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Volumn 30, Issue 3, 1998, Pages 569-643

Strategies to characterize the mechanisms of action and the active sites of glutathione S-transferases: A review

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE;

EID: 0031950471     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.3109/03602539808996325     Document Type: Review
Times cited : (11)

References (169)
  • 1
    • 0026459859 scopus 로고
    • The ATP-dependent glutathione S-conjugate export pump
    • T. Ishikawa, The ATP-dependent glutathione S-conjugate export pump. Trends Biochem. Sci., 17, 463-468 (1992).
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 463-468
    • Ishikawa, T.1
  • 2
    • 0029008428 scopus 로고
    • Enzymes and transport systems involved in the formation and disposition of glutathione S-conjugates
    • J. N. M. Commandeur, G. J. Stijntjes, and N. P. E. Vermeulen, Enzymes and transport systems involved in the formation and disposition of glutathione S-conjugates, Pharmacol. Rev., 47, 271-330 (1995).
    • (1995) Pharmacol. Rev. , vol.47 , pp. 271-330
    • Commandeur, J.N.M.1    Stijntjes, G.J.2    Vermeulen, N.P.E.3
  • 3
    • 0000107746 scopus 로고
    • Identification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties
    • B. Mannervik, P. Ålin, C. Guthenberg, H. Jensson, M. K. Tahir, M. Warholm, and H. Jornvall, Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. USA, 82, 7202-7206 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7202-7206
    • Mannervik, B.1    Ålin, P.2    Guthenberg, C.3    Jensson, H.4    Tahir, M.K.5    Warholm, M.6    Jornvall, H.7
  • 5
    • 0027058697 scopus 로고
    • Glutathione S-transferases: Amino acid sequence comparison, classification and phylogenetic relationship
    • T. M. Buetler and D. L. Eaton, Glutathione S-transferases: amino acid sequence comparison, classification and phylogenetic relationship, Environ. Carcinogen. Ecotoxicol. Rev., C10, 181-203 (1992).
    • (1992) Environ. Carcinogen. Ecotoxicol. Rev. , vol.C10 , pp. 181-203
    • Buetler, T.M.1    Eaton, D.L.2
  • 7
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST* and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • J. D. Hayes and D. J. Pulford, The glutathione S-transferase supergene family: regulation of GST* and the contribution of the isoenzymes to cancer chemoprotection and drug resistance, Crit. Rev. Biochem. Molec. Biol., 30, 445-600 (1995).
    • (1995) Crit. Rev. Biochem. Molec. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 8
    • 0015238924 scopus 로고
    • Ligandin: A hepatic protein which binds steroids, bilirubin, carcinogens and a number of organic anions
    • G. Litwack, B. Ketterer, and I. M. Arias, Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of organic anions, Nature, 234, 466-467 (1971).
    • (1971) Nature , vol.234 , pp. 466-467
    • Litwack, G.1    Ketterer, B.2    Arias, I.M.3
  • 9
    • 0017819154 scopus 로고
    • Ligandin: Bilirubin binding and glutathione S-transferase activity are independent processes
    • M. M. Bhargava, I. Listowsky, and I. M. Arias, Ligandin: bilirubin binding and glutathione S-transferase activity are independent processes, J. Biol. Chem., 253, 4112-4115 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 4112-4115
    • Bhargava, M.M.1    Listowsky, I.2    Arias, I.M.3
  • 10
    • 0020316718 scopus 로고
    • Glutathione conjugation and DNA-binding of (±)-trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene and (±)-7β,8α-dihydroxy-9α, 10α-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene in isolated rat hepatocytes
    • B. Jernström, J. R. Babson, P. Moldéus, A. Homgren, and D. J. Reed, Glutathione conjugation and DNA-binding of (±)-trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene and (±)-7β,8α-dihydroxy-9α, 10α-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene in isolated rat hepatocytes, Carcinogenesis, 3, 861-866 (1982).
    • (1982) Carcinogenesis , vol.3 , pp. 861-866
    • Jernström, B.1    Babson, J.R.2    Moldéus, P.3    Homgren, A.4    Reed, D.J.5
  • 12
    • 0023922295 scopus 로고
    • Stereoselectivity of rat liver glutathione transferase isoenzymes for α-bromoisovaleric acid and α-bromoisovalerylurea enantiomers
    • J. M. Te Koppele, B. Coles, B. Ketterer, and G. J. Mulder, Stereoselectivity of rat liver glutathione transferase isoenzymes for α-bromoisovaleric acid and α-bromoisovalerylurea enantiomers, Biochem. J., 252, 137-142 (1988).
    • (1988) Biochem. J. , vol.252 , pp. 137-142
    • Te Koppele, J.M.1    Coles, B.2    Ketterer, B.3    Mulder, G.J.4
  • 13
    • 0027521246 scopus 로고
    • Stereoselectivity of human liver and intestinal cytosolic fractions as well as purified human glutathione S-transferase isoenzymes towards 2-bromoisovalerylurea enantiomers
    • T. M. T. Mulders, B. Van Ommen, P. J. Van Bladeren, D. D. Breimer, and G. J. Mulder, Stereoselectivity of human liver and intestinal cytosolic fractions as well as purified human glutathione S-transferase isoenzymes towards 2-bromoisovalerylurea enantiomers, Biochem. Pharmacol., 46, 1775-1780 (1993).
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1775-1780
    • Mulders, T.M.T.1    Van Ommen, B.2    Van Bladeren, P.J.3    Breimer, D.D.4    Mulder, G.J.5
  • 14
    • 0000259325 scopus 로고
    • An enzyme from rat liver catalyzing conjugation with glutathione
    • J. Booth, E. Boyland, and P. Sims, An enzyme from rat liver catalyzing conjugation with glutathione, Biochem. J., 79, 516-524 (1961).
    • (1961) Biochem. J. , vol.79 , pp. 516-524
    • Booth, J.1    Boyland, E.2    Sims, P.3
  • 16
    • 0018438330 scopus 로고
    • The binding and catalytic activities of forms of ligandin after modification of its thiol groups
    • T. Carne, E. Tipping, and B. Ketterer, The binding and catalytic activities of forms of ligandin after modification of its thiol groups, Biochem. J., 177, 433-439 (1979).
    • (1979) Biochem. J. , vol.177 , pp. 433-439
    • Carne, T.1    Tipping, E.2    Ketterer, B.3
  • 17
    • 0024672971 scopus 로고
    • Studies on the active site of rat glutathione S-transferase isoenzyme 4-4. Chemical modification by tetrachloro-1,4-benzoquinone and its glutathione conjugate
    • B. Van Ommen, J. H. T. M. Ploemen, H. J. Ruven, R. M. E. Vos, J. J. P. Bogaards, W. J. H. Van Berkel, and P. J. Van Bladeren, Studies on the active site of rat glutathione S-transferase isoenzyme 4-4. Chemical modification by tetrachloro-1,4-benzoquinone and its glutathione conjugate, Eur. J. Biochem., 181, 423-429 (1989).
    • (1989) Eur. J. Biochem. , vol.181 , pp. 423-429
    • Van Ommen, B.1    Ploemen, J.H.T.M.2    Ruven, H.J.3    Vos, R.M.E.4    Bogaards, J.J.P.5    Van Berkel, W.J.H.6    Van Bladeren, P.J.7
  • 18
    • 18544398557 scopus 로고
    • Cysteine plays a role in catalysis in glutathione S-transferase 1-1
    • R. M. McCarthy and D. Sheehan, Cysteine plays a role in catalysis in glutathione S-transferase 1-1, Biochem. Soc. Trans., 23, 388S (1995).
    • (1995) Biochem. Soc. Trans. , vol.23
    • McCarthy, R.M.1    Sheehan, D.2
  • 19
    • 0025860039 scopus 로고    scopus 로고
    • Irreversible inhibition of human glutathione S-transferase isoenzymes by tetrachloro-1,4-benzoquinone and its glutathione conjugate
    • J. H. T. M. Ploemen, B. Van Ommen, and P. J. Van Bladeren, Irreversible inhibition of human glutathione S-transferase isoenzymes by tetrachloro-1,4-benzoquinone and its glutathione conjugate, Biochem. Pharmacol., 41, 1665-1669 (1996).
    • (1996) Biochem. Pharmacol. , vol.41 , pp. 1665-1669
    • Ploemen, J.H.T.M.1    Van Ommen, B.2    Van Bladeren, P.J.3
  • 21
  • 22
    • 0025742879 scopus 로고
    • Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 33
    • J-C. Hsieh, S-C. Huang, W-L. Chen, Y-C. Lai, and M. F. Tam, Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 33, Biochem. J., 278, 293-297 (1991).
    • (1991) Biochem. J. , vol.278 , pp. 293-297
    • Hsieh, J.-C.1    Huang, S.-C.2    Chen, W.-L.3    Lai, Y.-C.4    Tam, M.F.5
  • 23
    • 0025935297 scopus 로고
    • The single cysteine residue on an alpha family chick liver glutathione S-transferase CL 3-3 is not functionally important
    • L-H. Chang, L-Y. Wang, and M. F. Tam, The single cysteine residue on an alpha family chick liver glutathione S-transferase CL 3-3 is not functionally important, Biochem. Biophys. Res. Commun., 180, 323-328 (1991).
