PDK1

Not to be confused with the master kinase PDK1, 3-phosphoinositide-dependent protein kinase (PDPK1).

Pyruvate dehydrogenase kinase, isozyme 1
Identifiers
Symbols	PDK1 ;
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20576
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PDK1 206686 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Pyruvate dehydrogenase kinase, isozyme 1, also known as PDK1, is a human gene. It codes for an isozyme of pyruvate dehydrogenase kinase (PDK).

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.

Further reading

• 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. PMID 12676647.
• Gudi R, Bowker-Kinley MM, Kedishvili NY; et al. (1996). "Diversity of the pyruvate dehydrogenase kinase gene family in humans". J. Biol. Chem. 270 (48): 28989–94. PMID 7499431.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Liu S, Baker JC, Andrews PC, Roche TE (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. PMID 7864652.CS1 maint: Multiple names: authors list (link)
• Kolobova E, Tuganova A, Boulatnikov I, Popov KM (2001). "Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites". Biochem. J. 358 (Pt 1): 69–77. PMID 11485553.CS1 maint: Multiple names: authors list (link)
• Korotchkina LG, Patel MS (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. PMID 11486000.
• Tuganova A, Boulatnikov I, Popov KM (2002). "Interaction between the individual isoenzymes of pyruvate dehydrogenase kinase and the inner lipoyl-bearing domain of transacetylase component of pyruvate dehydrogenase complex". Biochem. J. 366 (Pt 1): 129–36. doi:10.1042/BJ20020301. PMID 11978179.CS1 maint: Multiple names: authors list (link)