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Literature summary for 2.5.1.72 extracted from
- Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation (2008), Biochemistry, 47, 8467-8469.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | residues C291 and C294 of the C291XXC294XXC297 motif undergo reversible disulfide formation, which regulates the activity of the enzyme. Disulfide-bond formation and reduction are effected by oxidized and reduced forms of thioredoxin, with a midpoint potential of -264 mV for the redox couple | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | residues C291 and C294 of the C291XXC294XXC297 motif undergo reversible disulfide formation, which regulates the activity of the enzyme | Escherichia coli | ? | - |
? |  |
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