Role of aspartate-133 and histidine-458 in the mechanism of tryptophan indole-lyase from Proteus vulgaris

Biochemistry

Volumn 42, Issue 38, 2003, Pages 11161-11169

  Demidkina, Tatyana V ^a   Zakomirdina, Lyudmila N ^a   Kulikova, Vitalia V ^a   Dementieva, Irene S ^a,b   Faleev, Nicolai G ^b   Ronda, Luca ^c   Mozzarelli, Andrea ^c   Gollnick, Paul D ^d   Phillips, Robert S ^e  

^a ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^b A N NESMEYANOV INSTITUTE OF ORGANOELEMENT COMPOUNDS   (Russian Federation)

^c UNIVERSITY OF PARMA   (Italy)

^d UNIVERSITY AT BUFFALO   (United States)

^e UNIVERSITY OF GEORGIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; CATALYST ACTIVITY; CRYSTALS; ENZYME INHIBITION; HYDROGEN BONDS; HYDROLYSIS; MUTAGENESIS; RATE CONSTANTS;

ELIMINATION REACTIONS;

ENZYME KINETICS;

3 CHLOROALANINE; ALANINE; ALPHA AMINOACRYLATE; AMMONIUM PYRUVATE; ASPARTIC ACID; BACTERIAL ENZYME; BETA PHENYLSERINE; CYSTEINE; HISTIDINE; INDOLE; LYASE; METHIONINE; OXINDOLYLALANINE; PHENYLALANINE; PYRIDOXAL 5 PHOSPHATE; QUINONE DERIVATIVE; S (O NITROPHENYL)CYSTEINE; TRYPTASE; TRYPTOPHAN; TRYPTOPHAN INDOLE LYASE; TRYPTOPHANASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; HYDROGEN BOND; HYDROLYSIS; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEUS VULGARIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO ACIDS; ASPARTIC ACID; BINDING SITES; BINDING, COMPETITIVE; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEUS VULGARIS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY; TRYPTOPHANASE;

BACTERIA (MICROORGANISMS); FELIS CATUS; PROTEUS VULGARIS;

EID: 0141791274     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034348t     Document Type: Article

References (28)

1. Morino, Y., and Snell, E. E. (1967) J. Biol. Chem. 242, 2800.
2. Kamath, A. V., and Yanofsky, C. (1992) J. Biol. Chem. 267, 19978.
3. Martin, K., Morlin, G., Smith, A., Nordyke, A., Eisenstark, A., and Golomb, M. (1998) J. Bacteriol. 180, 107.
4. Heidelberg, J. F., Eisen, J. A., Nelson, W. C., Clayton, R. A., Gwinn, M. L., Dodson, R. J., Haft, D. H., Hickey, E. K., Peterson, J. D., Umayam, L., Gill, S. R., Nelson, K. E., Read, T. D., Tettelin, H., Richardson, D., Ermolaeva, M. D., Vamathevan, J., Bass, S., Qin, H., Dragoi, I., Sellers, P., McDonald, L., Utterback, T., Fleishmann, R. D., Nierman, W. C., and White, O. (2000) Nature 406, 477.
5. Di Martino, P., Merieau, A., Phillips, R., Orange, N. and Hulen, C. (2002) Can. J. Microbiol. 48, 132-137.
6. Suelter, C. H., Wang, J., and Snell, E. E. (1976) FEBS Lett. 66, 230.
7. Watanabe, T., and Snell, E. E. (1977) J. Biochem. (Tokyo) 82, 733.
8. Phillips, R. S. (1987) Arch. Biochem. Biophys. 256, 302.
9. Phillips, R. S., Miles, E. W., and Cohen, L. A. (1984) Biochem. 23, 6228.
10. Kiick, D. M., and Phillips, R. S. (1988) Biochem. 27, 7333.
11. Phillips, R. S. (1989) J. Am. Chem. Soc. 113, 727.
12. Phillips, R. S. (1991) Biochemistry 30, 5927.
13. Phillips, R. S., Sundararaju, B., and Faleev, N. G. (2000) J. Am. Chem. Soc. 122, 1008-14.
14. Isupov, M. N., Antson, A. A., Dodson, E. J., Dodson, G. G., Dementieva, I. S., Zakomirdina, L. N., Wilson, K. S., Dauter, Z., Lebedev, A. A., and Harutyunyan, E. H. (1998) J. Mol. Biol. 276, 603.
15. Phillips, R. S., Johnson, N. and Kamath, A. V., (2002) Biochemistry 41, 4012-9.
16. Alexander, F. W., Sandmeier, E., Mehta, P. K., and Christen, P., (1994) Eur. J. Biochem. 219, 953-60
17. Sundararaju, B., Antson, A. A., Phillips, R. S., Demidkina, T. V., Barbolina, M. V., Gollnick, P., Dodson, G. G., and Wilson, K. S. (1997) Biochemistry 36, 6502.
18. Demidkina, T. V., Barbolina, M. V., Faleev, N. G., Sundararaju, B., Gollnick, P. D., and Phillips, R. S. (2002) Biochem. J. 363, 745-752.
19. Dua, R. K., Taylor, E. W., and Phillips, R. S. (1993) J. Am. Chem. Soc. 115, 1264.
20. Zakomirdina, L. N., Kulikova, V. V., Gogoleva, O. I., Dementieva, I. S., Faleev, N. G., and Demidkina, T. V. (2002) Biochemistry (Moscow) 67, 1189.
21. Vieira, J., and Messing, J. (1987) Methods Enzymol. 153, 1.
22. Morino, Y., and Snell, E. E. (1970) Methods Enzymol. 17A, 439.
23. Cleland, W. W. (1979) Methods Enzymol. 63, 103.
24. Matheson, I. B. C. (1990) Comput. Chem. 14, 49.
25. Strickland, S., Palmer, G., and Massey, V. (1975) J. Biol. Chem. 250, 4048.
26. Phillips, R. S., Demidkina, T. V., Zakomirdina, L. N., Bruno, S., Ronda, L. and Mozzarelli, A. (2002) J. Biol. Chem. 277, 21592.
27. Mozzarelli, A., and Rossi, G. L. (1996) Annu. Rev. Biophys. Biomol. Struct. 25, 343.
28. DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA. http://www.pymol.org.