PDK3

From Wikipedia, the free encyclopedia

Pyruvate dehydrogenase kinase, isozyme 3

PDB rendering based on 1y8n.

Available structures: 1y8n, 1y8o, 1y8p

Identifiers

Symbol(s)

PDK3;

External IDs

OMIM: 602526 MGI: 2384308 HomoloGene: 55897

Gene ontology
Molecular Function:	• protein histidine kinase activity • [pyruvate dehydrogenase (lipoamide) kinase activity] • ATP binding
Cellular Component:	• mitochondrion
Biological Process:	• carbohydrate metabolic process • glucose metabolic process • phosphorylation • peptidyl-histidine phosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005391 (mRNA)
NP_005382 (protein)

NM_145630 (mRNA)
NP_663605 (protein)

Location

Chr X: 24.39 - 24.46 Mb

Chr X: 90.02 - 90.08 Mb

Pubmed search

[1]

[2]

Pyruvate dehydrogenase kinase, isozyme 3, also known as PDK3, is a human gene.^[1] It codes for an isozyme of pyruvate dehydrogenase kinase.

[edit] References

^ Entrez Gene: PDK3 pyruvate dehydrogenase kinase, isozyme 3.

[edit] 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. 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. 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.
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. 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. 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.
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. PMID 12477932.
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. PMID 15226823.
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. PMID 15489334.
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. PMID 15861126.
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. PMID 17532006.
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. PMID 17683942.