Pyruvate dehydrogenase kinase

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Pyruvate dehydrogenase kinase (PDC kinase, PDK) is a kinase enzyme which acts to phosphorylate pyruvate dehydrogenase using ATP.

Pyruvate dehydrogenase kinase participates in the regulation of the pyruvate dehydrogenase complex. When phosphorylated, pyruvate dehydrogenase is inactivated. Dephosphorylation and activation of pyruvate dehydrogenase is catalyzed by a phosphoprotein phosphatase called pyruvate dehydrogenase phosphatase.

Genes

It has four isozymes:

Pyruvate dehydrogenase kinase is stimulated by ATP, NADH and acetyl-CoA.

It is inhibited by ADP, NAD+, CoA-SH and pyruvate.

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v • d • e Kinases: Serine/threonine-specific protein kinases (primarily EC 2.7.11)
2.7.11	Pyruvate dehydrogenase kinase - Protein kinase A - Protein kinase G - Protein kinase C (Protein kinase Mζ) - Rhodopsin - Beta adrenergic receptor - G-protein coupled receptor kinases - Ca2+/calmodulin-dependent - Myosin light-chain) - Phosphorylase - Cyclin-dependent - Mitogen-activated (Extracellular signal-regulated, C-Jun N-terminal (MAPK8, MAPK9), P38 mitogen-activated protein) - MAP3K - GSK-3 - AMP-activated
2.7.12	MAP2K (1, 2, 3, 4, 5, 6, 7)
2.7.1.37, or unknown	Anti-Mullerian hormone receptor - Ataxia telangiectasia mutated - Aurora (A, B) - Mammalian target of rapamycin - Bone morphogenetic protein receptors (1, 2) - CDKL5 - c-Raf - EIF-2 - Ribosomal s6 - Protein kinase B - PDK1