Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Escherichia coli | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
a [protein] carrying a disulfide bond + thioredoxin-1 | Escherichia coli | overall reaction | a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a [protein] carrying a disulfide bond + thioredoxin-1 | overall reaction | Escherichia coli | a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide | - |
? | |
additional information | the enzyme is composed of three domains, each containing two redox-active cysteines. All six of these cysteines are required for enzyme activity. The N-terminal periplasmic domain DsbDalpha directly reduces DsbC. DsbDalpha is then itself reduced by the C-terminal periplasmic domain, DsbDgamma, a thioredoxin-like polypeptide. The resulting oxidized DsbDgamma is reduced by the membrane-embedded DsbDbeta domain that contains eight transmembrane segments. Electrons passed from cytoplasmic thioredoxin 1 restore DsbDbeta to the reduced form, thus allowing it to continue to transfer electrons to DsbDgamma | Escherichia coli | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
DsbD | - |
Escherichia coli |