EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
   1.8.4.16 | a [protein] carrying a disulfide bond + thioredoxin |
overall reaction |
Escherichia coli |
a [protein] with reduced L-cysteine residues + thioredoxin disulfide |
- |
? |
| 1.8.4.16 | a [protein] carrying a disulfide bond + thioredoxin |
overall reaction |
Escherichia coli |
a [protein] with reduced L-cysteine residues + thioredoxin disulfide |
? |
- |
| 1.8.4.16 | a [protein] carrying a disulfide bond + thioredoxin-1 |
overall reaction |
Escherichia coli |
a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide |
- |
? |
| 1.8.4.16 | a [protein] with reduced L-cysteine residues + thioredoxin disulfide |
overall reaction |
Escherichia coli |
a [protein] carrying a disulfide bond + thioredoxin |
- |
? |
| 1.8.4.16 | insulin + dithiothreitol |
- |
Escherichia coli |
reduced insulin + oxidized dithiothreitol |
- |
? |
| 1.8.4.16 | more |
electron transfer by the enzyme involves sequential reduction and oxidation of its three structural domains, in which reducing potential is transferred from cytoplasmic thioredoxin to the beta domain, then successively to gamma and alpha, and thence to periplasmic substrates. Formation of a disulfide bond between cysteines 163 and 285 of the beta domain is part of the mechanism of the transmembrane electron transfer by the enzyme |
Escherichia coli |
? |
- |
- |
| 1.8.4.16 | more |
the enzyme does not catalyze the reduction of the disulfide of the thioredoxin-like oxidant DsbA |
Escherichia coli |
? |
- |
- |
| 1.8.4.16 | more |
the enzyme includes three domains, each containing a pair of cysteine residues that perform a series of disulfide exchange reactions. In the first step, the transmembrane domain accepts electrons from thioredoxin in the cytoplasm; these are then transferred to the periplasmic C-terminal domain and finally to the N-terminal domain, which is also located in the periplasm |
Escherichia coli |
? |
- |
- |
| 1.8.4.16 | more |
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 |
? |
- |
- |
| 1.8.4.16 | more |
the enzyme transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment |
Escherichia coli |
? |
- |
- |
