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Literature summary extracted from

  • Absmanner, B.; Schmeiser, V.; Kämpf, 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 (2010), Biochem. J., 426, 205-217.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.131 E318A mutation has no effect on activity Saccharomyces cerevisiae
2.4.1.131 E356A mutation has no effect on activity Saccharomyces cerevisiae
2.4.1.131 E405/H406A double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression Saccharomyces cerevisiae
2.4.1.131 E405A mutation causes an underglycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 E405A/E413 double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression Saccharomyces cerevisiae
2.4.1.131 E413A mutation has no effect Saccharomyces cerevisiae
2.4.1.131 F407A mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 G84A mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 G84P mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 G85A mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 G85P mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 G87A mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 G87P mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 H406A mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y Saccharomyces cerevisiae
2.4.1.131 K302A mutation has no effect on activity Saccharomyces cerevisiae
2.4.1.131 K319A mutation causes loss of Alg11 activity Saccharomyces cerevisiae
2.4.1.131 K322A mutation has no effect on activity Saccharomyces cerevisiae
2.4.1.131 K343A mutation has no effect on activity Saccharomyces cerevisiae
2.4.1.131 V412A mutation is not detrimental for growth Saccharomyces cerevisiae

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.131 63140
-
 calculated from sequence Saccharomyces cerevisiae
2.4.1.131 63143
-
 x * 63143, calculated from sequence Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.131 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 Saccharomyces cerevisiae 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 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.131 Saccharomyces cerevisiae P53954
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.131 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
-
 Saccharomyces cerevisiae 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
-
 ?
2.4.1.131 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 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 Saccharomyces cerevisiae 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
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.131 ? x * 63143, calculated from sequence Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.4.1.131 Alg11
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.131 26
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.131 6
-
 assay at Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.4.1.131 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 Saccharomyces cerevisiae