(S)-Mandelate dehydrogenase from Pseudomonas putida: Mutations of the catalytic base histidine-274 and chemical rescue of activity

Biochemistry

Volumn 38, Issue 31, 1999, Pages 9948-9955

  Lehoux, Isabelle E ^a   Mitra, Bharati ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

(S) 2 HYDROXY ACID OXIDASE; ALANINE; ASPARAGINE; GLYCINE; HISTIDINE; IMIDAZOLE DERIVATIVE; MANDELIC ACID; OXIDOREDUCTASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; MUTATION; NONHUMAN; PKA; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA;

ALANINE; ALCOHOL OXIDOREDUCTASES; ASPARAGINE; BINDING SITES; CATALYSIS; DEUTERIUM; ENZYME INHIBITORS; FLAVIN MONONUCLEOTIDE; GLYCINE; HISTIDINE; HYDROGEN-ION CONCENTRATION; IMIDAZOLES; KINETICS; MANDELIC ACIDS; MUTAGENESIS, SITE-DIRECTED; PSEUDOMONAS PUTIDA; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; SULFITES;

BACTERIA (MICROORGANISMS); MITRA; NEGIBACTERIA; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0033520066     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9907532     Document Type: Article

References (21)

1. Diep Le, K. H., and Lederer, F. (1991) J. Biol. Chem. 266, 20877-20881.
2. Mitra, B., Gerlt, J. A., Babbitt, P. C., Woo, C. W., Kenyon, G. L., Joseph, D., and Petsko, G. A. (1993) Biochemistry 32, 12959-12967.
3. Lindqvist, Y., and Branden, C.-I. (1989) J. Biol. Chem. 264, 3624-3628.
4. Xia, Z., and Mathews, F. S. (1990) J. Mol. Biol. 212, 837-863.
5. Lindqvist, Y., Branden, C.-I., Mathews, F. S. and Lederer, F. (1991) J. Biol. Chem. 266, 3198-3207.
6. Reid, G. A., White, S., Black, M. T., Lederer, F., Mathews, F. S., and Chapman, S. K. (1988) Eur. J. Biochem. 178, 329-333.
7. Mattevi, A., Vanoni, M. A., Todone, F., Rizzi, M., Teplyakov, A., Coda, A., Bolognesi, M., and Curti, B. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 7496-7501.
8. Muh, U., Williams, C. H., and Massey, V. (1994) J. Biol. Chem. 269, 7989-7993.
9. Gaume, B., Sharp, R. E., Manson, F. D. C., Chapman, S. K., Reid, G. A., and Lederer, F. (1995) Biochimie 77, 621-630.
10. Lehoux, I. E., and Mitra, B. (1999) Biochemistry 38, 5836-5848.
11. Toney, M. D., and Kirsch, J. F. (1989) Science 243, 1485-1488.
12. Landro, J. A., Kallarakal, A. T., Ransom, S. C., Gerlt, J. A., Kozarich, J. W., Neidhart, D. J., and Kenyon, G. L. (1991) Biochemistry 30, 9274-9281.
13. Alberty, R. A., and Massey, V. (1954) Biochim. Biophys. Acta 13, 347-353.
14. Segel, I. H. (1975) in Enzyme Kinetics, pp 914-917, John Wiley & Sons, Inc., New York.
15. Tegoni M., and Mathews, F. S. (1988) J. Biol. Chem. 263, 19278-19281.
16. Harpel, M. R., and Hartman, F. C. (1994) Biochemistry 33, 5553-5561.
17. Gondry, M., and Lederer, F. (1996) Biochemistry 35, 8587-8594.
18. Newmyer, S. L., and Ortiz de Montellano, P. R. (1996) J. Biol. Chem. 271, 14891-14896.
19. Newmyer, S. L., Sun, J., Loehr, T. M., and Ortiz de Montellano, P. R. (1996) Biochemistry 35, 12788-12795.
20. Huang, S., and Tu, S.-C. (1997) Biochemistry 36, 14609-14615.
21. Tu, C. K., Silverman, D. N., Forsman, C., Jonsson, B. H., and Lindskog, S. (1989) Biochemistry 28, 7913-7918.