Contribution of the two conserved tryptophan residues to the catalytic and structural properties of Proteus mirabilis glutathione S-transferase B1-1

Biochemical Journal

Volumn 385, Issue 1, 2005, Pages 37-43

  Allocati, Nerino ^a   Masulli, Michele ^a   Pietracupa, Marilena ^a   Favaloro, Bartolo ^a   Federici, Luca ^b   Di Ilio, Carmine ^a  

^a UNIVERSITY OF CHIETI   (Italy)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

2 (p toluidino)naphthalene 6 sulphonic acid (TNS); Bacterial glutathione S transferase (GST); CD spectroscopy; Proteus mirabilis glutathione S transferase B1 1 (PmGSTB1 1); Tryptophan mutant

Indexed keywords

ANTIBIOTICS; BACTERIA; CATALYST ACTIVITY; MONOMERS; MUTAGENESIS; SUBSTITUTION REACTIONS;

BACTERIAL ENZYMES; ENZYME ACTIVE SITES; STRUCTURAL STABILIZATION; TRYPTOPHAN RESIDUES;

ENZYMES;

1 CHLORO 2,4 DINITROBENZENE; 2 (2 TOLUIDINO)NAPHTHALENE 6 SULFONIC ACID; ANTIBIOTIC AGENT; BACTERIAL ENZYME; DNA; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE B1 1; MUTANT PROTEIN; NAPHTHALENE DERIVATIVE; RIFAMYCIN; TETRACYCLINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; CATALYSIS; CIRCULAR DICHROISM; DNA SEQUENCE; DRUG BINDING SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE; FLUORESCENCE SPECTROSCOPY; GENE EXPRESSION; GENETIC TRANSCRIPTION; HYDROPHOBICITY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEUS MIRABILIS; TEMPERATURE SENSITIVITY;

AMINO ACID SUBSTITUTION; ANTI-BACTERIAL AGENTS; CATALYSIS; CONSERVED SEQUENCE; ELECTROSTATICS; ENZYME STABILITY; GLUTATHIONE TRANSFERASE; GUANIDINE; KINETICS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN RENATURATION; PROTEUS MIRABILIS; SPECTRUM ANALYSIS; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; TRYPTOPHAN;

BACTERIA (MICROORGANISMS); MIRABILIS; NEGIBACTERIA; PROTEUS MIRABILIS;

EID: 12744260133     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040890     Document Type: Article

References (32)