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 323-328
    • Chang, L.-H.1    Wang, L.-Y.2    Tam, M.F.3
  • 24
    • 0027249687 scopus 로고
    • Inactivation of mouse liver glutathione S-transferase YfYf (Pi class) by ethacrynic acid and 5,5′-dithiobis-(2-nitro-benzoic acid)
    • M. F. Phillips and T. J. Mantle, Inactivation of mouse liver glutathione S-transferase YfYf (Pi class) by ethacrynic acid and 5,5′-dithiobis-(2-nitro-benzoic acid), Biochem. J., 294, 57-62 (1993).
    • (1993) Biochem. J. , vol.294 , pp. 57-62
    • Phillips, M.F.1    Mantle, T.J.2
  • 25
    • 0028209437 scopus 로고
    • Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1
    • J. H. T. M. Ploemen, A. Van Schanke, B. Van Ommen, and P. J. Van Bladeren, Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase P1-1, Cancer Res., 54, 915-919 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 915-919
    • Ploemen, J.H.T.M.1    Van Schanke, A.2    Van Ommen, B.3    Van Bladeren, P.J.4
  • 26
    • 0026657724 scopus 로고
    • Site-directed mutagenesis of glutathione S-transferase YaYa: Functional studies of histidine, cysteine and trypthophane mutants
    • R. W. Wang, D. J. Newton, C. B. Pickett, and A. Y. H. Lu, Site-directed mutagenesis of glutathione S-transferase YaYa: functional studies of histidine, cysteine and trypthophane mutants, Arch. Biochem. Biophys., 297, 86-91 (1992).
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 86-91
    • Wang, R.W.1    Newton, D.J.2    Pickett, C.B.3    Lu, A.Y.H.4
  • 27
    • 0025999878 scopus 로고
    • Cysteine residues are not essential for the catalytic activity of human class mu glutathione transferase M1a-1a
    • M. Widersten, E. Holmström, and B. Mannervik, Cysteine residues are not essential for the catalytic activity of human class mu glutathione transferase M1a-1a, FEBS Lett., 293, 156-159 (1991).
    • (1991) FEBS Lett. , vol.293 , pp. 156-159
    • Widersten, M.1    Holmström, E.2    Mannervik, B.3
  • 28
    • 0026348775 scopus 로고
    • Non-essentiality of cysteine and histidine residues for the activity of human class pi glutathione S-transferase
    • K.-H. Kong, H. Inoue, and K. Takahashi, Non-essentiality of cysteine and histidine residues for the activity of human class pi glutathione S-transferase, Biochem. Biophys. Res. Commun., 181, 748-755 (1991).
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 748-755
    • Kong, K.-H.1    Inoue, H.2    Takahashi, K.3
  • 29
    • 0026474677 scopus 로고
    • Characterization of cysteine residues of glutathione S-transferase P: Evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47
    • J. Nishihira, T. Ishibashi, M. Sakai, S. Nishi, T. Kumazaki, Y. Hatanaka, S. Tsuda, and K. Hikichi, Characterization of cysteine residues of glutathione S-transferase P: evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47, Biochem. Biophys. Res. Commun., 188, 424-432 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 424-432
    • Nishihira, J.1    Ishibashi, T.2    Sakai, M.3    Nishi, S.4    Kumazaki, T.5    Hatanaka, Y.6    Tsuda, S.7    Hikichi, K.8
  • 30
    • 0014869437 scopus 로고
    • The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites
    • M. S. Rose and E. A. Lock, The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites, Biochem. J., 120, 151-157 (1970).
    • (1970) Biochem. J. , vol.120 , pp. 151-157
    • Rose, M.S.1    Lock, E.A.2
  • 31
    • 0023100097 scopus 로고
    • Evidence for the involvement of histidine at the active site of glutathione S-transferase ψ from human liver
    • Y. C. Awasthi, A. Bhatnagar, and S. V. Singh, Evidence for the involvement of histidine at the active site of glutathione S-transferase ψ from human liver, Biochem. Biophys. Res. Commun., 143, 965-970 (1987).
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 965-970
    • Awasthi, Y.C.1    Bhatnagar, A.2    Singh, S.V.3
  • 33
    • 0027480756 scopus 로고
    • Site-directed mutagenesis and chemical modification of histidine residues on an α-class chick liver glutathione S-transferase CL 3-3
    • L. H. Chang and M. F. Tam, Site-directed mutagenesis and chemical modification of histidine residues on an α-class chick liver glutathione S-transferase CL 3-3, Eur. J. Biochem., 211, 805-811 (1993).
    • (1993) Eur. J. Biochem. , vol.211 , pp. 805-811
    • Chang, L.H.1    Tam, M.F.2
  • 34
    • 0029009697 scopus 로고
    • Chemical modification of a cloned glutathione S-transferase from Schistosoma japonicum: Evidence for an essential histidine residue
    • J. Walker, P. Crowley, and J. Barrett, Chemical modification of a cloned glutathione S-transferase from Schistosoma japonicum: evidence for an essential histidine residue, Exp. Parasitol., 80, 616-623 (1995).
    • (1995) Exp. Parasitol. , vol.80 , pp. 616-623
    • Walker, J.1    Crowley, P.2    Barrett, J.3
  • 35
    • 0026629005 scopus 로고
    • Chemical modification of human placental glutathione transferase by pyridoxal 5′-phosphate
    • M. Lo Bello, R. Petruzzelli, L. Reale, G. Ricci, D. Barra, and G. Federici, Chemical modification of human placental glutathione transferase by pyridoxal 5′-phosphate, Biochim. Biophys. Acta, 1121, 167-172 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 167-172
    • Lo Bello, M.1    Petruzzelli, R.2    Reale, L.3    Ricci, G.4    Barra, D.5    Federici, G.6
  • 36
    • 0026722795 scopus 로고
    • Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione a 2.8 Å resolution
    • P. Reinemer, H. W. Dirr, R. Ladenstein, R. Huber, M. Lo Bello, G. Federici, and M. W. Parker, Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione a 2.8 Å resolution, J. Molec. Biol., 227, 214-226 (1992).
    • (1992) J. Molec. Biol. , vol.227 , pp. 214-226
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Huber, R.4    Lo Bello, M.5    Federici, G.6    Parker, M.W.7
  • 37
    • 0027194321 scopus 로고
    • Chemical modification of GSH transferase P1-1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding domain of the active site
    • C. Xia, D. J. Meyer, H. Chen, P. Reinemer, R. Huber, and B. Ketterer, Chemical modification of GSH transferase P1-1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding domain of the active site, Biochem. J., 293, 357-362 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 357-362
    • Xia, C.1    Meyer, D.J.2    Chen, H.3    Reinemer, P.4    Huber, R.5    Ketterer, B.6
  • 38
    • 0025816448 scopus 로고
    • The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution
    • P. Reinemer, H. W. Dirr, R. Ladenstein, J. Schäffer, O. Gallay, and R. Huber, The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution, EMBO J., 10, 1997-2005 (1991).
    • (1991) EMBO J. , vol.10 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schäffer, J.4    Gallay, O.5    Huber, R.6
  • 39
    • 0028079744 scopus 로고
    • Refined crystal structure of porcine class π glutathione S-transferase (pGST P1-1) at 2.1 Å resolution
    • H. W. Dirr, P. Reinemer, and R. Huber, Refined crystal structure of porcine class π glutathione S-transferase (pGST P1-1) at 2.1 Å resolution, J. Molec. Biol., 243, 72-92 (1994).
    • (1994) J. Molec. Biol. , vol.243 , pp. 72-92
    • Dirr, H.W.1    Reinemer, P.2    Huber, R.3
  • 40
    • 0026778393 scopus 로고
    • Contribution of five amino acid residues in the glutathione binding site to the function of glutathione transferase P1-1
    • M. Widersten, R. H. Kolm, R. Björnestedt, and B. Mannervik, Contribution of five amino acid residues in the glutathione binding site to the function of glutathione transferase P1-1, Biochem. J., 285, 377-381 (1992).
    • (1992) Biochem. J. , vol.285 , pp. 377-381
    • Widersten, M.1    Kolm, R.H.2    Björnestedt, R.3    Mannervik, B.4
  • 41
    • 0026652120 scopus 로고
    • Mutational substitution of residues implicated by crystal structure in binding the substrate glutathione to human glutathione S-transferase pi
    • T. W. Manoharan, A. M. Gulick, P. Reinemer, H. W. Dirr, R. Huber, and W. W. Fahl, Mutational substitution of residues implicated by crystal structure in binding the substrate glutathione to human glutathione S-transferase pi, J. Molec. Biol., 226, 319-322 (1992).
