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Literature summary for 4.1.1.49 extracted from
- The kinetic properties of phosphoenolpyruvate carboxykinase of Escherichia coli (1980), Can. J. Biochem., 58, 309-318.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.05 | - |
ADP | - |
Escherichia coli |  |
| 0.06 | - |
ATP | - |
Escherichia coli | |
| 0.07 | - |
phosphoenolpyruvate | - |
Escherichia coli | |
| 0.67 | - |
oxaloacetate | - |
Escherichia coli | |
| 13 | - |
CO2 | CO2 in form of HCO3- | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | activates | Escherichia coli | |
| Mg2+ | Km: 0.09 mM | Escherichia coli | |
| Mn2+ | activation | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2 | sequential mechanism | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + phosphoenolpyruvate + CO2 | - |
Escherichia coli | ATP + oxaloacetate | - |
? | |
| ATP + oxaloacetate | - |
Escherichia coli | ADP + phosphoenolpyruvate + CO2 | - |
? | |
| additional information | catalyzes an exchange reaction between C14O2 and the beta-carboxyl group of oxaloacetate | Escherichia coli | ? | - |
? | |
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