Pyruvate, water dikinase
| pyruvate, water dikinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.9.2 | ||||||||
| CAS number | 9013-09-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a pyruvate, water dikinase (EC 2.7.9.2) is an enzyme that catalyzes the chemical reaction
- ATP + pyruvate + H2O AMP + phosphoenolpyruvate + phosphate
The 3 substrates of this enzyme are ATP, pyruvate, and H2O, whereas its 3 products are AMP, phosphoenolpyruvate, and phosphate.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:pyruvate, water phosphotransferase. Other names in common use include phosphoenolpyruvate synthase, pyruvate-water dikinase (phosphorylating), PEP synthetase, phosphoenolpyruvate synthase, phoephoenolpyruvate synthetase, phosphoenolpyruvic synthase, and phosphopyruvate synthetase. This enzyme participates in pyruvate metabolism and reductive carboxylate cycle (CO2 fixation). It employs one cofactor, manganese.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2OLS.
References
- Berman KM, Cohn M (1970). "Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions". J. Biol. Chem. 245 (20): 5309–18. PMID 4319237.
- Berman KM, Cohn M (1970). "Phosphoenolpyruvate synthetase. Partial reactions studied with adenosine triphosphate analogues and the inorganic phosphate-H2 18O exchange reaction". J. Biol. Chem. 245 (20): 5319–25. PMID 4319238.
- Cooper RA, Kornberg HL (1965). "Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli". Biochim. Biophys. Acta. 104 (2): 618–20. doi:10.1016/0304-4165(65)90374-0. PMID 5322808.
- Cooper RA; Kornberg HL (1969). "Phosphoenolpyruvate synthetase". Methods Enzymol. Methods in Enzymology. 13: 309–314. doi:10.1016/0076-6879(69)13053-0. ISBN 978-0-12-181870-8.