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Literature summary for 6.2.1.4 extracted from
- Evidence for allosteric regulation of succinyl-CoA synthetase (1993), Biochem. J., 295, 821-826.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Dictyostelium discoideum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + succinate + CoA | - |
Dictyostelium discoideum | GDP + phosphate + succinyl-CoA | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| GDP | allosteric regulator, at high concentration it serves as a substrate. However 100fold lower concentrations of GDP, which do not bind to the catalytic site to induce succinyl-CoA synthetase dephosphorylation, stimulate phosphorylation of p36, the alpha-subunit of succinyl-CoA synthetase | Dictyostelium discoideum | |
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Release 2023.1 (January 2023)
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