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Pyruvate dehydrogenase kinase, isozyme 1
Symbol(s) PDK1;
External IDs OMIM: 602524 MGI1926119 Homologene20576
RNA expression pattern


More reference expression data

Human Mouse
Entrez 5163 228026
Ensembl ENSG00000152256 ENSMUSG00000006494
Uniprot Q15118 Q3U5E5
Refseq NM_002610 (mRNA)
NP_002601 (protein)
NM_172665 (mRNA)
NP_766253 (protein)
Location Chr 2: 173.13 - 173.17 Mb Chr 2: 71.67 - 71.7 Mb
Pubmed search [1] [2]

Pyruvate dehydrogenase kinase, isozyme 1, also known as PDK1, is a human gene.[1] 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.[1]


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. PMID 12676647. doi:10.1152/ajpendo.00526.2002. 
  • 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. 
  • 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. 
  • 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. 
  • 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. PMID 11486000. doi:10.1074/jbc.M103069200. 
  • 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. PMID 11978179. doi:10.1042/BJ20020301.