Pyruvate dehydrogenase (PDH) is a part of a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation.
^Gudi R, Bowker-Kinley M, Kedishvili N, Zhao Y, Popov K (Jan 1996). "Diversity of the pyruvate dehydrogenase kinase gene family in humans". J Biol Chem270 (48): 28989–94. doi:10.1074/jbc.270.48.28989. PMID7499431.
Sugden M, Holness M (2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs". Am. J. Physiol. Endocrinol. Metab.284 (5): E855–62. doi:10.1152/ajpendo.00526.2002 (inactive 2015-01-09). PMID12676647.
Liu S, Baker J, Andrews P, Roche T (1995). "Recombinant expression and evaluation of the lipoyl domains of the dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex". Arch. Biochem. Biophys.316 (2): 926–40. doi:10.1006/abbi.1995.1124. PMID7864652.
Korotchkina L, Patel M (2001). "Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase". J. Biol. Chem.276 (40): 37223–9. doi:10.1074/jbc.M103069200. PMID11486000.