PDK1

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

Pyruvate dehydrogenase kinase, isozyme 1
Rendering based on PDB 2Q8F.
Available structures PDB 2Q8F, 2Q8G, 2Q8H
Identifiers
Symbols	PDK1;
External IDs	OMIM: 602524 MGI: 1926119 HomoloGene: 20576 GeneCards: PDK1 Gene
EC number	2.7.11.2
Gene Ontology Molecular function • two-component sensor activity • nucleotide binding • protein kinase activity • pyruvate dehydrogenase (acetyl-transferring) kinase activity • ATP binding • transferase activity • protein complex binding • protein homodimerization activity • protein heterodimerization activity Cellular component • mitochondrion • mitochondrial matrix • pyruvate dehydrogenase complex Biological process • carbohydrate metabolic process • glucose metabolic process • pyruvate metabolic process • protein phosphorylation • protein phosphorylation • cell surface receptor linked signaling pathway • small GTPase mediated signal transduction • regulation of acetyl-CoA biosynthetic process from pyruvate • peptidyl-histidine phosphorylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5163	228026
Ensembl	ENSG00000152256	ENSMUSG00000006494
UniProt	Q15118	Q3U5E5
RefSeq (mRNA)	NM_002610.3	NM_172665.4
RefSeq (protein)	NP_002601.1	NP_766253.2
Location (UCSC)	Chr 2: 173.42 – 173.49 Mb	Chr 2: 71.71 – 71.74 Mb
PubMed search	[1]	[2]

Pyruvate dehydrogenase lipoamide kinase isozyme 1, mitochondrial is an enzyme that in humans is encoded by the PDK1 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.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.

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Citric_acid_cycle edit

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 (inactive 2008-06-23). PMID 12676647. 
• 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. doi:10.1006/abbi.1995.1124. 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. doi:10.1042/0264-6021:3580069. PMC 1222033. PMID 11485553. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222033. 
• 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. PMC 1222743. PMID 11978179. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222743.