- Pyruvate dehydrogenase kinase
Pyruvate dehydrogenase kinase (also pyruvate dehydrogenase complex kinase, PDC kinase, or PDK; EC number|22.214.171.124) is a
kinase enzymewhich acts to inactivate the enzyme pyruvate dehydrogenaseby phosphorylating it using ATP.
PDK thus participates in the regulation of the
pyruvate dehydrogenase complexof which pyruvate dehydrogenase is the first component. Both PDK and the pyruvate dehydrogenase complex are located in the mitochondrial matrixof eukaryotes. The complex acts to convert pyruvate(a product of glycolysisin the cytosol) to acetyl-coA, which is then oxidized in the mitochondria to produce energy, in the citric 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 phosphatasecalled pyruvate dehydrogenase phosphatase.
PDK has four
Pyruvate dehydrogenase kinase is stimulated by ATP,
It is inhibited by ADP,
NAD+, CoA-SHand pyruvate.
Pyruvate dehydrogenase kinase is also inhibited by the drug
dichloroacetic acidwhich has been tried as a treatment of certain metabolic diseases and is under investigation as a treatment of cancer.
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