Phosphoenolpyruvate carboxykinase (ATP)
| Phosphoenolpyruvate carboxykinase (ATP) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.1.49 | ||||||||
| CAS number | 9073-94-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49, phosphopyruvate carboxylase (ATP), phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxykinase, phosphopyruvate carboxykinase (adenosine triphosphate), PEP carboxylase, PEP carboxykinase, PEPCK (ATP), PEPK, PEPCK, phosphoenolpyruvic carboxylase, phosphoenolpyruvic carboxykinase, phosphoenolpyruvate carboxylase (ATP), phosphopyruvate carboxykinase, ATP:oxaloacetate carboxy-lyase (transphosphorylating)) is an enzyme with systematic name ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- ATP + oxaloacetate ADP + phosphoenolpyruvate + CO2
See also
References
- ↑ Cannata, J.J.B. (1970). "Phosphoenolpyruvate carboxykinase from bakers' yeast. Isolation of the enzyme and study of its physical properties". J. Biol. Chem. 245: 792–798. PMID 5416663.
- ↑ Cannata, J.J.B.; Stoppani, A.O.M. (1963). "Phosphopyruvate carboxylase from baker's yeast. I. Isolation, purification, and characterization". J. Biol. Chem. 238: 1196–1207. PMID 14018315.
- ↑ Cannata, J.J.B.; Stoppani, A.O.M. (1963). "Phosphopyruvate carboxylase from baker's yeast. II. Properties of enzyme". J. Biol. Chem. 238: 1208–1212. PMID 14018316.
External links
- Phosphoenolpyruvate carboxykinase (ATP) at the US National Library of Medicine Medical Subject Headings (MeSH)
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