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Literature summary extracted from

  • Schulz, B.L.; Aebi, M.
    Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency (2009), Mol. Cell. Proteomics, 8, 357-364.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.99.18 plasmids with subunit genes introduced into mutants lacking both subunits Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.4.99.18 additional information strains with deleted OST3 and OST6 loci are grown with plasmids introducing either one of the subunits Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.18 N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall Saccharomyces cerevisiae glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616 ?
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Organism

EC Number Organism UniProt Comment Textmining
2.4.99.18 Saccharomyces cerevisiae
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.18 N-acetyl-D-glucosamine + glycoprotein bound to polysaccharide cell wall glycoproteins as substrates are P15703, O13547, P53301, P32623, P28319, P38248, P22146, Q03655, Q08193, P38616 Saccharomyces cerevisiae ?
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?

Synonyms

EC Number Synonyms Comment Organism
2.4.99.18 oligosaccharyltransferase
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Saccharomyces cerevisiae
2.4.99.18 OST subunit Ost3p and Ost6p Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.4.99.18 physiological function subunits Ost3p and Ost6p are necessary for efficient glycosylation of distinct defined glycosylation sites Saccharomyces cerevisiae