Amino acid residues responsible for the recognition of dichloroacetate by pyruvate dehydrogenase kinase 2

FEBS Letters

Volumn 581, Issue 16, 2007, Pages 2988-2992

  Klyuyeva, Alla ^a   Tuganova, Alina ^a   Popov, Kirill M ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

Cancer; Carbohydrate metabolism; Diabetes; Dichloroacetate; Mitochondria; Oxidative decarboxylation of pyruvate; Protein phosphorylation; Pyruvate dehydrogenase kinase

Indexed keywords

AMINO ACID; CHLORMIDAZOLE; DICHLOROACETIC ACID; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE KINASE 2; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; DRUG MECHANISM; ENZYME ACTIVE SITE; ENZYME BINDING; INTROSPECTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; AMINO ACIDS; ANIMALS; BINDING SITES; DICHLOROACETATE; MODELS, MOLECULAR; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN KINASE INHIBITORS; PROTEIN KINASES; RATS;

EID: 34250178104     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.05.052     Document Type: Article

References (16)

1. Holness M.J., and Sugden M.C. Regulation of pyruvate dehydrogenase complex activity by reversible phosphorylation. Biochem. Soc. Trans. 31 (2003) 1143-1151
2. Randle P.J. Metabolic fuel selection: general integration at the whole-body level. Proc. Nutr. Soc. 54 (1995) 317-327
3. Roche T.E., Baker J.C., Yan X., Hiromasa Y., Gong X., Peng T., Dong J., Turkan A., and Kasten S.A. Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms. Prog. Nucleic. Acid. Res. Mol. Biol. 70 (2001) 33-75
4. Bowker-Kinley M.M., Davis W.I., Wu P., Harris R.A., and Popov K.M. Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex. Biochem. J. 329 (1998) 191-196
5. Steussy C.N., Popov K.M., Bowker-Kinley M.M., Sloan Jr. R.B., Harris R.A., and Hamilton J.A. Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase. J. Biol. Chem. 276 (2001) 37443-37450
6. Kato M., Chuang J.L., Tso S.C., Wynn R.M., and Chuang D.T. Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex. EMBO J. 24 (2005) 1763-1774
7. Knoechel T.R., Tucker A.D., Robinson C.M., Phillips C., Taylor W., Bungay P.J., Kasten S.A., Roche T.E., and Brown D.G. Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands. Biochemistry 45 (2006) 402-415
8. Kolobova E., Tuganova A., Boulatnikov I., and Popov K.M. Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites. Biochem. J. 358 (2001) 69-77
9. Harris R.A., Bowker-Kinley M.M., Wu P., Jeng J., and Popov K.M. Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex. J. Biol. Chem. 272 (1997) 19746-19751
10. Tuganova A., Boulatnikov I., and Popov K.M. 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 (2002) 129-136
11. Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74 (1977) 5463-5467
12. Hiromasa Y., Hu L., and Roche T.E. Ligand-induced effects on pyruvate dehydrogenase kinase isoform 2. J. Biol. Chem. 281 (2006) 12568-12579
13. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
14. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R.J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
15. Stacpoole P.W., Moore G.W., and Kornhauser D.M. Metabolic effects of dichloroacetate in patients with diabetes mellitus and hyperlipoproteinemia. N. Engl. J. Med. 298 (1978) 526-530
16. + channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth. Cancer Cell 11 (2007) 37-51