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Literature summary for 2.4.99.19 extracted from
- Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase (2020), Biomolecules, 10, 624 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Campylobacter lari | B9KDD4 | - |
- |
| Campylobacter lari RM2100 | B9KDD4 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain | Campylobacter lari |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PglB protein | - |
Campylobacter lari |
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 | Campylobacter lari |
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Release 2023.1 (January 2023)
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