Delineation of xenobiotic substrate sites in rat glutathione S-transferase M1-1

Protein Science

Volumn 14, Issue 10, 2005, Pages 2526-2536

  Hearne, Jennifer L ^a   Colman, Roberta F ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

Glutathione S transferase M1 1; Monobromobimane; Site directed mutagenesis; Substrate site

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; ALANINE; BROMOBIMANE; GLUTATHIONE TRANSFERASE M1; TYROSINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CATALYSIS; COMPETITIVE INHIBITION; CONTROLLED STUDY; ENZYME BINDING; ENZYME KINETICS; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME SUBSTRATE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; RAT; RECEPTOR AFFINITY; SITE DIRECTED MUTAGENESIS; XENOBIOTIC METABOLISM;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; GLUTATHIONE TRANSFERASE; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RATS; SUBSTRATE SPECIFICITY; XENOBIOTICS;

EID: 25844449746     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051651905     Document Type: Article

References (43)

1. Adang, A.E.P., Brussee, J., Gen, A.V.D., and Mulder, G.J. 1990. The glutathione-binding site in glutathione S-transferases. Biochem. J. 269: 47-54.
2. Armstrong, R.N. 1991. Glutathione S-transferases: Reaction mechanism, structure, and function. Chem. Res. Toxicol. 4: 131-140.
3. _. 1998. Mechanistic imperative for the evolution of glutathione transferases. Curr. Opin. Chem. Biol. 2: 618-623.
4. Barycki, J.J. and Colman, R.F. 1993. Affinity labeling of glutathione Stransferase, isozyme 4-4, by 4-(fluorosulfonyl)benzoic acid reveals Tyr 115 to be an important determinant of xenobiotic substrate specificity. Biochemistry 32: 13002-13011.
5. Bhargava, M.M., Listowsky, I., and Arias, I.M. 1978. Studies on subunit structure and evidence that ligandin is a heterodimer. J. Biol. Chem. 253: 4116-4119.
6. Board, P.G., Baker, R.T., Chelvanayagam, G., and Jermiin, L.S. 1997. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 328: 929-935.
7. Board, P.G., Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L.S., Schulte, G.K., Danley, D.E., Hoth, L.R., Griffor, M.C., Kamath, A.V., et al. 2000. Identification, characterization, and crystal structure of the v class glutathione transferases. J. Biol. Chem. 275: 24798-24806.
8. Boyer, T.D. 1989. The glutathione S-transferases: An update. Hepatology 9: 486-496.
9. Coles, B. and Ketterer, B. 1990. The role of glutathione and glutathione transferases in chemical carcinogenesis. Crit. Rev. Biochem. Mol. Biol. 25: 47-70.
10. Combet, C., Blanchet, C., Geourjon, C., and Deleage, G. 2000. NPS@: Network Protein Sequence analysis (CLUSTALW multiple alignment). TIBS 291: 147-150.
11. Eaton, D.L. and Bammler, T.K. 1999. Concise review of the glutathione Stransferases and their significance in toxicology. Toxicol. Sci. 49: 156-164.
12. Habig, W.H., Pabst, M.J., and Jakoby, W.B. 1974. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249: 7130-7139.
13. Hearne, J.L. and Colman, R.F. 2004. Delineation of xenobiotic substrate site in glutathione S-transferase M1-1 (GST M1-1) by mutagenesis. In Abstracts of Papers, 228th ACS National Meeting, Philadelphia, PA, USA, August 22-26, p. BIOL-095.
14. Hu, L. and Colman, R.F. 1995. Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase 3-3. J. Biol. Chem. 270: 21875-21883.
15. Hu, L., Borleske, B.L., and Colman, R.F. 1997. Probing the active site of α-class rat liver glutatione S-transferases using affinity labeling by monobromobimane. Protein Sci. 6: 43-52.
16. Hulbert, P.B. and Yakubu, S.I. 1983. Monobromobimane: A substrate for the fluorimetric assay of glutathione transferase. J. Pharm. Pharmacol. 35: 384-386.
17. Jakoby, W.B. and Habig, W.H. 1980. Enzymatic basis of detoxification (ed. W.B. Jakoby), pp. 63-94. Academic Press, New York.
18. Ji, X., Zhang, P., Armstrong, R.N., and Gilliland, G.L. 1992. The three-dimensional structure of a glutathione S-transferase from the μ gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-Å resolution. Biochemistry 31: 10169-10184.
19. Ji, X., Armstrong, R.N., and Gilliland, G.L. 1993. Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase. Biochemistry 32: 12949-12954.
