PDK2

From Wikipedia, the free encyclopedia


Pyruvate dehydrogenase kinase, isozyme 2
PDB rendering based on 1jm6.
Available structures: 1jm6, 2btz, 2bu2, 2bu5, 2bu6, 2bu7, 2bu8
Identifiers
Symbol(s) PDK2;
External IDs OMIM: 602525 MGI1343087 HomoloGene68265
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 5164 18604
Ensembl ENSG00000005882 ENSMUSG00000038967
Uniprot Q15119 Q8VC63
Refseq NM_002611 (mRNA)
NP_002602 (protein)
XM_975730 (mRNA)
XP_980824 (protein)
Location Chr 17: 45.53 - 45.54 Mb Chr 11: 94.84 - 94.86 Mb
Pubmed search [1] [2]

Pyruvate dehydrogenase kinase, isozyme 2, also known as PDK2, is a human gene.[1] It codes for an isozyme of pyruvate dehydrogenase kinase.


[edit] References

[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. 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. 
  • Kobayashi T, Cohen P (1999). "Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2.". Biochem. J. 339 ( Pt 2): 319–28. PMID 10191262. 
  • Gold MR, Scheid MP, Santos L, et al. (1999). "The B cell antigen receptor activates the Akt (protein kinase B)/glycogen synthase kinase-3 signaling pathway via phosphatidylinositol 3-kinase.". J. Immunol. 163 (4): 1894–905. PMID 10438924. 
  • 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. 
  • Steussy CN, Popov KM, Bowker-Kinley MM, et al. (2001). "Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase.". J. Biol. Chem. 276 (40): 37443–50. doi:10.1074/jbc.M104285200. PMID 11483605. 
  • 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. 
  • Peters SJ, Harris RA, Wu P, et al. (2002). "Human skeletal muscle PDH kinase activity and isoform expression during a 3-day high-fat/low-carbohydrate diet.". Am. J. Physiol. Endocrinol. Metab. 281 (6): E1151–8. PMID 11701428. 
  • 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. 
  • Boulatnikov I, Popov KM (2003). "Formation of functional heterodimers by isozymes 1 and 2 of pyruvate dehydrogenase kinase.". Biochim. Biophys. Acta 1645 (2): 183–92. PMID 12573248. 
  • Hiromasa Y, Roche TE (2003). "Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase.". J. Biol. Chem. 278 (36): 33681–93. doi:10.1074/jbc.M212733200. PMID 12816949. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Watt MJ, Heigenhauser GJ, LeBlanc PJ, et al. (2005). "Rapid upregulation of pyruvate dehydrogenase kinase activity in human skeletal muscle during prolonged exercise.". J. Appl. Physiol. 97 (4): 1261–7. doi:10.1152/japplphysiol.00132.2004. PMID 15169745. 
  • 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. 
  • Bao H, Kasten SA, Yan X, Roche TE (2004). "Pyruvate dehydrogenase kinase isoform 2 activity limited and further inhibited by slowing down the rate of dissociation of ADP.". Biochemistry 43 (42): 13432–41. doi:10.1021/bi049488x. PMID 15491150. 
  • Bao H, Kasten SA, Yan X, et al. (2004). "Pyruvate dehydrogenase kinase isoform 2 activity stimulated by speeding up the rate of dissociation of ADP.". Biochemistry 43 (42): 13442–51. doi:10.1021/bi0494875. PMID 15491151. 
  • Abbot EL, McCormack JG, Reynet C, et al. (2005). "Diverging regulation of pyruvate dehydrogenase kinase isoform gene expression in cultured human muscle cells.". FEBS J. 272 (12): 3004–14. doi:10.1111/j.1742-4658.2005.04713.x. PMID 15955060.