PDK2
From Wikipedia, the free encyclopedia
Pyruvate dehydrogenase kinase, isozyme 2
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PDB rendering based on 1jm6. | ||||||||||||||
Available structures: 1jm6, 2btz, 2bu2, 2bu5, 2bu6, 2bu7, 2bu8 | ||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | PDK2; | |||||||||||||
External IDs | OMIM: 602525 MGI: 1343087 HomoloGene: 68265 | |||||||||||||
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RNA expression pattern | ||||||||||||||
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) |
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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: . 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: . 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: . 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: . 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: . 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: . 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: . 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: . 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: . 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: . 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: . 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: . 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: . PMID 15955060.