Crystallization (Comment) | Organism |
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sitting drop vapor diffusion method, dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6 | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
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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 | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q03723 | dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6 | - |
Purification (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 |