    • (1992) J. Molec. Biol. , vol.226 , pp. 319-322
    • Manoharan, T.W.1    Gulick, A.M.2    Reinemer, P.3    Dirr, H.W.4    Huber, R.5    Fahl, W.W.6
  • 42
    • 0345082665 scopus 로고
    • Similarities in inactivation of glutathione S-transferases by arginine specific chemical modifying agents
    • C. S. Schasteen, B. M. Krivak, and D. J. Reed, Similarities in inactivation of glutathione S-transferases by arginine specific chemical modifying agents, Fed. Proc., 42, 2036 (1983).
    • (1983) Fed. Proc. , vol.42 , pp. 2036
    • Schasteen, C.S.1    Krivak, B.M.2    Reed, D.J.3
  • 43
    • 0029170741 scopus 로고
    • Chemical modification of glutathione S-transferase from C6/36, an Aedes albopictus cell line
    • P.-S. Chen, T.-C. Wang, and G.-G. Chang, Chemical modification of glutathione S-transferase from C6/36, an Aedes albopictus cell line, Insect Biochem. Molec. Biol., 25, 613-619 (1995).
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 613-619
    • Chen, P.-S.1    Wang, T.-C.2    Chang, G.-G.3
  • 44
    • 0026529977 scopus 로고
    • Tyrosine-7 is an essential residue for the catalytic activity of human class pi glutathione S-transferase: Chemical modification and site-directed mutagenesis studies
    • K.-H. Kong, M. Nishida, H. Inoue, and K. Takahashi, Tyrosine-7 is an essential residue for the catalytic activity of human class pi glutathione S-transferase: chemical modification and site-directed mutagenesis studies, Biochem. Biophys. Res. Commun., 182, 1122-1129 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1122-1129
    • Kong, K.-H.1    Nishida, M.2    Inoue, H.3    Takahashi, K.4
  • 46
    • 0026736592 scopus 로고
    • Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1-1
    • R. H. Kolm, G. E. Sroga, and B. Mannervik, Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1-1, Biochem. J., 285, 537-540 (1992).
    • (1992) Biochem. J. , vol.285 , pp. 537-540
    • Kolm, R.H.1    Sroga, G.E.2    Mannervik, B.3
  • 47
    • 0026705291 scopus 로고
    • Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase
    • S. Liu, P. Zhang, X. Ji, W. W. Johnson, G. L. Gilliland, and R. N. Armstrong, Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase, J. Biol. Chem., 267, 4296-4299 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 4296-4299
    • Liu, S.1    Zhang, P.2    Ji, X.3    Johnson, W.W.4    Gilliland, G.L.5    Armstrong, R.N.6
  • 48
    • 0027216743 scopus 로고
    • Identification of ionizable groups essential for the enzyme catalysis on glutathione S-transferase P
    • J. Nishihira, M. Sakai, and S. Nishi, Identification of ionizable groups essential for the enzyme catalysis on glutathione S-transferase P, Biochem. Biophys. Res. Commun., 194, 1466-1474 (1993).
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1466-1474
    • Nishihira, J.1    Sakai, M.2    Nishi, S.3
  • 49
    • 0026741014 scopus 로고
    • Evidence for the involvement of tryptophane 38 in the active site of glutathione S-transferase P
    • J. Nishihira, T. Ishibashi, M. Sakai, S. Nishi, and T. Kumazaki, Evidence for the involvement of tryptophane 38 in the active site of glutathione S-transferase P, Biochem. Biophys. Res. Commun., 185, 1069-1077 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 1069-1077
    • Nishihira, J.1    Ishibashi, T.2    Sakai, M.3    Nishi, S.4    Kumazaki, T.5
  • 50
    • 0023766436 scopus 로고
    • Active site-directed irreversible inhibition of glutathione S-transferases by the glutathione conjugate of tetrachloro-1,4-benzoquinone
    • B. Van Ommen, C. Den Besten, A. L. M. Rutten, J. H. T. M. Ploemen, R. M. E. Vos, F. Müller, and P. J. Van Bladeren, Active site-directed irreversible inhibition of glutathione S-transferases by the glutathione conjugate of tetrachloro-1,4-benzoquinone, J. Biol. Chem., 263, 12939-12942 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 12939-12942
    • Van Ommen, B.1    Den Besten, C.2    Rutten, A.L.M.3    Ploemen, J.H.T.M.4    Vos, R.M.E.5    Müller, F.6    Van Bladeren, P.J.7
  • 51
    • 0028131953 scopus 로고
    • 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
    • J. H. T. M. Ploemen, W. W. Johnson, S. Jespersen, D. Vanderwall, B. Van Ommen, J. Van der Greef, P. J. Van Bladeren, and R. N. Armstrong, 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, J. Biol. Chem., 269, 26890-26897 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 26890-26897
    • Ploemen, J.H.T.M.1    Johnson, W.W.2    Jespersen, S.3    Vanderwall, D.4    Van Ommen, B.5    Van Der Greef, J.6    Van Bladeren, P.J.7    Armstrong, R.N.8
  • 52
    • 0028607620 scopus 로고
    • Modification of glutathione S-transferase 3-3 mutants with 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone. Identification of the C-terminal tryptic fragments as part of the H-site and evidence that 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone is not specific for cysteine labelling
    • J.-L. Hong, L.-F. Liu, L.-Y. Wang, S.-P. Tsai, C.-H. Hsieh, C.-D. Hsiao, and M. F. Tam, Modification of glutathione S-transferase 3-3 mutants with 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone. Identification of the C-terminal tryptic fragments as part of the H-site and evidence that 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone is not specific for cysteine labelling, Biochem. J., 304, 825-831 (1994).
    • (1994) Biochem. J. , vol.304 , pp. 825-831
    • Hong, J.-L.1    Liu, L.-F.2    Wang, L.-Y.3    Tsai, S.-P.4    Hsieh, C.-H.5    Hsiao, C.-D.6    Tam, M.F.7
  • 53
    • 0026320285 scopus 로고
    • S-(4-Bromo-2,3-dioxobutyl)glutathione: A new affinity label for the 4-4 isoenzyme of rat liver glutathione S-transferase
    • R. M. Katusz and R. F Colman, S-(4-Bromo-2,3-dioxobutyl)glutathione: a new affinity label for the 4-4 isoenzyme of rat liver glutathione S-transferase, Biochemistry, 30, 11230-11238 (1991).
    • (1991) Biochemistry , vol.30 , pp. 11230-11238
    • Katusz, R.M.1    Colman, R.F.2
  • 54
    • 0027241006 scopus 로고
    • Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase
    • W. W. Johnson, S. Liu, X. Ji, G. L. Gilliland, and R. N. Armstrong, Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase, J. Biol. Chem., 268, 11508-11511 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 11508-11511
    • Johnson, W.W.1    Liu, S.2    Ji, X.3    Gilliland, G.L.4    Armstrong, R.N.5
  • 55
    • 0026519636 scopus 로고
    • Mapping the substrate-binding site of a human class mu glutathione transferase using nuclear magnetic resonance spectroscopy
    • C. J. Pennington and G. S. Rule, Mapping the substrate-binding site of a human class mu glutathione transferase using nuclear magnetic resonance spectroscopy, Biochemistry, 31, 2912-2920 (1992).
    • (1992) Biochemistry , vol.31 , pp. 2912-2920
    • Pennington, C.J.1    Rule, G.S.2
  • 56
    • 0026613704 scopus 로고
    • 115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3
    • 115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3, Arch. Biochem. Biophys., 298, 667-677 (1992).
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 667-677
    • Katusz, R.M.1    Bono, B.2    Colman, R.F.3
  • 57
    • 0026611616 scopus 로고
    • 111 of glutathione S-transferase, isoenzyme 1-1, by S-(4-bromo-2,3-dioxobutyl)-glutathione
    • 111 of glutathione S-transferase, isoenzyme 1-1, by S-(4-bromo-2,3-dioxobutyl)-glutathione, Biochemistry, 31, 8984-8990 (1992).
    • (1992) Biochemistry , vol.31 , pp. 8984-8990
    • Katusz, R.M.1    Bono, B.2    Colman, R.F.3
  • 58
    • 0027769771 scopus 로고
    • 115 to be an important determinant of xenobiotic substrate specificity
    • 115 to be an important determinant of xenobiotic substrate specificity, Biochemistry, 32, 13002-13011 (1993).
