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Literature summary for 4.1.1.31 extracted from
- Kinetics and equilibrium binding of phosphoenolpyruvate to phosphoenolpyruvate carboxylase from Zea mays (1999), Phys. Chem. Chem. Phys., 1, 455-461.
No PubMed abstract available
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.1 | - |
phosphoenolpyruvate | pH 8.0 | Zea mays |  |
| 8.7 | - |
phosphoenolpyruvate | pH 7.0 | Zea mays | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Zea mays | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphoenolpyruvate + CO2 | concerted sequential allosteric mechanism | Zea mays | phosphate + oxaloacetate | - |
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