Pyruvate, water dikinase
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
pyruvate, water dikinase | |||||||||
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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 / QuickGO | ||||||||
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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 (CO
2 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.