer leaflet of the endoplasmic reticulum, resulting in CDG-Ip, a congenital disorders of glycosylation. Mutation p.L86S in the endoplasmic reticulum mannosyltransferase hALG11 leads to accumulation of Man3GlcNAc2-PP-dolichol and Man4GlcNAc2-PP-dolichol in the index CDG-Ip patient
malfunction
compared with wild-type cells, DELTAalg11 grows poorly and osmotic stabilization by KCl only slightly improved growth. Deletion of ALG11 causes a temperature-sensitive lethality between 32°C and 36°C
malfunction
gmd3 mutant cannot grow at 37°C. Construction of a plasmid pREP1+/-ALG11HA for the expression of Saccharomyces cerevisiae ALG11 in Schizosaccharomyces pombe and introducing it into gmd3 mutant. The gmd3 mutant, carrying pREP+/-ALG11HA, grows at 37°C, whereas the gmd3 mutant, carrying vector pREP1 alone, does not. The defect in acid phosphatase glycosylation of gmd3 mutant is also suppressed by Saccharomyces cerevisiae ALG11. The gmd3+/alg11+ gene is a functional homologue of the Saccharomyces cerevisiae ALG11 gene
malfunction
-
mutant lew3, which has a defect in alpha-1,2-mannosyltransferase is deficient in N-glycosylation
Show AA Sequence and Transmembrane Helices (3418 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63140
63143
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
the protein is predicted to contain four N-linked glycosylation sites, but none appear to be utilized, because Alg11p is insensitive to digestion with endo H
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L86P
mutant enzyme does not complement the growth deffect of the mutant strain DELTAalgg3 (Saccharomyces cerevisiae)
L86S
mutant enzyme slightly complements the growth deffect of the mutant strain DELTAalgg3 (Saccharomyces cerevisiae)
E405/H406A
double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression
E405A
E405A/E413
double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression
E413A
F407A
mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G84A
mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G84P
mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G85A
mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G85P
mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G87A
mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
G87P
mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
H406A
mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y
additional information
E405A
mutation causes an underglycosylation of the vacuolar model glycoproteincarboxypeptidase Y
E405A
mutation causes nearly complete abrogation of product formation
E413A
activity is indistinguishable from that of the wild-type under comparable conditions
additional information
chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1 (from yeast, EC 2.4.1.142), Alg2 (from human, EC 2.4.1.257), and Alg11 proteins, chemo-enzymatic synthesis strategy to extend the glycan moiety of synthetic LLO analogues to Dol-PP-GlcNAc2Man5, method, overview
additional information
-
chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1 (from yeast, EC 2.4.1.142), Alg2 (from human, EC 2.4.1.257), and Alg11 proteins, chemo-enzymatic synthesis strategy to extend the glycan moiety of synthetic LLO analogues to Dol-PP-GlcNAc2Man5, method, overview
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, solubilized enzyme, 2 weeks: about 40% loss of activity, 7 days: about 20% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His10-tagged enzyme ALG11 from Escherichia coli strain BL21-Gold (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ALG9 gene encodes a middle-arm terminal alpha1,2-mannosyltransferase Alg9p
-
construction of a plasmid pREP1+/-ALG11HA for the expression of Saccharomyces cerevisiae ALG11 in Schizosaccharomyces pombe and introducing it into gmd3 mutant. The gmd3 mutant, carrying pREP+/-ALG11HA, grows at 37°C, whereas the gmd3 mutant, carrying vector pREP1 alone, does not. The defect in acid phosphatase glycosylation of gmd3 mutant is also suppressed by Saccharomyces cerevisiae ALG11. The gmd3+/alg11+ gene is a functional homologue of the Saccharomyces cerevisiae ALG11 gene
gene ALG11, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21-Gold (DE3)
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
retroviral expression of human wild-type and mutated ALG11 cDNA in patient-derived fibroblasts as well as using a yeast alg11 deletion strain as a heterologous expression system for hALG11 variants
transformation of the LEW3 gene into the yeast mutant alg11, which exhibits a lowtemperature-sensitive phenotype and grows slowly at and below 30°C but normally at 37°C. Expression of LEW3 partially complements the slow-growth phenotype of the yeast mutant alg11, suggesting that the plant ALG11 homolog is able to partially substitute for the function of ALG11 in yeast
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schutzbach, J.S.; Springfield, J.D.; Jensen, J.W.
