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Literature summary extracted from
- The binding of Na(+) to apo-enolase permits the binding of substrate (2000), Biochim. Biophys. Acta, 1476, 279-286.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.11 | NaClO4 | inactivation is due to dissociation of the enolase into inactive monomers, 2-phospho-D-glycerate prevents this inactivation | Oryctolagus cuniculus |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.11 | Mg2+ | three binding sites, binding at the first two is required for activity, binding at the third site is inhibitory | Oryctolagus cuniculus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.11 | Oryctolagus cuniculus | - |
rabbit | - |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 4.2.1.11 | muscle | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.11 | 2-phospho-D-glycerate | - |
Oryctolagus cuniculus | phosphoenolpyruvate | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.11 | beta,beta-enolase | - |
Oryctolagus cuniculus |
| 4.2.1.11 | enolase | - |
Oryctolagus cuniculus |
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Release 2023.1 (January 2023)
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