    • (1993) Biochemistry , vol.32 , pp. 13002-13011
    • Barycki, J.J.1    Colman, R.F.2
  • 59
    • 0029941851 scopus 로고    scopus 로고
    • Tyrosine 8 contributes to catalysis but is not required for activity of rat liver glutathione S-transferase, 1-1
    • J. Wang, J. J. Barycki, and R. F. Colman, Tyrosine 8 contributes to catalysis but is not required for activity of rat liver glutathione S-transferase, 1-1. Protein Sci., 5, 1032-1042 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 1032-1042
    • Wang, J.1    Barycki, J.J.2    Colman, R.F.3
  • 60
    • 0029127173 scopus 로고
    • Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase 3-3
    • L. Hu and R. F. Colman, Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase 3-3, J. Biol. Chem., 270, 21875-21883 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21875-21883
    • Hu, L.1    Colman, R.F.2
  • 61
    • 0022237942 scopus 로고
    • Isolation and characterization of the multiple glutathione S-transferases from human liver. Evidence for unique heme-binding sites
    • D. L. Vander Jagt, L. A. Hunsaker, K. B. Garcia, and R. E. Royer, Isolation and characterization of the multiple glutathione S-transferases from human liver. Evidence for unique heme-binding sites, J. Biol. Chem., 260, 11603-11610 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 11603-11610
    • Vander Jagt, D.L.1    Hunsaker, L.A.2    Garcia, K.B.3    Royer, R.E.4
  • 62
    • 0027436258 scopus 로고
    • Reversible modification of rat liver glutathione S-transferase 3-3 with 1-chloro-2,4-dinitrobenzene: Specific labelling of Tyr-115
    • L.-F. Liu, J.-L. Hong, S.-P. Tsai, J.-C. Hsieh, and M. F. Tam, Reversible modification of rat liver glutathione S-transferase 3-3 with 1-chloro-2,4-dinitrobenzene: specific labelling of Tyr-115, Biochem, J., 296, 189-197 (1993).
    • (1993) Biochem, J. , vol.296 , pp. 189-197
    • Liu, L.-F.1    Hong, J.-L.2    Tsai, S.-P.3    Hsieh, J.-C.4    Tam, M.F.5
  • 64
    • 0004273970 scopus 로고
    • (B. Horecker, N. O. Kaplan, J. Marmur, and H. A. Scheraga, eds.), Academic Press, New York
    • G. G. Hammes, Enzyme Catalysis and Regulation (B. Horecker, N. O. Kaplan, J. Marmur, and H. A. Scheraga, eds.), Academic Press, New York, 1982.
    • (1982) Enzyme Catalysis and Regulation
    • Hammes, G.G.1
  • 65
    • 0006339343 scopus 로고
    • The chemical modification of proteins by group-specific and site-specific reagents
    • (H. Neurath and R. L. Hill, eds.), Academic Press, New York
    • A. N. Glazer, The chemical modification of proteins by group-specific and site-specific reagents, in The Proteins (H. Neurath and R. L. Hill, eds.), Academic Press, New York, 1976, pp. 2-103.
    • (1976) The Proteins , pp. 2-103
    • Glazer, A.N.1
  • 66
    • 0019326970 scopus 로고
    • Photoaffinity labelling by S-(p-azidophenacyl)glutathione of glyoxalase II and glutathione S-transferase
    • A. P. Seddon, M. Bunni, and K. T. Douglas, Photoaffinity labelling by S-(p-azidophenacyl)glutathione of glyoxalase II and glutathione S-transferase, Biochem. Biophys. Res. Commun., 95, 446-452 (1980).
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 446-452
    • Seddon, A.P.1    Bunni, M.2    Douglas, K.T.3
  • 67
    • 0024457718 scopus 로고
    • Localization of a portion of the active site of two rat liver glutathione S-transferases using a photoaffinity label
    • R. M. Hoesch and T. D. Boyer, Localization of a portion of the active site of two rat liver glutathione S-transferases using a photoaffinity label, J. Biol. Chem., 264, 17712-17717 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 17712-17717
    • Hoesch, R.M.1    Boyer, T.D.2
  • 68
    • 0028075427 scopus 로고
    • Photoaffinity labelling of the active site of the rat glutathione transferases 3-3 and 1-1 and human glutathione transferase A1-1
    • R. Cooke, R. Björnestedt, K. T. Douglas, J. H. McKie, M. D. King, B. Coles, B. Ketterer, and B. Mannervik, Photoaffinity labelling of the active site of the rat glutathione transferases 3-3 and 1-1 and human glutathione transferase A1-1, Biochem. J., 302, 383-390 (1994).
    • (1994) Biochem. J. , vol.302 , pp. 383-390
    • Cooke, R.1    Björnestedt, R.2    Douglas, K.T.3    McKie, J.H.4    King, M.D.5    Coles, B.6    Ketterer, B.7    Mannervik, B.8
  • 71
    • 0029133325 scopus 로고
    • Identification of the electrophilic substrate-binding site of glutathione S-transferase P by photo-affinity labeling
    • J. Nishihira, M. Sakai, S. Nishi, and Y. Hatanaka, Identification of the electrophilic substrate-binding site of glutathione S-transferase P by photo-affinity labeling, Eur. J. Biochem., 232, 106-110 (1995).
    • (1995) Eur. J. Biochem. , vol.232 , pp. 106-110
    • Nishihira, J.1    Sakai, M.2    Nishi, S.3    Hatanaka, Y.4
  • 72
    • 0028218792 scopus 로고
    • Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S-(-p-nitrobenzyl)glutathione and other inhibitors
    • I. García-Sáez, A. Párraga, M. F. Phillips, T. J. Mantle, and M. Coll, Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S-(-p-nitrobenzyl)glutathione and other inhibitors, J. Molec. Biol., 237, 298-314 (1994).
    • (1994) J. Molec. Biol. , vol.237 , pp. 298-314
    • García-Sáez, I.1    Párraga, A.2    Phillips, M.F.3    Mantle, T.J.4    Coll, M.5
  • 73
    • 0030602878 scopus 로고    scopus 로고
    • Structural studies of a human pi class glutathione S-transferase. Photoaffinity labeling of the active site and target size analysis
    • R. Whalen, E. S. Kempner, and T. D. Boyer, Structural studies of a human pi class glutathione S-transferase. Photoaffinity labeling of the active site and target size analysis, Biochem. Pharmacol., 52, 281-288 (1996).
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 281-288
    • Whalen, R.1    Kempner, E.S.2    Boyer, T.D.3
  • 74
    • 0026782101 scopus 로고
    • Site-directed mutagenesis and chemical modification of cysteine residues of rat glutathione S-transferase 3-3
    • W.-L. Chen, J.-C. Hsieh, J.-L. Hong, S.-P. Tsai, and M. F. Tam, Site-directed mutagenesis and chemical modification of cysteine residues of rat glutathione S-transferase 3-3, Biochem. J., 286, 205-210 (1992).
    • (1992) Biochem. J. , vol.286 , pp. 205-210
    • Chen, W.-L.1    Hsieh, J.-C.2    Hong, J.-L.3    Tsai, S.-P.4    Tam, M.F.5
  • 76
    • 0028809193 scopus 로고
    • Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperativity in glutathione transferase P1-1
    • G. Ricci, M. Lo Bello, A. M. Caccuri, A. Pastore, M. Nuccetelli, M. W. Parker, and G. Federici, Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperativity in glutathione transferase P1-1, J. Biol. Chem., 270, 1243-1248 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 1243-1248
    • Ricci, G.1    Lo Bello, M.2    Caccuri, A.M.3    Pastore, A.4    Nuccetelli, M.5    Parker, M.W.6    Federici, G.7
  • 77
    • 0019853770 scopus 로고
    • Purification and bilirubin binding properties of glutathione S-transferase from human placenta
    • D. L. Vander Jagt, S. P. Wilson, and J. E. Heidrich, Purification and bilirubin binding properties of glutathione S-transferase from human placenta, FEBS Lett., 136, 319-321 (1981).
    • (1981) FEBS Lett. , vol.136 , pp. 319-321
    • Vander Jagt, D.L.1    Wilson, S.P.2    Heidrich, J.E.3
  • 79
    • 0028842236 scopus 로고
    • Site-directed mutagenesis of human glutathione transferase P1-1. Spectral, kinetic and structural properties of Cys-47 and Lys-54 mutants
    • M. Lo Bello, A. Battistoni, A. P. Mazzetti, P. G. Board, M. Muramatsu, G. Federici, and G. Ricci, Site-directed mutagenesis of human glutathione transferase P1-1. Spectral, kinetic and structural properties of Cys-47 and Lys-54 mutants, J. Biol. Chem., 270, 1249-1253 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 1249-1253
    • Lo Bello, M.1    Battistoni, A.2    Mazzetti, A.P.3    Board, P.G.4    Muramatsu, M.5    Federici, G.6    Ricci, G.7
  • 80
    • 0025864823 scopus 로고
    • Site-directed mutagenesis of glutathione S-transferase YaYa: Nonessential role of histidine in catalysis
    • R. W. Wang, D. J. Newton, C. B. Pickett, and A. Y. H. Lu, Site-directed mutagenesis of glutathione S-transferase YaYa: nonessential role of histidine in catalysis, Arch. Biochem. Biophys., 286, 574-578 (1991).
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 574-578
    • Wang, R.W.1    Newton, D.J.2    Pickett, C.B.3    Lu, A.Y.H.4
  • 81
    • 0026641325 scopus 로고
    • A structural role of histidine 15 in human glutathione transferase M1-1, an amino acid residue conserved in class Mu enzymes
    • M. Widersten and B. Mannervik, A structural role of histidine 15 in human glutathione transferase M1-1, an amino acid residue conserved in class Mu enzymes, Protein Eng., 5, 551-557 (1992).
