PDK3

Pyruvate dehydrogenase kinase, isozyme 3
PDB rendering based on 1y8n.
Available structures PDB 1Y8N, 1Y8O, 1Y8P, 2PNR, 2Q8I
Identifiers
Symbols	PDK3;
External IDs	OMIM: 602526 MGI: 2384308 HomoloGene: 55897 GeneCards: PDK3 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 • protein binding • ATP binding • transferase activity Cellular component • mitochondrion • mitochondrial matrix Biological process • carbohydrate metabolic process • glucose metabolic process • pyruvate metabolic process • protein phosphorylation • protein phosphorylation • 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	5165	236900
Ensembl	ENSG00000067992	ENSMUSG00000035232
UniProt	Q15120	Q3V250
RefSeq (mRNA)	NM_001142386.2	NM_145630.2
RefSeq (protein)	NP_001135858.1	NP_663605.1
Location (UCSC)	Chr X: 24.48 – 24.56 Mb	Chr X: 91.01 – 91.08 Mb
PubMed search	[1]	[2]

[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial is an enzyme that in humans is encoded by the PDK3 gene.^[1][2] It codes for an isozyme of pyruvate dehydrogenase kinase.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.^[3]

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Citric_acid_cycle edit

References

1. ^ Gudi R, Bowker-Kinley MM, Kedishvili NY, Zhao Y, Popov KM (Jan 1996). "Diversity of the pyruvate dehydrogenase kinase gene family in humans". J Biol Chem 270 (48): 28989–94. doi:10.1074/jbc.270.48.28989. PMID 7499431. 
2. ^ "Entrez Gene: PDK3 pyruvate dehydrogenase kinase, isozyme 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5165. 
3. ^ The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78". http://www.wikipathways.org/index.php/Pathway:WP78. 

Further reading

• Sugden MC, Holness MJ (2003). "Therapeutic potential of the mammalian pyruvate dehydrogenase kinases in the prevention of hyperglycaemia". Curr. Drug Targets Immune Endocr. Metabol. Disord. 2 (2): 151–65. doi:10.2174/1568008023340785. PMID 12476789. 
• 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 2008-10-14). PMID 12676647. 
• Baker JC, Yan X, Peng T, et al. (2000). "Marked differences between two isoforms of human pyruvate dehydrogenase kinase". J. Biol. Chem. 275 (21): 15773–81. doi:10.1074/jbc.M909488199. PMID 10748134. 
• 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. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Spriet LL, Tunstall RJ, Watt MJ, et al. (2005). "Pyruvate dehydrogenase activation and kinase expression in human skeletal muscle during fasting". J. Appl. Physiol. 96 (6): 2082–7. doi:10.1152/japplphysiol.01318.2003. PMID 14966024. 
• Blackshaw S, Harpavat S, Trimarchi J, et al. (2006). "Genomic Analysis of Mouse Retinal Development". PLoS Biol. 2 (9): E247. doi:10.1371/journal.pbio.0020247. PMC 439783. PMID 15226823. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=439783. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Kato M, Chuang JL, Tso SC, et al. (2005). "Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex". EMBO J. 24 (10): 1763–74. doi:10.1038/sj.emboj.7600663. PMC 1142596. PMID 15861126. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1142596. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Tso SC, Kato M, Chuang JL, Chuang DT (2006). "Structural determinants for cross-talk between pyruvate dehydrogenase kinase 3 and lipoyl domain 2 of the human pyruvate dehydrogenase complex". J. Biol. Chem. 281 (37): 27197–204. doi:10.1074/jbc.M604339200. PMID 16849321. 
• Devedjiev Y, Steussy CN, Vassylyev DG (2007). "Crystal Structure of an Asymmetric Complex of Pyruvate Dehydrogenase Kinase 3 with Lipoyl Domain 2 and its Biological Implications". J. Mol. Biol. 370 (3): 407–16. doi:10.1016/j.jmb.2007.04.083. PMC 1994203. PMID 17532006. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1994203. 
• Degenhardt T, Saramäki A, Malinen M, et al. (2007). "Three members of the human pyruvate dehydrogenase kinase gene family are direct targets of the peroxisome proliferator-activated receptor beta/delta". J. Mol. Biol. 372 (2): 341–55. doi:10.1016/j.jmb.2007.06.091. PMID 17669420. 
• Kato M, Li J, Chuang JL, Chuang DT (2007). "Distinct Structural Mechanisms for Inhibition of Pyruvate Dehydrogenase Kinase Isoforms by AZD7545, Dichloroacetate, and Radicicol". Structure 15 (8): 992–1004. doi:10.1016/j.str.2007.07.001. PMC 2871385. PMID 17683942. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2871385.