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 |
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