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Literature summary extracted from

  • Kämpf, M.; Absmanner, B.; Schwarz, M.; Lehle, L.
    Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis (2009), J. Biol. Chem., 284, 11900-11912.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.132 D203A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 D248A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 E264A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 E335A mutant has some residual activity Saccharomyces cerevisiae
2.4.1.132 E343A inactive mutant enzyme Saccharomyces cerevisiae
2.4.1.132 G337A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 G337E nonfunctional enzyme variant Saccharomyces cerevisiae
2.4.1.132 G337R nonfunctional enzyme variant Saccharomyces cerevisiae
2.4.1.132 G338A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 H336A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 K206A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 K210A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 K229A mutation has no effect on growth and glycosylation Saccharomyces cerevisiae
2.4.1.132 K230A mutation causes loss of Alg2 activity Saccharomyces cerevisiae
2.4.1.132 K251A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 additional information 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 Saccharomyces cerevisiae
2.4.1.132 N231A mutation has no effect on growth and glycosylation Saccharomyces cerevisiae
2.4.1.132 N392A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 P192A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.132 P359A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 D203A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 D248A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 E264A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 E335A mutant has some residual activity Saccharomyces cerevisiae
2.4.1.257 E343A inactive mutant enzyme Saccharomyces cerevisiae
2.4.1.257 G337A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 G337E nonfunctional enzyme variant Saccharomyces cerevisiae
2.4.1.257 G337R nonfunctional enzyme variant Saccharomyces cerevisiae
2.4.1.257 G338A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 H336A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 K206A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 K210A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 K229A mutation has no effect on growth and glycosylation Saccharomyces cerevisiae
2.4.1.257 K230A mutation causes loss of Alg2 activity Saccharomyces cerevisiae
2.4.1.257 K251A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 additional information 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 Saccharomyces cerevisiae
2.4.1.257 N231A mutation has no effect on growth and glycosylation Saccharomyces cerevisiae
2.4.1.257 N392A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 P192A mutation has no influence on Alg2 function Saccharomyces cerevisiae
2.4.1.257 P359A mutation has no influence on Alg2 function Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.132 membrane
-
 Saccharomyces cerevisiae 16020
-
2.4.1.257 membrane
-
 Saccharomyces cerevisiae 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.132 GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol Saccharomyces cerevisiae 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 GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
 ?
2.4.1.257 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol Saccharomyces cerevisiae 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 GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.132 Saccharomyces cerevisiae P43636
-
-
2.4.1.257 Saccharomyces cerevisiae P43636
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.132 no glycoprotein
-
 Saccharomyces cerevisiae
2.4.1.257 no glycoprotein
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.132 GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 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 Saccharomyces cerevisiae GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
 ?
2.4.1.132 GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol Alg2 is able to catalyze both the addition of the alpa1,3- 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 Saccharomyces cerevisiae GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
 ?
2.4.1.257 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 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 Saccharomyces cerevisiae GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
 ?
2.4.1.257 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 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 Saccharomyces cerevisiae GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.132 Alg2
-
 Saccharomyces cerevisiae
2.4.1.132 Alg2 mannosyltransferase
-
 Saccharomyces cerevisiae
2.4.1.257 Alg2
-
 Saccharomyces cerevisiae
2.4.1.257 Alg2 mannosyltransferase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.132 26
-
 assay at Saccharomyces cerevisiae
2.4.1.257 26
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.132 6
-
 assay at Saccharomyces cerevisiae
2.4.1.257 6
-
 assay at Saccharomyces cerevisiae