Literature summary for 2.4.1.131 extracted from

Absmanner, B.; Schmeiser, V.; K�mpf, 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.

Search for more literature for 2.4.1.131

Protein Variants

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

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P53954	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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 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

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

Synonyms

Synonyms	Comment	Organism
Alg11	-	Saccharomyces cerevisiae

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)