- Pyruvate dehydrogenase kinase
Pyruvate dehydrogenase kinase (also pyruvate dehydrogenase complex kinase, PDC kinase, or PDK; EC number|2.7.11.2) is a
kinase enzyme which acts to inactivate the enzymepyruvate dehydrogenase by phosphorylating it using ATP.PDK thus participates in the regulation of the
pyruvate dehydrogenase complex of which pyruvate dehydrogenase is the first component. Both PDK and the pyruvate dehydrogenase complex are located in themitochondrial matrix ofeukaryote s. The complex acts to convertpyruvate (a product ofglycolysis in thecytosol ) toacetyl-coA , which is then oxidized in the mitochondria to produce energy, in thecitric acid cycle . By downregulating the activity of this complex, PDK will decrease the oxidation of pyruvate in mitochondria and increase the conversion of pyruvate to lactate in the cytosol.The opposite action of PDK, namely the dephosphorylation and activation of pyruvate dehydrogenase, is catalyzed by a
phosphoprotein phosphatase calledpyruvate dehydrogenase phosphatase .Genes
PDK has four
isozymes :
*PDK1
*PDK2
*PDK3
*PDK4 Regulation
Pyruvate dehydrogenase kinase is stimulated by ATP,
NADH andacetyl-CoA .It is inhibited by ADP,
NAD+ ,CoA-SH andpyruvate .Pyruvate dehydrogenase kinase is also inhibited by the drug
dichloroacetic acid which has been tried as a treatment of certain metabolic diseases and is under investigation as a treatment of cancer.External links
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