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
Identifiers
EC number2.7.9.2
CAS number9013-09-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

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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.


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