The biosynthesis of oligosaccharide-lipids. Formation of an alpha-1,2-mannosyl-mannose linkage
J. Biol. Chem.
255
4170-4175
1980
Oryctolagus cuniculus
brenda
Spencer, J.P.; Elbein, A.D.
Transfer of mannose from GDP-mannose to lipid-linked oligosaccharide by soluble mannosyl transferase
Proc. Natl. Acad. Sci. USA
77
2524-2527
1980
Sus scrofa
brenda
Jensen, J.W.; Springfield, J.D.; Schutzbach, J.S.
The biosynthesis of oligosaccharide-lipids. Isolation of an oligosaccharide-P-P-lipid acceptor
J. Biol. Chem.
255
11268-11272
1980
Oryctolagus cuniculus
brenda
Prakash, C.; Katial, A.; Kang, M.S.; Vijay, I.K.
Solubilization of mannosyltransferase activities for the biosynthesis of mammary glycoproteins. Elongation of tetrasaccharide-lipid to heptasaccharide-lipid by a solubilized enzyme preparation
Eur. J. Biochem.
139
87-93
1984
Bos taurus
brenda
Cipollo, J.F.; Trimble, R.B.
The Saccharomyces cerevisiae alg12delta mutant reveals a role for the middle-arm alpha1,2Man- and upper-arm alpha1,2Manalpha1,6Man-residues of Glc(3)Man(9)GlcNAc(2)-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus
Glycobiology
12
749-762
2002
Saccharomyces cerevisiae
brenda
Gao, X.D.; Nishikawa, A.; Dean, N.
Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum
Glycobiology
14
559-570
2004
Saccharomyces cerevisiae
brenda
Absmanner, B.; Schmeiser, V.; Kmpf, M.; Lehle, L.
Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide
Biochem. J.
426
205-217
2010
Saccharomyces cerevisiae (P53954), Saccharomyces cerevisiae
brenda
O'Reilly, M.K.; Zhang, G.; Imperiali, B.
In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis
Biochemistry
45
9593-9603
2006
Saccharomyces cerevisiae (P53954), Saccharomyces cerevisiae
brenda
Rind, N.; Schmeiser, V.; Thiel, C.; Absmanner, B.; Lbbehusen, J.; Hocks, J.; Apeshiotis, N.; Wilichowski, E.; Lehle, L.; Krner, C.
A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip
Hum. Mol. Genet.
19
1413-1424
2010
Homo sapiens (Q2TAA5), Homo sapiens
brenda
Cipollo, J.F.; Trimble, R.B.; Chi, J.H.; Yan, Q.; Dean, N.
The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum
J. Biol. Chem.
276
21828-21840
2001
Saccharomyces cerevisiae (P53954), Saccharomyces cerevisiae
brenda
Zhang, M.; Henquet, M.; Chen, Z.; Zhang, H.; Zhang, Y.; Ren, X.; van der Krol, S.; Gonneau, M.; Bosch, D.; Gong, Z.
LEW3, encoding a putative alpha-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana
Plant J.
60
983-999
2009
Arabidopsis thaliana
brenda
Umeda, K.; Yoko-o, T.; Nakayama, K.; Suzuki, T.; Jigami, Y.
Schizosaccharomyces pombe gmd3(+)/alg11(+) is a functional homologue of Saccharomyces cerevisiae ALG11 which is involved in N-linked oligosaccharide synthesis
Yeast
16
1261-1271
2000
Schizosaccharomyces pombe (O74878), Schizosaccharomyces pombe, Saccharomyces cerevisiae (P53954), Saccharomyces cerevisiae
brenda
Ramirez, A.S.; Boilevin, J.; Lin, C.W.; Ha Gan, B.; Janser, D.; Aebi, M.; Darbre, T.; Reymond, J.L.; Locher, K.P.
Chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins
Glycobiology
27
726-733
2017
Saccharomyces cerevisiae (P53954), Saccharomyces cerevisiae ATCC 204508 (P53954)
brenda
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