“Pyruvate, water dikinase”的意思、由来-开放百科全书

词条

Pyruvate, water dikinase

释义

Structural studies
References

{{enzyme
| Name = pyruvate, water dikinase
| EC_number = 2.7.9.2
| CAS_number = 9013-09-6
| IUBMB_EC_number = 2/7/9/2
| GO_code = 0008986
| image =
| width =
| caption =
}}

In enzymology, a pyruvate, water dikinase ({{EC number|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 {{PDB link|2OLS}}.

References

{{cite journal | vauthors = Berman KM, Cohn M | date = 1970 | title = Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions | journal = J. Biol. Chem. | volume = 245 | pages = 5309–18 | pmid = 4319237 | issue = 20 }}
{{cite journal | vauthors = Berman KM, Cohn M | date = 1970 | title = Phosphoenolpyruvate synthetase. Partial reactions studied with adenosine triphosphate analogues and the inorganic phosphate-H2 18O exchange reaction | journal = J. Biol. Chem. | volume = 245 | pages = 5319–25 | pmid = 4319238 | issue = 20 }}
{{cite journal | vauthors = Cooper RA, Kornberg HL | date = 1965 | title = Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli | journal = Biochim. Biophys. Acta | volume = 104 | pages = 618–20 | pmid = 5322808 | issue = 2 | doi=10.1016/0304-4165(65)90374-0}}
{{cite journal |author1 = Cooper RA |author2 =Kornberg HL | date = 1969 | title = Phosphoenolpyruvate synthetase | journal = Methods Enzymol. | volume = 13 | pages = 309–314 | doi = 10.1016/0076-6879(69)13053-0 | series = Methods in Enzymology | isbn = 978-0-12-181870-8 }}

3 : EC 2.7.9|Manganese enzymes|Enzymes of known structure

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