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Literature summary for 2.4.99.18 extracted from
- The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast (2005), Glycobiology, 15, 1396-1406.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 500000 | - |
non-denaturing gel electrophoresis | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dolichyl diphosphooligosaccharide + [protein]-L-asparagine | Saccharomyces cerevisiae | oligosaccharyltransferase complex catalyzes the transfer of a lipid-linked core oligosaccharide onto asparagine residues of nascent polypeptide chains in the lumen of the endoplasmic reticulum | dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dolichyl diphosphooligosaccharide + [protein]-L-asparagine | - |
Saccharomyces cerevisiae | dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine | - |
? | |
| dolichyl diphosphooligosaccharide + [protein]-L-asparagine | oligosaccharyltransferase complex catalyzes the transfer of a lipid-linked core oligosaccharide onto asparagine residues of nascent polypeptide chains in the lumen of the endoplasmic reticulum | Saccharomyces cerevisiae | dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | six different subunits are detected in the wild-type complex, including Stt3p, Ost1p, Wbp1p, Swp1p, Ost3p, and Ost6p. The small 3.4-kDa subunit Ost4p is required for the incorporation of either Ost3p or Ost6p into the complex, resulting in two, functionally distinct OTase complexes in vivo. Ost3p and Ost6p are not absolutely required for OTase activity, but modulate the affinity of the enzyme toward different protein substrates | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| oligosaccharyltransferase | - |
Saccharomyces cerevisiae |
| OTase | - |
Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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