Pyruvate, phosphate dikinase

pyruvate, phosphate dikinase
Identifiers
EC number 2.7.9.1
CAS number 9027-40-1
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 / EGO

In enzymology, a pyruvate, phosphate dikinase (EC 2.7.9.1) is an enzyme that catalyzes the chemical reaction

ATP + pyruvate + phosphate \rightleftharpoons AMP + phosphoenolpyruvate + diphosphate

The 3 substrates of this enzyme are ATP, pyruvate, and phosphate, whereas its 3 products are 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.[1] It is a key enzyme in gluconeogensis 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 transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). 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 \rightleftharpoons AMP + phosphate

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1DIK, 1GGO, 1H6Z, 1JDE, 1KBL, 1KC7, 1VBG, 1VBH, 2DIK, and 2FM4.

References

  1. ^ Pocalyko DJ, Carroll LJ, Martin BM, Babbitt PC, Dunaway-Mariano D (December 1990). "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". Biochemistry 29 (48): 10757–65. doi:10.1021/bi00500a006. PMID 2176881. 

Further reading