Pyruvate dehydrogenase (E1) is one of the three components (E1, E2, and E3) of the large pyruvate dehydrogenase complex. Pyruvate dehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex. Pyruvate dehydrogenase phosphatases catalyze the dephosphorylation and activation of the E1 component to reverse the effects of pyruvate dehydrogenase kinases. Pyruvate dehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits. Two catalytic subunits have been reported; one is predominantly expressed in skeletal muscle and another one is much more abundant in the liver. The catalytic subunit, encoded by this gene, is the former, and belongs to the protein phosphatase 2C (PP2C) superfamily. Along with the pyruvate dehydrogenase complex and pyruvate dehydrogenase kinases, this enzyme is located in the mitochondrial matrix.
^Lawson JE, Niu XD, Browning KS, Trong HL, Yan J, Reed LJ (September 1993). "Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C". Biochemistry32 (35): 8987–93. doi:10.1021/bi00086a002. PMID8396421.
Piccinini M, Mostert M, Alberto G et al. (2005). "Down-regulation of pyruvate dehydrogenase phosphatase in obese subjects is a defect that signals insulin resistance". Obes. Res.13 (4): 678–86. doi:10.1038/oby.2005.76. PMID15897476.
Auffray C, Behar G, Bois F et al. (1995). "[IMAGE: molecular integration of the analysis of the human genome and its expression]". C. R. Acad. Sci. III, Sci. Vie318 (2): 263–72. PMID7757816.
Lejeune F, Li X, Maquat LE (2003). "Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities". Mol. Cell12 (3): 675–687. doi:10.1016/S1097-2765(03)00349-6. PMID14527413.
Cameron JM, Maj M, Levandovskiy V et al. (2009). "Pyruvate dehydrogenase phosphatase 1 (PDP1) null mutation produces a lethal infantile phenotype". Hum. Genet.125 (3): 319–26. doi:10.1007/s00439-009-0629-6. PMID19184109.
Maj MC, MacKay N, Levandovskiy V et al. (2005). "Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation". J. Clin. Endocrinol. Metab.90 (7): 4101–7. doi:10.1210/jc.2005-0123. PMID15855260.
Sugden MC, Holness MJ (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. PMID12676647.
Korotchkina LG, Patel MS (1995). "Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation". J. Biol. Chem.270 (24): 14297–304. doi:10.1074/jbc.270.24.14297. PMID7782287.
Stellingwerff T, Spriet LL, Watt MJ et al. (2006). "Decreased PDH activation and glycogenolysis during exercise following fat adaptation with carbohydrate restoration". Am. J. Physiol. Endocrinol. Metab.290 (2): E380–8. doi:10.1152/ajpendo.00268.2005. PMID16188909.
Ito M, Kobashi H, Naito E et al. (1992). "Decrease of pyruvate dehydrogenase phosphatase activity in patients with congenital lactic acidemia". Clin. Chim. Acta209 (1–2): 1–7. doi:10.1016/0009-8981(92)90327-M. PMID1327585.
Adams MD, Kerlavage AR, Fleischmann RD et al. (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence". Nature377 (6547 Suppl): 3–174. PMID7566098.
Caruso M, Maitan MA, Bifulco G et al. (2001). "Activation and mitochondrial translocation of protein kinase Cdelta are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells". J. Biol. Chem.276 (48): 45088–97. doi:10.1074/jbc.M105451200. PMID11577086.