ENZYME entry: EC 1.8.5.9
| Accepted Name |
|---|
| Protein dithiol:quinone oxidoreductase DsbB.
|
| Reaction catalysed |
|---|
| A [DsbA protein] with reduced L-cysteine residues + a quinone <=> a [DsbA protein] carrying a disulfide bond + a quinol (overall reaction) |
| Comment(s) |
|---|
- DsbB is a protein found in Gram-negative bacteria that functions
within a pathway for protein disulfide bond formation.
- The enzyme catalyzes the oxidation of the DsbA protein by generating
disulfide bonds de novo via the reduction of membrane quinones.
- Cf. EC 1.8.4.15.
|
| Cross-references |
|---|
| BRENDA | 1.8.5.9 |
| EC2PDB | 1.8.5.9 |
| ExplorEnz | 1.8.5.9 |
| PRIAM enzyme-specific profiles | 1.8.5.9 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.8.5.9 |
| IUBMB Enzyme Nomenclature | 1.8.5.9 |
| IntEnz | 1.8.5.9 |
| MEDLINE | Find literature relating to 1.8.5.9 |
| MetaCyc | 1.8.5.9 |
| Rhea expert-curated reactions | 1.8.5.9 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.8.5.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-