Pyruvate dehydrogenase kinase isoform 2 (PDK2)

Pyruvate dehydrogenase kinase isoform 2 (PDK2) is a mitochondrial enzyme that phosphorylates and inactivates the pyruvate dehydrogenase complex (PDC), thus regulating the entry of pyruvate into the tricarboxylic acid (TCA) cycle and maintaining the balance between glucose oxidation and glycolysis. PDK2 is one of four mammalian PDK isozymes and is encoded by the PDK2 gene on human chromosome 17. It is highly responsive to allosteric effectors, with regulation mediated by metabolites such as NADH, acetyl-CoA, ADP, and CoA-SH, and plays a pivotal role in metabolic adaptation and disease. Inhibition of PDK2 increases PDC activity, shifting cell metabolism from glycolysis toward oxidative phosphorylation, which is of therapeutic interest in conditions like cancer and metabolic syndrome[1][2][3][4][5][6][7].

Other names

Pyruvate dehydrogenase lipoamide kinase isozyme 2, mitochondrialPDHK2PDK P45Pyruvate dehydrogenase kinase, isoenzyme 2

Inhibition of kinase activity (e.g., DCA inhibits PDK2, leading to dephosphorylation and activation of pyruvate dehydrogenase complex) - Allosteric modulation