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Literature summary extracted from

  • Schulz, B.L.; Stirnimann, C.U.; Grimshaw, J.P.; Brozzo, M.S.; Fritsch, F.; Mohorko, E.; Capitani, G.; Glockshuber, R.; Grütter, M.G.; Aebi, M.
    Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency (2009), Proc. Natl. Acad. Sci. USA, 106, 11061-11066.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.99.18 sitting drop vapor diffusion method, dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.4.99.18 additional information mutation of the active-site cysteine residues of Ost6p and its paralogue Ost3p affect the glycosylation efficiency of a subset of glycosylation sites Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Saccharomyces cerevisiae asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. Eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.18 Saccharomyces cerevisiae Q03723 dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.99.18
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 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. Eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding Saccharomyces cerevisiae dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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 ?

Subunits

EC Number Subunits Comment Organism
2.4.99.18 More functional and structural investigations of the Ost3/6p components of the yeast enzyme. Genetic, biochemical and structural analyses of the lumenal domain of Ost6p reveals oxidoreductase activity mediated by a thioredoxin-like fold with a distinctive active-site loop that changed conformation with redox state Saccharomyces cerevisiae