Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase

Journal of Biological Chemistry

Volumn 272, Issue 40, 1997, Pages 25105-25111

  Turnbull, Andrew P ^a   Baker, Patrick J ^a   Rice, David W ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

LEUCINE DEHYDROGENASE; OXIDOREDUCTASE; VALINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS SPHAERICUS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SEQUENCE ANALYSIS; STREPTOMYCES CINNAMONEUS; STREPTOMYCES COELICOLOR;

AMINO ACID OXIDOREDUCTASES; AMINO ACID SEQUENCE; BACILLUS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; LEUCINE DEHYDROGENASE; MACROMOLECULAR SUBSTANCES; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOMYCES; SUBSTRATE SPECIFICITY;

BACILLUS SPHAERICUS; STREPTOMYCES CINNAMONENSIS; STREPTOMYCES CINNAMONEUS; STREPTOMYCES COELICOLOR;

EID: 0030808441     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.40.25105     Document Type: Article

References (39)

1. Britton, K. L., Baker, P. J., Engel, P. C., Rice, D. W., and Stillman, T. J. (1993) J. Mol. Biol. 234, 938-945
2. Teller, J. K, Smith, R. J., McPherson, M. J., Engel, P. C., and Guest, J. R. (1992) Eur. J. Biochem. 286, 151-159
3. Nagata, S., Tanizawa, K., Esaki, N., Sakamoto, Y., Ohshima, T., Tanaka, H., and Soda, K. (1988) Biochemistry 27, 9056-9062
4. Leiser, A., Birch, A., and Robinson, J. A. (1996) Gene (Amst.) 177, 217-222
5. Takada, H., Yoshimura, T., Ohshima, T., Esaki, N., and Soda, K. (1991) J. Biochem. (Tokyo) 109, 371-376
6. Hanson, R. L., Singh, J., Kissick, T. P., Patel, R. N., Szarka, L. J., Mueller, R. H. (1990) Bioorg. Chem. 18, 116-130
7. Patchett, A. A., Harris, E., Tristram, E. W., Wyvratt, M. J., Wu, M. T., Taub, D., Peterson, E. R., Ikeler, T. J., Broeke, J., Payne, L. G., Ondeyka, D. L., Thorsett, E. D., Greenlee, W. J., Lohr, N. S., Hoffsommer, R. D., Johshua, H., Ruyle, W. V., Rothrock, J. W., Aster, S. D., Maylock, A. L., Robinson, F. M., Hirschmann, R., and Sweet, C. S., Ulm, E. H., Gross, D. M., Vassil, T. C., and Stone, C. A. (1980) Nature 288, 280-283
8. Dooley, K. C. (1992) Clin. Biochem. 25, 271-275
9. Livesey, G., and Lund, P. (1988) Methods Enzymol. 166, 3-10
10. Yamaguchi, A., Mizushima, Y., Fukushi, M., Shimizu, Y., Kikuchi, Y., and Takasugi. N. (1992) Screening 1, 49-62
11. Mudd, S. H., Levy, H. L., Skovby, F. (1989) in The Metabolic Basis of Inherited Disease (Sciver, C. R., Beudet, A. L., Sly, W. S., and Valle, D. eds) pp. 693-734, McGraw-Hill, New York
12. Omura, S., Tanaka, Y., Mamada, H., and Masuma, R. (1983) J. Antibiot. 36, 1792-1794
13. Tang, L., and Hutchinson, C. R. (1993) J. Bacteriol. 175, 4176-4185
14. Tang, L., Zhang, Y.-X., and Hutchinson, C. R. (1994) J. Bacteriol. 176, 6107-6119
15. Priestley, N. D., and Robinson, J. A. (1989) Biochem. J. 261, 853-861
16. Navarrete, R. M., Vara, J. A., and Hutchinson, C. R. (1990) J. Gen. Microbiol. 136, 273-281
17. Vančurová, I., Vančura, A., Volc, J., Neužil, J., Flieger, M., Basařová, G., and Bêhal, V. (1988) J. Bacteriol. 170, 5192-5196
18. Vančura, A., Vančurová, I., Volc, J., Fussey, S. P. M., Flieger, M., Neužil, J., Maršálec, J., and Bêhal, V. (1988) J. Gen. Microbiol. 134, 3213-3219
19. Ohshima, T., and Soda, K. (1993) Biochim. Biophys. Acta 1162, 221-226
20. Misono, H., Sugihara, K., Kuwamoto, Y., Nagata, S., and Nagasaki, S. (1990) Agric. Biol. Chem. 54, 1491-1498
21. Ohshima, T., Misono, H., and Soda, K. (1978) J. Biol. Chem. 253, 5719-5725
22. Ohshima, T., Nishida, N., Bakthavatsalam, S., Kataoka, K., Takada, H., Yoshimura, T., Esaki, N., and Soda, K. (1994) Eur. J. Biochem. 222, 305-312
23. Nagata, S., Bakthavatsalam, S., Galkin, A. G., Asada, H., Sakai, S., Esaki, N., Soda, K., Ohshima, T., Nagasaki, S., and Misono, H. (1995) Appl. Microbiol. Biotechnol. 44, 432-438
24. Schütte, H., Hummel, W., Tsai, H., and Kula, M.-R. (1985) Appl. Microbiol. Biotechnol. 22, 306-317
25. Britton, K. L., Baker, P. J., Rice, D. W., and Stillman, T. J. (1992) Eur. J. Biochem. 209, 851-859
26. Baker, P. J., Britton, K. L., Engel, P. C., Farrants, G. W., Lilley, K. S., Rice, D. W., and Stillman, T. J. (1992) Proteins Struct. Funct. Genet. 12, 75-86
27. Stillman, T. J., Baker, P. J., Britton, K. L., and Rice, D. W. (1993) J. Mol. Biol. 234, 1131-1139
28. Baker, P. J., Turnbull, A. P., Sedelnikova, S. E., Stillman, T. J., and Rice, D. W. (1995) Structure 3, 693-705
29. Turnbull, A. P., Ashford, S. R., Baker, P. J., Rice, D. W., Rodgers, F. H., Stillman, T. J., and Hanson, R. L. (1994) J. Mol. Biol. 236, 663-665
30. Lee, B., and Richards, F. M. (1971) J. Mol. Biol. 55, 379-400
31. Rife, J. E., and Cleland, W. W. (1980) Biochemistry 19, 2328-2333
32. Fisher, H. F., Maniscalco, S., Singh, N., Mehrotra, R. N., and Srinivasan, R. (1992) Biochim. Biophys. Acta 1119, 52-56
33. Rossmann, M. G., Moras, D., and Olsen, K. W. (1974) Nature 250, 194-199
34. Wierenga, R. K., De Maeyer, M. C. H., and Hol, W. G. L. (1985) Biochemistry 24, 1346-1357
35. Staden, R. (1982) Nucleic Acids Res. 10, 2951-2961
36. Schwartz, R. M., and Dayhoff, M. O. (1978) in Atlas of Protein Sequence and Structure (Dayhoff, M. O., ed) pp. 353-358, National Biomedical Research Foundation, Washington, D.C.
37. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
38. Ferrin, T. E., Huang, C. C., Jarvis, L. E., and Langridge, R. (1988) J. Mol. Graphics 6, 13-27
39. Huang, C. C., Pettersen, E. F., Klein, T. E., Ferrin, T. E., and Langridge, R. (1991) J. Mol. Graphics 9, 230-236