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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
BRENDA1.8.4.16
EC2PDB1.8.4.16
ExplorEnz1.8.4.16
PRIAM enzyme-specific profiles1.8.4.16
KEGG Ligand Database for Enzyme Nomenclature1.8.4.16
IUBMB Enzyme Nomenclature1.8.4.16
IntEnz1.8.4.16
MEDLINEFind literature relating to 1.8.4.16
MetaCyc1.8.4.16
Rhea expert-curated reactions1.8.4.16

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.8.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-