    • (1992) Protein Eng. , vol.5 , pp. 551-557
    • Widersten, M.1    Mannervik, B.2
  • 82
    • 0026024379 scopus 로고
    • Effects of directed mutagenesis on conserved arginine residues in a human class alpha glutathione transferase
    • G. Stenberg, P. G. Board, I. Carlberg, and B. Mannervik, Effects of directed mutagenesis on conserved arginine residues in a human class alpha glutathione transferase, Biochem. J., 274, 549-555 (1991).
    • (1991) Biochem. J. , vol.274 , pp. 549-555
    • Stenberg, G.1    Board, P.G.2    Carlberg, I.3    Mannervik, B.4
  • 83
    • 0027420775 scopus 로고
    • Site-directed mutagenesis of glutathione S-transferase YaYa: Mapping the glutathione binding site
    • R. W. Wang, D. J. Newton, A. R. Johnson, C. B. Pickett, and A. Y. H. Lu, Site-directed mutagenesis of glutathione S-transferase YaYa: mapping the glutathione binding site, J. Biol. Chem., 268, 23981-23985 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 23981-23985
    • Wang, R.W.1    Newton, D.J.2    Johnson, A.R.3    Pickett, C.B.4    Lu, A.Y.H.5
  • 85
    • 0027086872 scopus 로고
    • Site-directed mutagenesis of amino acid residues involved in the glutathione binding of human glutathione S-transferase P1-1
    • K.-H. Kong, H. Inoue, and K. Takahashi, Site-directed mutagenesis of amino acid residues involved in the glutathione binding of human glutathione S-transferase P1-1, J. Biochem., 112, 725-728 (1992).
    • (1992) J. Biochem. , vol.112 , pp. 725-728
    • Kong, K.-H.1    Inoue, H.2    Takahashi, K.3
  • 86
    • 0026753498 scopus 로고
    • Structural studies on human glutathione S-transferase π. Substitution mutations to determine amino acids necessary for binding glutathione
    • T. H. Manoharan, A. M. Gulick, R. B. Puchalski, A. L. Servais, and W. E. Fahl, Structural studies on human glutathione S-transferase π. Substitution mutations to determine amino acids necessary for binding glutathione, J. Biol. Chem., 267, 18940-18945 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 18940-18945
    • Manoharan, T.H.1    Gulick, A.M.2    Puchalski, R.B.3    Servais, A.L.4    Fahl, W.E.5
  • 87
    • 0026051660 scopus 로고
    • Mutation of an evolutionarily conserved tyrosine residue in the active site of a human class alpha glutathione transferase
    • G. Stenberg, P. G. Board, and M. Mannervik, Mutation of an evolutionarily conserved tyrosine residue in the active site of a human class alpha glutathione transferase, FEBS Lett., 293, 153-155 (1991).
    • (1991) FEBS Lett. , vol.293 , pp. 153-155
    • Stenberg, G.1    Board, P.G.2    Mannervik, M.3
  • 88
    • 0026640526 scopus 로고
    • Site-directed mutagenesis of glutathione S-transferase YaYa. Important roles of tyrosine 9 and aspartic acid 101 in catalysis
    • R. W. Wang, D. J. Newton, S.-E. W. Huskey, B. M. McKeever, C. B. Pickett, and A. Y. H. Lu, Site-directed mutagenesis of glutathione S-transferase YaYa. Important roles of tyrosine 9 and aspartic acid 101 in catalysis, J. Biol. Chem., 267, 19866-19871 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 19866-19871
    • Wang, R.W.1    Newton, D.J.2    Huskey, S.-E.W.3    McKeever, B.M.4    Pickett, C.B.5    Lu, A.Y.H.6
  • 90
    • 0029953767 scopus 로고    scopus 로고
    • Ligand effects on the fluorescence properties of tyrosine-9 in alpha 1-1 glutathione S-transferase
    • E. C. Dietze, R. W. Wang, A. Y. H. Lu, and W. M. Atkins, Ligand effects on the fluorescence properties of tyrosine-9 in alpha 1-1 glutathione S-transferase, Biochemistry, 35, 6745-6753 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6745-6753
    • Dietze, E.C.1    Wang, R.W.2    Lu, A.Y.H.3    Atkins, W.M.4
  • 92
    • 0001457141 scopus 로고
    • Second-sphere electrostatic effects in the active site of glutathione S-transferase. Observation of an on-face hydrogen bond between the side chain of threonine 13 and the π-cloud of tyrosine 6 and its influence on catalysis
    • S. Liu, X. Ji, G. L. Gilliland, W. J. Stevens, and R. N. Armstrong, Second-sphere electrostatic effects in the active site of glutathione S-transferase. Observation of an on-face hydrogen bond between the side chain of threonine 13 and the π-cloud of tyrosine 6 and its influence on catalysis, J. Am. Chem. Soc., 115, 7910-7911 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7910-7911
    • Liu, S.1    Ji, X.2    Gilliland, G.L.3    Stevens, W.J.4    Armstrong, R.N.5
  • 94
    • 0027170216 scopus 로고
    • Electrostatic evidence for the activation of the glutathione thiol by Tyr7 in π-class glutathione transferases
    • A. Karshikoff, P. Reinemer, R. Huber, and R. Ladenstein, Electrostatic evidence for the activation of the glutathione thiol by Tyr7 in π-class glutathione transferases, Eur. J. Biochem., 215, 663-670 (1993).
    • (1993) Eur. J. Biochem. , vol.215 , pp. 663-670
    • Karshikoff, A.1    Reinemer, P.2    Huber, R.3    Ladenstein, R.4
  • 95
    • 0029960278 scopus 로고    scopus 로고
    • Proton configuration in the ground state and transition state of a glutathione transferase-catalyzed reaction inferred from the properties of tetradeca(3-fluorotyrosyl)glutathione transferase
    • J. F. Parsons and R. N. Armstrong, Proton configuration in the ground state and transition state of a glutathione transferase-catalyzed reaction inferred from the properties of tetradeca(3-fluorotyrosyl)glutathione transferase, J. Am. Chem. Soc., 118, 2295-2296 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2295-2296
    • Parsons, J.F.1    Armstrong, R.N.2
  • 96
    • 0028568331 scopus 로고
    • Molecular cloning and site-directed mutagenesis of glutathione S-transferase from Escherichia coli
    • M. Nishida, K.-H. Kong, H. Inoue, and K. Takahashi, Molecular cloning and site-directed mutagenesis of glutathione S-transferase from Escherichia coli, J. Biol. Chem., 269, 32536-32541 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 32536-32541
    • Nishida, M.1    Kong, K.-H.2    Inoue, H.3    Takahashi, K.4
  • 97
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • M. C. J. Wilce, P. G. Board, S. C. Feil, and M. W. Parker, Crystal structure of a theta-class glutathione transferase, EMBO J., 14, 2133-2143 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2133-2143
    • Wilce, M.C.J.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 98
    • 0029101750 scopus 로고
    • Evidence for an essential serine residue in the active site of the theta class glutathione tranferases
    • P. G. Board, M. Coggan, M. C. J. Wilce, and M. W. Parker, Evidence for an essential serine residue in the active site of the theta class glutathione tranferases, Biochem. J., 311, 247-250 (1995).
    • (1995) Biochem. J. , vol.311 , pp. 247-250
    • Board, P.G.1    Coggan, M.2    Wilce, M.C.J.3    Parker, M.W.4
  • 99
    • 0028132923 scopus 로고
    • Engineering of a metal coordinating site into human glutathione transferase M1-1 based on immobilized metal ion affinity chromatography of homologous rat enzymes
    • G. Chaga, M. Widersten, L. Andersson, J. Porath, U. H. Danielson, and B. Mannervik, Engineering of a metal coordinating site into human glutathione transferase M1-1 based on immobilized metal ion affinity chromatography of homologous rat enzymes, Protein Eng., 7, 1115-1119 (1994).
    • (1994) Protein Eng. , vol.7 , pp. 1115-1119
    • Chaga, G.1    Widersten, M.2    Andersson, L.3    Porath, J.4    Danielson, U.H.5    Mannervik, B.6
  • 100
    • 0029589955 scopus 로고
    • Generation of a Ni(II) binding site by introduction of ahistidine cluster in the structure of human glutathione transferase A1-1
    • S. Yilmaz, M. Widersten, T. Emahazion, and B. Mannervik, Generation of a Ni(II) binding site by introduction of ahistidine cluster in the structure of human glutathione transferase A1-1, Protein Eng., 8, 1163-1169 (1995).
    • (1995) Protein Eng. , vol.8 , pp. 1163-1169
    • Yilmaz, S.1    Widersten, M.2    Emahazion, T.3    Mannervik, B.4
  • 101
    • 0025138395 scopus 로고
    • Construction, expression, and preliminary characterization of chimeric class μ glutathione S-transferases with altered catalytic properties
    • P. Zhang and R. N. Armstrong, Construction, expression, and preliminary characterization of chimeric class μ glutathione S-transferases with altered catalytic properties, Biopolymers, 29, 159-169 (1990).
