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Literature summary for 1.8.4.2 extracted from
- Influence of the pKa value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases (2000), FEBS Lett., 477, 21-26.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol | C-X-X-C motif in active site for disulfide bonding, either oxidizing, reducing and isomerising activity | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GSH + protein disulfide | protein disulfide: thioredoxin | Escherichia coli | GSSG + protein-dithiol | - |
r |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | thiol-disulfide oxidoreductase of the thioredoxin family | Escherichia coli |
| thiol-disulfide oxidoreductase | - |
Escherichia coli |
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