1. Hayes, J. D. and Pulford, D. J. (1995) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30, 445-600
2. Hayes, J. D. and McLellan, L. I. (1999) Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radical Res. 31, 273-300
3. Armstrong, R. N. (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10, 2-18
4. Mannervik, B. and Danielson, U. H. (1988) Glutathione transferases: structure and catalytic activity. Crit. Rev. Biochem. Mol. Biol. 23, 283-337
5. Sheehan, D., Meade, G., Foley, V. M. and Dowd, C. A. (2001) Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360,1-16
6. Di Ilio, C., Aceto, A., Piccolomini, R., Allocati, N., Faraone, A., Cellini, L., Ravagnan, G. and Federici, G. (1988) Purification and characterization of three forms of glutathione transferase from Proteus mirabilis. Biochem. J. 255, 971-975
7. Mignogna, G., Allocati, N., Aceto, A., Piccolomini, R., Di Ilio, C., Barra, D. and Martini, F. (1993) The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes. Eur. J. Biochem. 211, 421-425
8. Perito, B., Allocati, N., Casalone, E., Masulli, M., Dragani, B., Polsinelli, M., Aceto, A. and Di Ilio, C. (1996) Molecular cloning and overexpression of a glutathione transferase gene from Proteus mirabilis. Biochem. J. 318, 157-162
9. Casalone, E., Allocati, N., Ceccarelli, I., Masulli, M., Rossjohn, J., Parker, M. W. and Di Ilio, C. (1998) Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site. FEBS Lett. 423, 122-124
10. Rossjohn, J., Polekhina, G., Feil, S. C., Allocati, N., Masulli, M., Di Ilio, C. and Parker, M. W. (1998) A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6, 721-734
11. Allocati, N., Casalone, E., Masulli, M., Ceccarelli, I., Carletti, E., Parker, M. W. and Di Ilio, C. (1999) Functional of the evolutionary conserved proline 53 residue in Proteus mirabilis glutathione transferase B1-1. FEBS Lett. 445, 347-350
12. Allocati, N., Casalone, E., Masulli, M., Polekhina, G., Rossjohn, J., Parker, M. W. and Di Ilio, C. (2000) Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases. Biochem. J. 351, 341-346
13. Allocati, N., Masulli, M., Casalone, E., Santucci, S., Favaloro, B., Parker, M. W. and Di Ilio, C. (2002) Glutamic acid 65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1. Biochem. J. 363, 189-193
14. Caccuri, A. M., Antonini, G., Allocati, N., Di Ilio, C., Innocenti, F., De Maria, F., Parker, M. W., Masulli, M., Polizio, F., Federici, G. et al. (2002) Properties and utility of the peculiar mixed disulfide in the bacterial glutathione transferase B1-1. Biochemistry 41, 4686-4693
15. Caccuri, A. M., Antonini, G., Allocati, N., Di Ilio, C., De Maria, F., Innocenti, F., Parker, M. W., Masulli, M., Lo Bello, M., Turella, P. et al. (2002) GSTB1-1 from Proteus mirabilis: a snapshot of an enzyme in the evolutionary pathway from a redox enzyme to a conjugating enzyme. J. Biol. Chem. 277, 18777-18784
16. Allocati, N., Favaloro, B., Masulli, M., Alexeyev, M. F. and Di Ilio, C. (2003) Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses. Biochem. J. 373, 305-311
17. Piccolomini, R., Di Ilio, C., Aceto, A., Allocati, N., Faraone, A., Cellini, L., Ravagnan, G. and Federici, G. (1989) Glutathione transferase in bacteria: subunit composition and antigenic characterization. J. Gen. Microbiol. 135, 3119-3125
18. Sanger, F., Nicklen, S. and Coulsen, A. R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467
19. Sambrook, J. and Russell, D. W. (2001) Molecular cloning: a laboratory manual, 3rd edn, Cold Spring Harbor Laboratory Press, Plainview, NY
20. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
21. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
22. Habig, W. H. and Jakoby, W. B. (1981) Assay for differentiation of glutathione S-transferases. Methods Enzymol. 77, 398-405
23. Di Ilio, C., Sacchetta, P., Lo Bello, M., Caccuri, A. M. and Federici, G. (1986) Selenium independent glutathione peroxidase activity associated with cationic forms of glutathione transferase in human heart. J. Mol. Cell. Cardiol. 18, 983-991
24. Anhalt, J. P. and Washington, II, J. A. (1991) Preparation and storage of antimicrobial solutions. In Manual of Clinical Microbiology (Balows, A., Hausler, Jr, W. J., Herrmann, K. L., Isenberg, H. D. and Shadomy, H. J., eds.), pp. 1199-1200, American Society for Microbiology, Washington, DC
25. Di Ilio, C., Sacchetta, P., Iannarelli, V. and Aceto, A. (1995) Binding of pesticides to alpha, mu and pi class glutathione transferase. Toxicol. Lett. 76, 173-177
26. Chang, T. C., Wu, C.-S. C. and Yang, J. T. (1978) Circular dichroism analysis of protein conformation: inclusion of the β-turns. Anal. Biochem. 91, 13-31
27. DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA, U.S.A.
28. Sali, A. and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815
29. Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
30. Nicholls, A., Sharp, K. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296
31. m for glutathione in glutathione transferases of the α, μ and π classes. Xenobiotica 23, 823-834
32. Ji, X., von Rosenvinge, E. C., Johnson, W. W., Tomarev, S. I., Piatigorsky, J., Armstrong, R. N. and Gilliland, G. L. (1995) Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry 34, 5317-5328