    • (1990) Biopolymers , vol.29 , pp. 159-169
    • Zhang, P.1    Armstrong, R.N.2
  • 102
    • 0026464467 scopus 로고
    • Modular mutagenesis of exons 1, 2, and 8 of a glutathione 5′-transferase from the mu class. Mechanistic and structural consequences for chimeras of isoenzyme 3-3
    • P. Zhang, S. Liu, S. Shan, X. Ji, G. L. Gilliland, and R. N. Armstrong, Modular mutagenesis of exons 1, 2, and 8 of a glutathione 5′-transferase from the mu class. Mechanistic and structural consequences for chimeras of isoenzyme 3-3, Biochemistry, 31, 10185-10193 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10185-10193
    • Zhang, P.1    Liu, S.2    Shan, S.3    Ji, X.4    Gilliland, G.L.5    Armstrong, R.N.6
  • 103
    • 0026460365 scopus 로고
    • The three-dimensional structure of a 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
    • X. Ji, P. Zhang, R. N. Armstrong, and G. L. Gilliland, The three-dimensional structure of a 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, 31, 10169-10184 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 104
    • 0028605708 scopus 로고
    • Rational construction of the active site of a class mu glutathione S-transferase
    • S. Shan and R. N. Armstrong, Rational construction of the active site of a class mu glutathione S-transferase, J. Biol. Chem., 269, 32373-32379 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 32373-32379
    • Shan, S.1    Armstrong, R.N.2
  • 105
    • 0026513368 scopus 로고
    • Design of two chimaeric human-rat class alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties
    • R. Björnestedt, M. Widersten, P. G. Board, and B. Mannervik, Design of two chimaeric human-rat class alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties, Biochem. J., 282, 505-510 (1992).
    • (1992) Biochem. J. , vol.282 , pp. 505-510
    • Björnestedt, R.1    Widersten, M.2    Board, P.G.3    Mannervik, B.4
  • 107
    • 0029565787 scopus 로고
    • The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site
    • R. Björnestedt, S. Tardioli, and B. Mannervik, The high activity of rat glutathione transferase 8-8 with alkene substrates is dependent on a glycine residue in the active site, J. Biol. Chem., 270, 29705-29709 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 29705-29709
    • Björnestedt, R.1    Tardioli, S.2    Mannervik, B.3
  • 108
    • 0029159746 scopus 로고
    • Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme
    • A. M. Gulick and W. E. Fahl, Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme, Proc. Natl. Acad. Sci. USA, 92, 8140-8144 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8140-8144
    • Gulick, A.M.1    Fahl, W.E.2
  • 109
    • 0029008514 scopus 로고
    • Glutathione transferases with novel active sites isolated by phage display from a library of random mutants
    • M. Widersten and B. Mannervik, Glutathione transferases with novel active sites isolated by phage display from a library of random mutants, J. Molec. Biol., 250, 115-122 (1995).
    • (1995) J. Molec. Biol. , vol.250 , pp. 115-122
    • Widersten, M.1    Mannervik, B.2
  • 110
    • 0024588467 scopus 로고
    • Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase
    • G. F. Graminski, Y. Kubo, and R. N. Armstrong, Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase, Biochemistry, 28, 3562-3568 (1989).
    • (1989) Biochemistry , vol.28 , pp. 3562-3568
    • Graminski, G.F.1    Kubo, Y.2    Armstrong, R.N.3
  • 111
    • 0023857692 scopus 로고
    • Dissection of the catalytic mechanism of isozyme 4-4 of glutathione S-transferase with alternative substrates
    • W.-J. Chen, G. F. Graminski, and R. N. Armstrong, Dissection of the catalytic mechanism of isozyme 4-4 of glutathione S-transferase with alternative substrates, Biochemistry, 27, 647-654 (1988).
    • (1988) Biochemistry , vol.27 , pp. 647-654
    • Chen, W.-J.1    Graminski, G.F.2    Armstrong, R.N.3
  • 112
    • 0024403592 scopus 로고
    • Formation of the 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate anion at the active site of glutathione S-transferase: Evidence for enzymic stabilization of σ-complex intermediates in nucleophilic aromatic substitution reactions
    • G. F. Graminski, P. Zhang, M. A. Sesay, H. L. Ammon, and R. N. Armstrong. Formation of the 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate anion at the active site of glutathione S-transferase: evidence for enzymic stabilization of σ-complex intermediates in nucleophilic aromatic substitution reactions, Biochemistry, 28, 6252-6258 (1989).
    • (1989) Biochemistry , vol.28 , pp. 6252-6258
    • Graminski, G.F.1    Zhang, P.2    Sesay, M.A.3    Ammon, H.L.4    Armstrong, R.N.5
  • 113
    • 0027325607 scopus 로고
    • Peculiar spectroscopic and kinetic properties of Cys-47 in human placental glutathione transferase. Evidence for an atypical thiolate ion pair near the active site
    • M. Lo Bello, M. W. Parker, A. Desideri, F. Polticelli, M. Falconi, G. Del Boccio, A. Pennelli, G. Federici, and G. Ricci, Peculiar spectroscopic and kinetic properties of Cys-47 in human placental glutathione transferase. Evidence for an atypical thiolate ion pair near the active site, J. Biol. Chem., 268, 19033-19038 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 19033-19038
    • Lo Bello, M.1    Parker, M.W.2    Desideri, A.3    Polticelli, F.4    Falconi, M.5    Del Boccio, G.6    Pennelli, A.7    Federici, G.8    Ricci, G.9
  • 114
    • 0027359462 scopus 로고
    • Fluorescence characterization of Trp 21 in rat glutathione S-transferase 1-1: Microconformational changes induced by S-hexyl glutathione
    • R. W. Wang, A. W. Bird, D. J. Newton, A. Y. H. Lu, and W. M. Atkins, Fluorescence characterization of Trp 21 in rat glutathione S-transferase 1-1: microconformational changes induced by S-hexyl glutathione, Protein Sci., 2, 2085-2094 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 2085-2094
    • Wang, R.W.1    Bird, A.W.2    Newton, D.J.3    Lu, A.Y.H.4    Atkins, W.M.5
  • 115
    • 0021363229 scopus 로고
    • Kinetic studies and active site-binding properties of glutathione S-transferase using spin-labeled glutathione. A product analogue
    • V. L. Schramm, R. McCluskey, F. A. Emig, and G. Litwack, Kinetic studies and active site-binding properties of glutathione S-transferase using spin-labeled glutathione. a product analogue, J. Biol. Chem., 259, 714-722 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 714-722
    • Schramm, V.L.1    McCluskey, R.2    Emig, F.A.3    Litwack, G.4
  • 116
    • 0026757472 scopus 로고
    • Investigation of the active site of human placenta glutathione transferase π by means of a spin-labelled glutathione analogue
    • A. M. Caccuri, F. Polizio, F. Piemonte, P. Tagliatesta, G. Federici, and A. Desideri, Investigation of the active site of human placenta glutathione transferase π by means of a spin-labelled glutathione analogue, Biochim. Biophys. Acta, 1122, 265-268 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1122 , pp. 265-268
    • Caccuri, A.M.1    Polizio, F.2    Piemonte, F.3    Tagliatesta, P.4    Federici, G.5    Desideri, A.6
  • 117
    • 0025816329 scopus 로고
    • Electron paramagnetic resonance identification of a highly reactive thiol group in the proximity of the catalytic site of human placenta glutathione transferase
    • A. Desideri, A. M. Caccuri, F. Polizio, R. Bastoni, and G. Federici, Electron paramagnetic resonance identification of a highly reactive thiol group in the proximity of the catalytic site of human placenta glutathione transferase, J. Biol. Chem., 266, 2063-2066 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 2063-2066
    • Desideri, A.1    Caccuri, A.M.2    Polizio, F.3    Bastoni, R.4    Federici, G.5
  • 118
    • 0026654230 scopus 로고
    • Application of site-directed mutagenesis in nuclear magnetic resonance spectroscopy
    • C. J. Penington and G. S. Rule, Application of site-directed mutagenesis in nuclear magnetic resonance spectroscopy, Biophys. J., 62, 116-118 (1992).
    • (1992) Biophys. J. , vol.62 , pp. 116-118
    • Penington, C.J.1    Rule, G.S.2
  • 119
    • 0023660944 scopus 로고
    • Crystallization and a preliminary X-ray diffraction study of isozyme 3-3 of glutathione S-transferase from rat liver
    • M. A. Sesay, H. L. Ammon, and R. N. Armstrong, Crystallization and a preliminary X-ray diffraction study of isozyme 3-3 of glutathione S-transferase from rat liver, J. Mol. Biol., 197, 377-378 (1987).
    • (1987) J. Mol. Biol. , vol.197 , pp. 377-378
    • Sesay, M.A.1    Ammon, H.L.2    Armstrong, R.N.3
  • 121
    • 25944470780 scopus 로고
    • Crystals of isoenzyme 3-3 of rat liver glutathione S-transferase with and without inhibitor
    • J.-H. Fu, J. Rose, Y.-J. Chung, M. F. Tam, and B. C. Wang, Crystals of isoenzyme 3-3 of rat liver glutathione S-transferase with and without inhibitor, Acta Crystallogr., B47, 813-814 (1991).
