ENZYME entry: EC 1.8.4.15
| Accepted Name |
|---|
| Protein dithiol oxidoreductase (disulfide-forming).
|
| Reaction catalysed |
|---|
| A [DsbA protein] carrying a disulfide bond + a [protein] with reduced L-cysteine residues <=> a [DsbA protein] with reduced L-cysteine residues + a [protein] carrying a disulfide bond |
| Comment(s) |
|---|
- DsbA is a periplasmic thiol:disulfide oxidoreductase found in Gram-
negative bacteria that promotes protein disulfide bond formation.
- DsbA contains a redox active disulfide bond that is catalytically
transferred via disulfide exchange to a diverse range of newly
translocated protein substrates.
- The protein is restored to the oxidized state by EC 1.8.5.9.
|
| Cross-references |
|---|
| BRENDA | 1.8.4.15 |
| EC2PDB | 1.8.4.15 |
| ExplorEnz | 1.8.4.15 |
| PRIAM enzyme-specific profiles | 1.8.4.15 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.8.4.15 |
| IUBMB Enzyme Nomenclature | 1.8.4.15 |
| IntEnz | 1.8.4.15 |
| MEDLINE | Find literature relating to 1.8.4.15 |
| MetaCyc | 1.8.4.15 |
| Rhea expert-curated reactions | 1.8.4.15 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.8.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.-.-
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