An Essential Role of Glu-243 and His-239 in the Phosphotransfer Reaction Catalyzed by Pyruvate Dehydrogenase Kinase

Journal of Biological Chemistry

Volumn 276, Issue 21, 2001, Pages 17994-17999

  Tuganova, Alina ^a,b   Yoder, Marilyn D ^a   Popov, Kirill M ^a  

^a UNIVERSITY OF MISSOURI KANSAS CITY   (United States)

^b PALLADIN INSTITUTE OF BIOCHEMISTRY   (Ukraine)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CHEMICAL ACTIVATION; ENZYME KINETICS; HYDROLYSIS; MUTAGENESIS;

PHOSPHORYLATION;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATE; ALANINE; ASPARTIC ACID; GLUTAMIC ACID; GLYCINE; HISTIDINE; HYDROXYL GROUP; NUCLEOTIDE; PHOSPHATE; PHOSPHOTRANSFERASE; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE KINASE; UNCLASSIFIED DRUG; (PYRUVATE DEHYDROGENASE (LIPOAMIDE))KINASE; GLUTAMINE; PROTEIN KINASE; RECOMBINANT PROTEIN;

ARTICLE; BINDING AFFINITY; CATALYSIS; CATALYST; COMPLEX FORMATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; GENE MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN HYDROLYSIS; PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; TITRIMETRY; ENZYME ACTIVATION; ESCHERICHIA COLI; GENETICS; HUMAN; METABOLISM; POINT MUTATION; STRUCTURE ACTIVITY RELATION;

CATALYSIS; ENZYME ACTIVATION; ESCHERICHIA COLI; GLUTAMINE; HISTIDINE; HUMANS; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN KINASES; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0242407760     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M009327200     Document Type: Article

References (36)

1. Randle, P. J. (1995) Proc. Nutr. Soc. 54, 317-327
2. Linn, T. C., Pettit, F. H., and Reed, L. J. (1968) Biochemistry 62, 234-241
3. Stepp, L. R., Pettit, F. H., Yeaman, S. J., and Reed, L. J. (1983) J. Biol. Chem. 258, 9454-9458
4. Teague, W. M., Pettit, F. H., Wu, T.-L., Silberman, S. R., and Reed, L. J. (1982) Biochemistry 21, 5585-5592
5. Popov, K. M., Kedishvili, N. Y., Zhao, Y., Gudi, R., and Harris, R. A. (1994) J. Biol. Chem. 269, 29720-29724
6. Huang, B., Gudi, R., Wu, P., Harris, R. A., Hamilton, J., and Popov, K. M. (1998) J. Biol. Chem. 273, 17680-17688
7. Bowker-Kinley, M. M., Davis, W. I., Wu, P., Harris, R. A., and Popov, K. M. (1998) Biochem. J. 329, 191-196
8. Sale, G. J., and Randle, P. J. (1982) Biochem. J. 203, 99-108
9. Popov, K. M., Zhao, Y., Shimomura, Y., Kuntz, M. J., and Harris, R. A. (1992) J. Biol. Chem. 267, 13127-13130
10. Robinson, V. L., Buckler, D. R., and Stock, A. M. (2000) Nat. Struct. Biol. 7, 626-633
11. Popov, K. M., Kedishvili, N. Y., Zhao, Y., Shimomura, Y., Crabb, D. W., and Harris, R. A. (1993) J. Biol. Chem. 268, 26602-26606
12. Bilwes, A. M., Alex, L. A., Crane, B. R., and Simon, M. I. (1999) Cell 96, 131-141
13. Tanaka, T., Saha, S. K., Tomomori, C., Ishima, R., Liu, D., Tong, K. I., Park, H., Dutta, R., Qin, L., Swindells, M. B., Yamazaki, T., Ono, A. M., Kainosho, M., Inouye, M., and Ikura, M. (1998) Nature 396, 88-92
14. Bowker-Kinley, M., and Popov, K. M. (1999) Biochem. J. 344, 47-53
15. Thelen, J. J., Miernyk, J. A., and Randall, D. D. (2000) Biochem. J. 349, 195-201
16. Davie, J. R., Wynn, R. M., Meng, M., Huang, Y. S., Aalund, G., Chuang, D. T., and Lau, K. S. (1995) J. Biol. Chem. 270, 19861-19867
17. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 488-492
18. Lewis, R. J., Singh, O. M. P., Smith, C. V., Skarzynski, T., Maxell, A., Wonacott, A. J., and Wigley, D. B. (1996) EMBO J. 15, 1412-1420
19. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U. S. A. 74, 5463-5467
20. Harris, R. A., Bowker-Kinley, M. M., Wu, P., Jeng, J., Popov, K. M. (1997) J. Biol. Chem. 272, 19746-19751
21. Jeng, J., Kallarakal, A. T., Kim, S. F., Popov, K. M., and Song, B. J. (1998) Comp. Biochem. Physiol. B Biochem. Mol. Biol. 120, 205-216
22. Wu, P., Sato, J., Zhao, Y., Jaskiewicz, J., Popov, K. M., and Harris, R. A. (1998) Biochem. J. 329, 197-201
23. Pratt, M. L., and Roche, T. E. (1979) J. Biol. Chem. 254, 7191-7196
24. Singh, U. S., and Cerione, R. A. (1996) J. Biol. Chem. 271, 27292-27298
25. Laemmli, U. K. (1970) Nature 227, 680-685
26. Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
27. Patel, M. S., and Roche, T. E. (1990) FASEB J. 4, 3224-3233
28. Popov, K. M. (1997) FEBS Lett. 419, 197-200
29. Najafi, S. M. A., Willis, A. C., and Yudkin, M. D. (1995) J. Bacteriol. 177, 2912-2913
30. Liu, S., Baker, J. C., and Roche, T. E. (1995) J. Biol. Chem. 270, 793-800
31. Knowles, J. R. (1980) Annu. Rev. Biochem. 49, 877-919
32. Moll, G. W., Jr., and Kaiser, E. T. (1976) J. Biol. Chem. 251, 3993-4000
33. Paudel, H. K., and Carlson, G. M. (1991) J. Biol. Chem. 266, 16524-16529
34. Panaretou, B., Prodromou, C., Roe, M. S., O'Brien, R., Ladbury, J. E., Piper, P. W., and Pearl, L. H. (1998) EMBO J. 17, 4829-4836
35. Obermann, W. M. J., Sondermann, H., Russo, A. A., Pavletich, N. P., and Hartl, F. U. (1998) J. Cell Biol. 143, 901-910
36. Roe, S. M., Prodromou, C., O'Bien, R., Ladbury, J. E., Piper, P. W., and Pearl, L. H. (1999) J. Med. Chem. 42, 260-266