    • (1991) Acta Crystallogr. , vol.B47 , pp. 813-814
    • Fu, J.-H.1    Rose, J.2    Chung, Y.-J.3    Tam, M.F.4    Wang, B.C.5
  • 122
    • 0024297328 scopus 로고
    • Glutathione transferase from bovine placenta. Preparation, biochemical characterization, crystallization and preliminary crystallographic analysis of a neutral class π enzyme
    • J. Schaeffer, O. Gallay, and R. Ladenstein, Glutathione transferase from bovine placenta. Preparation, biochemical characterization, crystallization and preliminary crystallographic analysis of a neutral class π enzyme, J. Biol. Chem., 263, 17405-17411 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 17405-17411
    • Schaeffer, J.1    Gallay, O.2    Ladenstein, R.3
  • 123
    • 0025369904 scopus 로고
    • Crystallization of glutathione S-transferase from human placenta
    • M. W. Parker, M. Lo Bello, and G. Federici, Crystallization of glutathione S-transferase from human placenta, J. Molec. Biol., 213, 221-222 (1990).
    • (1990) J. Molec. Biol. , vol.213 , pp. 221-222
    • Parker, M.W.1    Lo Bello, M.2    Federici, G.3
  • 124
    • 0029064985 scopus 로고
    • Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods
    • X. Ji, E. C. Von Rosenvinge, W. W. Johnson, S. I. Tomarev, J. Piatigorsky, R. N. Armstrong, and G. L. Gilliland, 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 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5317-5328
    • Ji, X.1    Von Rosenvinge, E.C.2    Johnson, W.W.3    Tomarev, S.I.4    Piatigorsky, J.5    Armstrong, R.N.6    Gilliland, G.L.7
  • 125
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function
    • H. Dirr, P. Reinemer, and R. Huber, X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function, Eur. J. Biochem., 220, 645-661 (1994).
    • (1994) Eur. J. Biochem. , vol.220 , pp. 645-661
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 126
    • 0030831220 scopus 로고    scopus 로고
    • Modeling the active sites of cytochrome P450s and glutathione S-transferases, two of the most important biotransformation enzymes
    • M. J. De Groot and N. P. E. Vermeulen, Modeling the active sites of cytochrome P450s and glutathione S-transferases, two of the most important biotransformation enzymes, Drug Met. Rev., 29(3), 747-799 (1997).
    • (1997) Drug Met. Rev. , vol.29 , Issue.3 , pp. 747-799
    • De Groot, M.J.1    Vermeulen, N.P.E.2
  • 127
    • 0029645124 scopus 로고
    • Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complex with ethacrynic acid and its glutathione conjugate
    • A. D. Cameron, I. Sinning, G. L'Hermite, B. Olin, P. G. Board, B. Mannervik, and T. A. Jones, Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complex with ethacrynic acid and its glutathione conjugate, Structure, 3, 717-727 (1995).
    • (1995) Structure , vol.3 , pp. 717-727
    • Cameron, A.D.1    Sinning, I.2    L'Hermite, G.3    Olin, B.4    Board, P.G.5    Mannervik, B.6    Jones, T.A.7
  • 128
    • 0027945373 scopus 로고
    • A surface mutant (G82R) of a human α-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal
    • K. Zeng, J. P. Rose, H.-C. Chen, C. L. Strickland, C.-P. D. Tu, and B.-C. Wang, A surface mutant (G82R) of a human α-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal, Protein-Struct. Funct. Genet., 20, 259-263 (1994).
    • (1994) Protein-Struct. Funct. Genet. , vol.20 , pp. 259-263
    • Zeng, K.1    Rose, J.P.2    Chen, H.-C.3    Strickland, C.L.4    Tu, C.-P.D.5    Wang, B.-C.6
  • 129
    • 0344220377 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of chicken-liver glutathione S-transferase CL 3-3
    • S.-C. Lin, H.-H. Yu, L.-F. Liu, J.-Y. Lee, A. Huang, M. F. Tam, and Y.-C. Liaw, Crystallization and preliminary X-ray analysis of chicken-liver glutathione S-transferase CL 3-3, Acta Crystallogr., D52, 601-603 (1996).
    • (1996) Acta Crystallogr. , vol.D52 , pp. 601-603
    • Lin, S.-C.1    Yu, H.-H.2    Liu, L.-F.3    Lee, J.-Y.4    Huang, A.5    Tam, M.F.6    Liaw, Y.-C.7
  • 130
    • 0028218381 scopus 로고
    • Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene
    • X. Ji, W. W. Johnson, M. A. Sesay, L. Dickert, S. M. Prasad, H. L. Ammon, R. N. Armstrong, and G. L. Gilliland, Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene, Biochemistry, 33, 1043-1052 (1994).
    • (1994) Biochemistry , vol.33 , pp. 1043-1052
    • Ji, X.1    Johnson, W.W.2    Sesay, M.A.3    Dickert, L.4    Prasad, S.M.5    Ammon, H.L.6    Armstrong, R.N.7    Gilliland, G.L.8
  • 131
    • 0028154194 scopus 로고
    • New crystal forms of a μ-class glutathione S-transferase from rat liver
    • J.-H. Fu and J. Rose, New crystal forms of a μ-class glutathione S-transferase from rat liver, Acta Crystallogr., D50, 219-224 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 219-224
    • Fu, J.-H.1    Rose, J.2
  • 132
    • 0028244183 scopus 로고
    • Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity
    • S. Raghunathan, R. J. Chandross, R. H. Kretsinger, T. J. Allison, C. J. Penington, and G. S. Rule, Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity, J. Molec. Biol., 238, 815-832 (1994).
    • (1994) J. Molec. Biol. , vol.238 , pp. 815-832
    • Raghunathan, S.1    Chandross, R.J.2    Kretsinger, R.H.3    Allison, T.J.4    Penington, C.J.5    Rule, G.S.6
  • 133
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV
    • K. Lim, J. X. Ho, K. Keeling, G. L. Gilliland, X. Ji, F. Rüker, and D. C. Carter, Three-dimensional structure of Schistoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV, Protein Sci., 3. 2233-2244 (1994).
    • (1994) Protein Sci. , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.X.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.5    Rüker, F.6    Carter, D.C.7
  • 134
    • 0028931691 scopus 로고
    • Crystal structures of a Schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
    • M. A. McTigue, D. R. Williams, and J. A. Tainer, Crystal structures of a Schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel, J. Molec. Biol., 246, 21-27 (1995).
    • (1995) J. Molec. Biol. , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 136
    • 0028258793 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a glutathione S-transferase from the Australian sheep blowfly. Lucilia cuprina
    • M. C. J. Wilce, S. C. Feil, P. G. Board, and M. W. Parker, Crystallization and preliminary X-ray diffraction studies of a glutathione S-transferase from the Australian sheep blowfly. Lucilia cuprina, J. Molec. Biol., 236, 1407-1409 (1994).
    • (1994) J. Molec. Biol. , vol.236 , pp. 1407-1409
    • Wilce, M.C.J.1    Feil, S.C.2    Board, P.G.3    Parker, M.W.4
  • 137
    • 0029914965 scopus 로고    scopus 로고
    • Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 Å resolution: Structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture
    • P. Reinemer, L. Prade, P. Hof, T. Neuefeind, R. Huber, R. Zettl, K. Palme, J. Schell, I. Koelln, H. D. Bartunik, and B. Bieseler, Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 Å resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture, J. Molec. Biol., 255, 289-309 (1996).
    • (1996) J. Molec. Biol. , vol.255 , pp. 289-309
    • Reinemer, P.1    Prade, L.2    Hof, P.3    Neuefeind, T.4    Huber, R.5    Zettl, R.6    Palme, K.7    Schell, J.8    Koelln, I.9    Bartunik, H.D.10    Bieseler, B.11
  • 141
    • 0021103450 scopus 로고
    • Stereoselectivity of isoenzyme C of glutathione S-transferase toward arene and azaarene oxides
    • D. Cobb, C. Boehlert, D. Lewis, and R. N. Armstrong, Stereoselectivity of isoenzyme C of glutathione S-transferase toward arene and azaarene oxides, Biochemistry, 22, 805-812 (1983).
    • (1983) Biochemistry , vol.22 , pp. 805-812
    • Cobb, D.1    Boehlert, C.2    Lewis, D.3    Armstrong, R.N.4
  • 142
    • 0022551157 scopus 로고
    • Cytosolic glutathione S-transferases in various rat tissues differ in stereoselectivity with polycyclic arene and alkene oxide substrates
    • L. A. Dostal, A. Aitio, C. Harris, A. V. Bhatia, O. Hernandez, and J. R. Bend, Cytosolic glutathione S-transferases in various rat tissues differ in stereoselectivity with polycyclic arene and alkene oxide substrates, Drug Metab. Disp., 14, 303-309 (1986).
