ENZYME entry: EC 1.8.4.16
| Accepted Name |
|---|
| Thioredoxin:protein disulfide reductase.
|
| Reaction catalysed |
|---|
| A [protein] with reduced L-cysteine residues + thioredoxin disulfide <=> a [protein] carrying a disulfide bond + thioredoxin |
| Comment(s) |
|---|
- DsbD is an inner membrane protein found in Gram-negative bacteria
that transfers electrons from cytoplasmic thioredoxin to the
periplasmic substrate proteins DsbC, DsbG and CcmG, reducing
disulfide bonds in the target proteins to dithiols.
- DsbD consists of three domains: a periplasmic N-terminal domain,
a central transmembrane domain and a periplasmic C-terminal domain.
|
| Cross-references |
|---|
| BRENDA | 1.8.4.16 |
| EC2PDB | 1.8.4.16 |
| ExplorEnz | 1.8.4.16 |
| PRIAM enzyme-specific profiles | 1.8.4.16 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.8.4.16 |
| IUBMB Enzyme Nomenclature | 1.8.4.16 |
| IntEnz | 1.8.4.16 |
| MEDLINE | Find literature relating to 1.8.4.16 |
| MetaCyc | 1.8.4.16 |
| Rhea expert-curated reactions | 1.8.4.16 |
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