Polo kinase

2013-04-16T09:00:37Z

193.137.94.3:

{{enzyme
| Name = pyruvate, phosphate dikinase
| EC_number = 2.7.9.1
| CAS_number = 9027-40-1
| IUBMB_EC_number = 2/7/9/1
| GO_code = 0050242
| image =
| width =
| caption =
}}
[[File:PPDK reaction.svg|thumb|350px|Reaction of the pyruvate, phosphate dikinase: the phosphorylation of pyruvate to phosphoenolpyruvate.]]

In [[enzymology]], a '''pyruvate, phosphate dikinase''' ({{EC number|2.7.9.1}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:ATP + pyruvate + phosphate <math>\rightleftharpoons</math> AMP + phosphoenolpyruvate + diphosphate

The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[pyruvate]], and [[phosphate]], whereas its 3 [[product (chemistry)|products]] are [[adenosine monophosphate|AMP]], [[phosphoenolpyruvate]] (PEP), and [[diphosphate]]. With that enzyme, bacteria can also form ATP if the reaction is running backwards.

This enzyme has been studied primarily in plants, but it has been studied in some bacteria as well.<ref name="pmid2176881">{{cite journal | author = Pocalyko DJ, Carroll LJ, Martin BM, Babbitt PC, Dunaway-Mariano D | title = Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs | journal = Biochemistry | volume = 29 | issue = 48 | pages = 10757–65 |date=December 1990 | pmid = 2176881 | doi = 10.1021/bi00500a006| url = | issn = }}</ref> It is a key enzyme in gluconeogenesis and photosynthesis that is responsible for reversing the reaction performed by pyruvate kinase in Embden-Meyerhof-Parnas glycolysis. It should not be confused with [[pyruvate, water dikinase]].

It belongs to the family of [[transferase]]s, to be specific, those transferring phosphorus-containing groups ([[phosphotransferase]]s) with paired acceptors ([[dikinase]]s). The systematic name of this enzyme class is '''ATP:pyruvate, phosphate phosphotransferase'''. Other names in common use include '''pyruvate, orthophosphate dikinase''', '''pyruvate-phosphate dikinase (phosphorylating)''', '''pyruvate, phosphate dikinase''', '''pyruvate-inorganic phosphate dikinase''', '''pyruvate-phosphate dikinase''', '''pyruvate-phosphate ligase''', '''pyruvic-phosphate dikinase''', '''pyruvic-phosphate ligase''', '''pyruvate, Pi dikinase''', and '''PPDK'''. This enzyme participates in [[pyruvate metabolism]] and [[carbon fixation]].

PPDK has been shown to undergo light/dark regulation by the pyruvate dikinase regulatory protein [[PDRP]]. PDRP reversibly phosphorylates Thr456 in the following reaction.
:ADP <math>\rightleftharpoons</math> AMP + phosphate

==Structural studies==

As of late 2007, 10 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1DIK}}, {{PDB link|1GGO}}, {{PDB link|1H6Z}}, {{PDB link|1JDE}}, {{PDB link|1KBL}}, {{PDB link|1KC7}}, {{PDB link|1VBG}}, {{PDB link|1VBH}}, {{PDB link|2DIK}}, and {{PDB link|2FM4}}.

==References==
{{reflist}}

== Further reading ==
{{refbegin}}
* {{cite journal | author = Hatch MD, Slack CR | date = 1968 | title = A new enzyme for the interconversion of pyruvate and phosphopyruvate and its role in the C4 dicarboxylic acid pathway of photosynthesis | journal = Biochem. J. | volume = 106 | pages = 141–6 | pmid = 4305612 | issue = 1 | pmc = 1198479 }}
* {{cite journal | author = Reeves RE | date = 1968 | title = A new enzyme with the glycolytic function of pyruvate kinase | journal = J. Biol. Chem. | volume = 243 | pages = 3202–4 | pmid = 4297474 | issue = 11 }}
* {{cite journal | author = Reeves RE | date = 1971 | title = Pyruvate,phosphate dikinase from Bacteroides symbiosus | journal = Biochem. J. | volume = 125 | pages = 531–9 | pmid = 5144757 | issue = 2 | pmc = 1178089 }}
* {{cite journal | author = Reeves RE, Menzies RA, Hsu DS | date = 1968 | title = The pyruvate-phosphate dikinase reaction. The fate of phosphate and the equilibrium | journal = J. Biol. Chem. | volume = 243 | pages = 5486–91 | pmid = 4302788 | issue = 20 }}
{{refend}}

{{enzyme-stub}}

[[Category:EC 2.7.9]]
[[Category:Enzymes of known structure]]
[[de: Pyruvat-Phosphat-Dikinase]]

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Polo kinase