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Xenobiotica
the fate of foreign compounds in biological systems
Volume 26, 1996 - Issue 2
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Research Article

Enzyme kinetics and substrate selectivities of rat glutathione S-transferase isoenzymes towards a series of new 2-substituted 1-chloro-4-nitrobenzenes

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Pages 143-155 | Received 05 Aug 1995, Published online: 22 Sep 2008

References

  • Adang A. E. P., Moree W. J., Brusee J., Mulder G. J., Van der Gen A. Inhibition of glutathione S-transferase 3–3 by glutathione derivatives that bind covalently to the active site. Bichemical Journal 1991; 278: 63–68
  • Armstrong R. N. Glutathione S-transferases: reaction mechanism, structure, and function. Chemical Research in Toxicology 1991; 4: 131–140
  • Asaoka K., Takahashi K. Inactivation of bovine liver glutathione S-transferase by specific modification of arginine residues with phenyl glyoxal. Journal of Enzyme Inhibition 1989; 3: 77–80
  • Benson A. M., Talalay P., Keen J. H., Jakoby W. B. Relationship between the soluble glutathione-dependent Δ5-3-ketosteroid isomerase and the glutathione S-transferases of the liver. Proceedings of the National Academy of Sciences, USA 1977; 74: 158–162
  • Bogaards J. J. P., Van Ommen B., Van Bladeren P. J. An improved method for the separation and quantification of glutathione S-transferase subunits in rat tissue using high-performance liquid chromatography. Journal of Chromatography 1989; 474: 435–440
  • Brakenhoff J. P. G., Commandeur J. N. M., De Kanter F. J. J., Van Baar B. L. M., Luijten W. C. M., Vermeulen N. P. E. Chemical and glutathione conjugation-related degradation of fotemustine: formation and characterization of a glutathione conjugate of diethyl (1-isocyanatoethyl)phosphonate, a reactive metabolite of fotemustine. Chemical Research in Toxicology 1994; 7: 380–389
  • Chen W. -J., Graminski G. F., Armstrong R. N. Dissection of the catalytic mechanism of isozyme 4–4 of glutathione S-transferase with alternative substrates. Biochemistry 1988; 27: 647–654
  • Commandeur J. N. M., Stijntjes G. J., Vermeulen N. P. E. Enzymes and transport systems involved in the formation and disposition of glutathione S-conjugates. Pharmacological Reviews 1995; 47: 1–60
  • Everyly C. R., Traynham J. G. Formation and rearrangement of Ipso intermediates in aromatic free-radical chlorination reactions. Journal of Organic Chemistry 1979; 44: 1784–1787
  • Fersht A. Basic equations of enzyme kinetics. Enzyme Structure and Mechanism, A. Fersht. Freeman, New York 1977; 98–120
  • Habig W. H., Jakoby W. B. Assays for differentiation of glutathione S-transferases. Methods in Enzymology 1981; 77: 398–405
  • Habig W. H., Pabst M. J., Jakoby W. B. Glutathione S-transferases. The first step in mercapturic acid formation. Journal of Biological Chemistry 1974; 249: 7130–7139
  • Hayes J. D., Wolf C. R. Review article-molecular mechanisms of drug resistance. Biochemical Journal 1990; 272: 281–295
  • Hess R. E., Schaeffer C. D., Yoder C. H. 13C-H coupling constants as a probe of ortho-substituent effects. Journal of Organic Chemistry 1971; 36: 2201–2202
  • Ishigaki S., Abramovitz M., Listowsky I. Glutathione S-transferases are major cytosolic thyroid hormone binding proteins. Archives of Biochemistry and Biophysics 1989; 273: 265–272
  • Ji X., Zhang P., Armstrong R. N., Gilliland G. L. The three-dimensional structure of glutathione S-transferase from the Mu gene class. Structural analysis of the binary complex of isoenzyme 3–3 and glutathione at 2.2-Å resolution. Biochemistry 1992; 31: 10169–10184
  • Johnson W. W., Liu S. X., Ji X. H., Gilliland G. L., Armstrong R. N. Tyrosine-115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase. Journal of Biological Chemistry 1993; 268: 11508–11511
  • Liu S., Zhang P., Ji X., Johnson W. W., Gilliland G. L., Armstrong R. N. Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3–3 of glutathione S-transferase. Journal of Biological Chemistry 1992; 267: 4296–4299
  • Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 1951; 193: 265–275
  • Mannervik B., Ålin P., Guthenberg C., Jenssen H., Tahir M. K., Warholm M., Jornvall H. Identification of three classes of glutathione transferases common to several mammalian species. Correlation between structural data and enzymatic properties. Proceedings of the National Academy of Sciences, USA 1985; 82: 7202–7206
  • Mannervik B., Danielson U. H. Glutathione transferases-structure and catalytic activity. CRC Critical Reviews in Biochemistry 1988; 23: 283–337
  • Meyer D. J., Coles B., Pemble S. E., Gilmore K. S., Fraser G. M., Ketterer B. Theta, a new class of glutathione transferases purified from rat and man liver. Biochemical Journal 1991; 274: 409–414
  • Miller J. Aromatic nucleophilic substitution. Reaction Mechanisms in Organic Chemistry, C. Eaborn, N. B. Chapman. Elsevier, New York 1968; vol. 8: 137–179
  • Ploemen J. H. T. M., Bogaards J. J. P., Veldink G. A., Van Ommen B., Jansen D. H. M., Van Bladeren P. J. Isoenzyme selective irreversible inhibition of rat and human glutathione S-transferases by ethacrynic acid and two brominated derivatives. Biochemical Pharmacology 1993; 45: 633–639
  • Ploemen J. H. T. M., Johnson W. W., Jespersen S., Vanderwall D., Van Ommen B., Greef Van Der J., Van Bladeren P. J., Armstrong R. N. Active-site tyrosyl residues are targets in the irreversible inhibition of a class mu glutathione transferase by 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone. Journal of Biological Chemistry 1994; 269: 26890–26897
  • Reinemer P., Dirr H. W., Ladenstein R., Huber R., Lo Bello M., Federici G., Parker M. W. Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. Journal of Molecular Biology 1992; 227: 214–226
  • Reinemer P., Dirr H. W., Ladenstein R., Schäffer J., Gallay O., Huber R. The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO Journal 1991; 10: 1997–2005
  • Sinning I., Kleywegt G. J., Cowan S. W., Reinemer P., Dirr H. W., Huber R., Gilliland G. L., Armstrong R. N., Ji X. H., Board P. G., Olin B., Mannervik B., Jones T. A. Structure determination and refinement of human-alpha class glutathione transferase A1–1, and a comparison with the Mu-class and Pi-class enzymes. Journal of Molecular Biology 1993; 232: 192–212
  • Stenberg G., Board P. G., Mannervik B. Mutation of an evolutionary conserved tyrosine residue in the active site of a human class alpha glutathione transferase. FEBS Letters 1991; 293: 153–155
  • Tan K. H., Meyer D. J., Coles B., Ketterer B. Thymine hydroperoxide, a substrate for rat Se-dependent glutathione peroxidase and glutathione S-transferase isoenzymes. FEBS Letters 1986; 207: 231–233
  • Vos R. M. E., Snoek M. C., Van Berkel W. J. H., Müller F., Van Bladeren P. J. Differential induction of rat hepatic glutathione S-transferase isoenzymes by hexachlorobenzene and benzyl isothiocyanate. Biochemical Pharmacology 1988; 37: 1077–1082
  • Wang R. W., Newton D. J., Johnson A. R., Pickett C. B., Lu A. Y. H. Site-directed mutagenesis of glutathione S-transferase Ya Ya. Mapping the glutathione-binding site. Journal of Biological Chemistry 1993; 268: 23981–23985
  • Waxman D. J. Glutathione S-transferases: role in alkylating agent, resistance and possible target for modulation chemotherapy—a review. Cancer Research 1990; 50: 6449–6454
  • Xia C., Meyer D. J., Chen H., Reinemer P., Huber P., Ketterer B. Chemical modification of GSH transferase P1–1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding dõmain of the active site. Biochemical Journal 1993; 293: 357–362
  • Zhang P., Liu S., Shan S., Ji X., Gilliland G. L., Armstrong R. N. Modular mutagenesis of exons 1, 2 and 8 of a glutathione S-transferase from the mu class. Mechanistic and structural consequences for chimeras of glutathione S-transferase 3–3. Biochemistry 1992; 31: 10185–10193

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