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Enzyme Nomenclature
Information on EC 2.4.1.257 - GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae
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EC NUMBER 
COMMENTARY 
2.4.1.257
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RECOMMENDED NAME
GeneOntology No.
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose + alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = GDP + 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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
GDP-D-mannose:D-Man-alpha-(1->3)-D-Man-beta-(1-4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-6-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation (cf. EC 2.4.1.132) of beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + 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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Alg2 shows no activity with D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol
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GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + 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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in eukaryotes, biosynthesis of N-glycans starts with the assembly of the common core oligosaccharide precursor Glc3Man9 GlcNAc2-PP-Dol, the glycan moiety of which is subsequently transferred onto selected Asn-Xaa-(Ser/Thr) acceptor sites of the nascent polypeptide chain by the oligosaccharyl-transferase complex
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?
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + 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 glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
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?
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
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?
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + 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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Alg2 is able to catalyze both the addition of the alpha1,3- and alpha1,6-linked mannose residue to Man1GlcNAc2-PP-Dol, forming Man2GlcNAc2-PP-Dol (cf. EC 2.4.1.132) and subsequently to Man3GlcNAc2-PP-Dol
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + 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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in eukaryotes, biosynthesis of N-glycans starts with the assembly of the common core oligosaccharide precursor Glc3Man9 GlcNAc2-PP-Dol, the glycan moiety of which is subsequently transferred onto selected Asn-Xaa-(Ser/Thr) acceptor sites of the nascent polypeptide chain by the oligosaccharyl-transferase complex
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?
GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
P43636
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
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?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E335A
E335A/E343A
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significant lower level of product formation, identical to that of the E335A mutant
E343A
additional information
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mutational analysis of Alg2 and identification of amino acids required for its activity. None of the four domains (predicted as transmembrane-spanning helices) is essential for transferase activity because truncated Alg2 variants can exert their function as long as Alg2 is associated with the endaplasmic reticulum by either its N- or C-terminal hydrophobic regions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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engineering of a synthetic pathway in Escherichia coli for the production of eukaryotic trimannosyl chitobiose glycans and the transfer of these glycans to specific asparagine residues in target proteins. Glycan biosynthesis is enabled by four eukaryotic glycosyltransferases, including the yeast uridine diphosphate-N-acetylglucosamine transferases Alg13 and Alg14 and the mannosyltransferases Alg1 and Alg2. By including the bacterial oligosaccharyltransferase PglB from Campylobacter jejuni, glycans are successfully transferred to eukaryotic proteins
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.257)
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