| pyruvate, water dikinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.9.2 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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 reaction catalyzed by pyruvate, water dikinase can run in both directions, but has a strong preference for AMP, phosphate, and phosphoenolpyruvate as substrate and typically runs in the ATP producing direction.[1][2]
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, PEP synthase, PEPS, phoephoenolpyruvate synthetase, phosphoenolpyruvic synthase, and phosphopyruvate synthetase. This enzyme participates in pyruvate metabolism and reductive carboxylate cycle (CO2 fixation). It employs one cofactor, manganese.
- ^ Hutchins, A. M.; Holden, J. F.; Adams, M. W. (2001). "Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus". Journal of Bacteriology. 183 (2): 709–715. doi:10.1128/JB.183.2.709-715.2001. ISSN 0021-9193. PMC 94928. PMID 11133966.
- ^ Sakuraba, H.; Utsumi, E.; Kujo, C.; Ohshima, T. (1999-04-01). "An AMP-dependent (ATP-forming) kinase in the hyperthermophilic archaeon Pyrococcus furiosus: characterization and novel physiological role". Archives of Biochemistry and Biophysics. 364 (1): 125–128. doi:10.1006/abbi.1999.1121. ISSN 0003-9861. PMID 10087174.