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Literature summary for 2.4.1.132 extracted from

  • 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 (2006), Biochemistry, 45, 9593-9603.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E335A significant lower level of product formation Saccharomyces cerevisiae
E335A/E343A significant lower level of product formation, identical to that of the E335A mutant Saccharomyces cerevisiae
E343A no activity Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
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Saccharomyces cerevisiae 16020
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Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P43636
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-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-alpha-D-mannose + 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 Saccharomyces cerevisiae GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
?
GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol Alg2 carries out an alpha1,3-mannosylation of Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway Saccharomyces cerevisiae GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
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?
additional information Alg2 shows no activity with D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol Saccharomyces cerevisiae ?
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?

Synonyms

Synonyms Comment Organism
Alg2
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Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Saccharomyces cerevisiae