20. Johnson, W.W., Liu, S., Ji, X., Gilliland, G.L., and Armstrong, R.N. 1993. Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase. J. Biol. Chem. 268: 11508-11511.
21. Kretsinger, J.K. and Schneider, J.P. 2003. Design and application of basic amino acids displaying enhanced hydrophobicity. J. Am. Chem. Soc. 125: 7907-7913.
22. Liu, L.F., Hong, J.L., Tsai, S.P., Hsieh, J.C., and Tam, M.F. 1993. Reversible modification of rat liver glutathione S-transferase 3-3 with 1-chloro-2, 4-dinitrobenzene: Specific labeling of Tyr-115. Biochem. J. 296: 189-197.
23. Mannervik, B. and Danielson, U.H. 1988. Glutathione transferases- structure and catalytic activity. CRC Crit. Rev. Biochem. 23: 283-337.
24. Mannervik, B., Alin, P., Guthenberg, C., Jensson, H., Tahir M.K., Warholm, M., and Jornvall, H. 1985. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. 82: 7202-7206.
25. Meyer, D.J., Coles, B., Pemble, S.E., Gilmore, K.S., Fraser, G.M., and Ketterer, B. 1991. Theta, a new class of glutathione transferases purified from rat and man. Biochem. J. 274: 409-414.
26. Pemble, S.E., Wardle, A.F., and Taylor, J.B. 1996. Glutathione S-transferase class κ: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem. J. 319: 749-754.
27. Pettigrew, N.E. and Colman, R.F. 2001. Heterodimers of glutathione Stransferase can form between isoenzyme classes π and μ. Arch. Biochem. Biophys. 396: 225-230.
28. Pettigrew, N.E., Brush, E.J., and Colman, R.F. 2001. 3-Methyleneoxindole: An affinity label of glutathione S-transferase π which targets tryptophan 38. Biochemistry 40: 7549-7558.
29. Pickett, C.B. and Lu, A.Y. 1989. Glutathione S-transferases: Gene structure, regulation, and biological function. Annu. Rev. Biochem. 58: 743-764.
30. Ploemen, J.H.T.M., Johnson, W.W., Jespersen, S., Vanderwall, D., van Ommen, B., van der Greef, J., van Bladeren, P.J., and Armstrong, R.A. 1994. Active-site tyrosyl residues are targets in the irreversible inhibition of a class μ glutathione transferase by 2-(S-glutathionyl)- 3, 5, 6,-trichloro-1, 4-benzoquinone. J. Biol. Chem. 269: 26890-26897.
31. Ralat, L.A. and Colman, R.F. 2003. Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase π. Protein Sci. 12: 2575-2587.
32. _. 2004. Glutathione S-transferase π has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site. J. Biol. Chem. 279: 50204-50213.
33. Rossjohn, J., Polekhina, G., Feil, S.C., Allocati, N., Masulli, M., De Illio, C., and Parker, M.W. 1998. A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications. Structure 6: 721-734.
34. Sambrook, J., Fritsch, E.F., and Maniatis, T. 1989. Molecular cloning: A laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
35. Schneider, J.P., Lear, J.D., and DeGrado, W.F. 1997. A designed buried salt bridge in a heterodimeric coiled coil. J. Am. Chem. Soc. 119: 5742-5743.
36. Shan, S. and Armstrong, R.N. 1994. Rational reconstruction of the active site of a class μ GST. J. Biol. Chem. 269: 32373-32379.
37. Sheenan, D., Meade, G., Foley, V.M., and Dowd, C.A. 2001. Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian member of an ancient enzyme superfamily. Biochem. J. 360: 1-16.
38. 4 biosynthesis. Adv. Prostaglandin Thromboxane Leukot Res. 19: 21-25.
39. Vander Jagt, D.L., Hunsaker, L.A., Garcia, K.B., and Royer, R.E. 1985. Isolation and characterization of the multiple glutathione S-transferases from human liver. Evidence for unique heme-binding sites. J. Biol. Chem. 260: 11603-11610.
40. Vargo, M.A. and Colman, R.F. 2004. Heterodimers of wild-type and subunit interface mutant enzymes of glutathione S-transferase A1-1: Interactive or independent active sites? Protein Sci. 13: 1586-1593.
41. Vargo, M.A., Nguyen, L., and Colman, R.F. 2004. Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium. Biochemistry 43: 3327-3335.
42. Waxman, D.J. 1990. Glutathione S-transferases: Role in alkylating agent resistance and possible target for modulation chemotherapy - A review. Cancer Res. 50: 6449-6454.
43. Wilce, M.C. and Parker, M.W. 1994. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta 1205: 1-18.