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Literature summary for 2.4.99.21 extracted from
- Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase (2020), Biomolecules, 10, 32316603 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O29867 | - |
- |
| Archaeoglobus fulgidus ATCC 49558 | O29867 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain | Archaeoglobus fulgidus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AglB protein | - |
Archaeoglobus fulgidus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability | Archaeoglobus fulgidus |
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Release 2023.1 (January 2023)
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