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Information on EC 2.4.1.131 - GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53954
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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 taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
alg11, halg11, gdp-man:man3glcnac2-pp-dolichol-alpha1,2-mannosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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 TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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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.
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
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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
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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?
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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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
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
?
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
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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
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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?
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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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63140
63143
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
ALG9 gene encodes a middle-arm terminal alpha1,2-mannosyltransferase Alg9p
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
Saccharomyces cerevisiae (P53954), Saccharomyces cerevisiae, Schizosaccharomyces pombe (O74878), Schizosaccharomyces pombe
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)
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