    • (1986) Drug Metab. Disp. , vol.14 , pp. 303-309
    • Dostal, L.A.1    Aitio, A.2    Harris, C.3    Bhatia, A.V.4    Hernandez, O.5    Bend, J.R.6
  • 144
    • 0022991461 scopus 로고
    • Glutathione transferases in rat lung: The presence of transferase 7-7, highly efficient in the conjugation of glutathione with the carcinogenic (+)-7β8α-dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo[a] pyrene
    • I. G. C. Robertson, H. Jensson, B. Mannervik, and B. Jernström, Glutathione transferases in rat lung: the presence of transferase 7-7, highly efficient in the conjugation of glutathione with the carcinogenic (+)-7β8α-dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo[a] pyrene. Carcinogenesis, 7, 295-299 (1986).
    • (1986) Carcinogenesis , vol.7 , pp. 295-299
    • Robertson, I.G.C.1    Jensson, H.2    Mannervik, B.3    Jernström, B.4
  • 145
    • 0022796435 scopus 로고
    • The enzymatic conjugation of glutathione with bay-region diol-epoxides of benzo[a]pyrene, benzo[a]anthracene and chrysene
    • I. G. C. Robertson and B. Jernström. The enzymatic conjugation of glutathione with bay-region diol-epoxides of benzo[a]pyrene, benzo[a]anthracene and chrysene, Carcinogenesis, 7, 1633-1636 (1986).
    • (1986) Carcinogenesis , vol.7 , pp. 1633-1636
    • Robertson, I.G.C.1    Jernström, B.2
  • 147
    • 0343173024 scopus 로고    scopus 로고
    • GST-targeted drug candidates
    • (N. P. E. Vermeulen, G. J. Mulder, H. Nieuwenhuyse, W. H. M. Peters, and P. J. van Bladeren, eds.), Taylor & Francis, London
    • L. M. Kauvar, GST-targeted drug candidates, in Glutathione S-transferases. Structure, Function and Clinical Applications (N. P. E. Vermeulen, G. J. Mulder, H. Nieuwenhuyse, W. H. M. Peters, and P. J. van Bladeren, eds.), Taylor & Francis, London, 1996, pp. 187-197.
    • (1996) Glutathione S-transferases. Structure, Function and Clinical Applications , pp. 187-197
    • Kauvar, L.M.1
  • 148
    • 0030057817 scopus 로고    scopus 로고
    • Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor cosubstrate on dynamics and kinetics of human glutathione transferase
    • A. M. Caccuri, P. Ascenzi, G. Antonini, M. W. Parker, A. J. Oakley, E. Chiessi, M. Nuccetelli, A. Battistoni, A. Bellizia, and G. Ricci, Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor cosubstrate on dynamics and kinetics of human glutathione transferase, J. Biol. Chem., 271, 16193-16198 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 16193-16198
    • Caccuri, A.M.1    Ascenzi, P.2    Antonini, G.3    Parker, M.W.4    Oakley, A.J.5    Chiessi, E.6    Nuccetelli, M.7    Battistoni, A.8    Bellizia, A.9    Ricci, G.10
  • 149
    • 0028051238 scopus 로고
    • Novel procedure for structure refinement in homology modeling and its application to the human class mu glutathione S-transferases
    • R. E. Cachau, J. W. Erickson, and H. O. Villar, Novel procedure for structure refinement in homology modeling and its application to the human class mu glutathione S-transferases, Protein Eng., 7, 831-839 (1994).
    • (1994) Protein Eng. , vol.7 , pp. 831-839
    • Cachau, R.E.1    Erickson, J.W.2    Villar, H.O.3
  • 150
    • 0028875690 scopus 로고
    • Amino acid sequencing, molecular cloning and modelling of the chick liver class-Theta glutathione S-transferase CL1
    • C.-D. Hsiao, E. O. Martsen, J.-Y., Lee, and M. F. Tam, Amino acid sequencing, molecular cloning and modelling of the chick liver class-Theta glutathione S-transferase CL1, Biochem. J., 312, 91-98 (1995).
    • (1995) Biochem. J. , vol.312 , pp. 91-98
    • Hsiao, C.-D.1    Martsen, E.O.2    Lee, J.-Y.3    Tam, M.F.4
  • 151
    • 0029009158 scopus 로고
    • Structural investigation of a glutathione binding site using computational analysis
    • T. R. Barry, P. Waters, S. Doonan, and D. Sheehan, Structural investigation of a glutathione binding site using computational analysis, Biochem. Soc. Trans., 23, 382S (1995).
    • (1995) Biochem. Soc. Trans. , vol.23
    • Barry, T.R.1    Waters, P.2    Doonan, S.3    Sheehan, D.4
  • 152
    • 0028925025 scopus 로고
    • Structural and functional properties of the 34-kDa fragment produced by the N-terminal chymotryptic cleavage of glutathione transferase P1-1
    • A. Aceto, P. Sacchetta, T. Bucciarelli, B. Dragani, S. Angelucci, G. L. Radatti, and C. Di Ilio, Structural and functional properties of the 34-kDa fragment produced by the N-terminal chymotryptic cleavage of glutathione transferase P1-1, Arch. Biochem. Biophys., 316, 873-878 (1995).
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 873-878
    • Aceto, A.1    Sacchetta, P.2    Bucciarelli, T.3    Dragani, B.4    Angelucci, S.5    Radatti, G.L.6    Di Ilio, C.7
  • 153
    • 0016821982 scopus 로고
    • Purification and characterization of two glutathione S-aryltransferase activities from rat liver
    • P. Askelöf, C. Guthenberg, I. Jakobson, and B. Mannervik, Purification and characterization of two glutathione S-aryltransferase activities from rat liver, Biochem. J., 147, 513 (1975).
    • (1975) Biochem. J. , vol.147 , pp. 513
    • Askelöf, P.1    Guthenberg, C.2    Jakobson, I.3    Mannervik, B.4
  • 154
    • 0023445343 scopus 로고
    • Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases
    • U. H. Danielson, H. Esterbauer, and B. Mannervik, Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases, Biochem. J., 247, 707-713 (1987).
    • (1987) Biochem. J. , vol.247 , pp. 707-713
    • Danielson, U.H.1    Esterbauer, H.2    Mannervik, B.3
  • 155
    • 0028892567 scopus 로고
    • Isothiocyanates as substrates for human glutathione transferases: Structure-activity studies
    • R. H. Kolm, U. H. Danielson, Y. Zhang, P. Talalay, and B. Mannervik, Isothiocyanates as substrates for human glutathione transferases: structure-activity studies, Biochem. J., 311, 453-459 (1995).
    • (1995) Biochem. J. , vol.311 , pp. 453-459
    • Kolm, R.H.1    Danielson, U.H.2    Zhang, Y.3    Talalay, P.4    Mannervik, B.5
  • 156
    • 0026788043 scopus 로고
    • Stereoselective conjugation of 2-bromocarboxylic acids and their urea derivatives by rat liver glutathione transferase 12-12 and some other isoforms
    • M. Polhuijs, G. J. Mulder, D. J. Meyer, and B. Ketterer, Stereoselective conjugation of 2-bromocarboxylic acids and their urea derivatives by rat liver glutathione transferase 12-12 and some other isoforms, Biochem. Pharmacol., 44, 1249-1253 (1992).
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1249-1253
    • Polhuijs, M.1    Mulder, G.J.2    Meyer, D.J.3    Ketterer, B.4
  • 157
    • 0027521246 scopus 로고
    • Stereoselectivity of human liver and intestinal cytosolic fractions as well as purified human glutathione S-transferase isoenzymes towards 2-bromoisovalerylurea enantiomers
    • T. M. T. Mulders, B. Van Ommen, P. J. Van Bladeren, D. D. Breimer, and G. I. Mulder, Stereoselectivity of human liver and intestinal cytosolic fractions as well as purified human glutathione S-transferase isoenzymes towards 2-bromoisovalerylurea enantiomers, Biochem. Pharmacol., 46, 1775-1780 (1993).
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1775-1780
    • Mulders, T.M.T.1    Van Ommen, B.2    Van Bladeren, P.J.3    Breimer, D.D.4    Mulder, G.I.5
  • 158
    • 0024421029 scopus 로고
    • Irreversible inhibition of rat hepatic glutathione S-transferase isoenzymes by a series of structurally related quinones
    • R. M. E. Vos, B. Van Ommen, M. S. J. Hoekstein, J. H. M. De Goede, and P. J. Van Bladeren, Irreversible inhibition of rat hepatic glutathione S-transferase isoenzymes by a series of structurally related quinones, Chem.-Biol. Interact., 71, 381-392 (1989).
    • (1989) Chem.-Biol. Interact. , vol.71 , pp. 381-392
    • Vos, R.M.E.1    Van Ommen, B.2    Hoekstein, M.S.J.3    De Goede, J.H.M.4    Van Bladeren, P.J.5
  • 159
    • 0025731332 scopus 로고
    • Irreversible inhibition of rat glutathione S-transferase 1-1 by quinones and their glutathione conjugates
    • B. Van Ommen, J. H. T. M. Ploemen, J. J. P. Bogaards, T. J. Monks, S. S. Lau, and P. J. Van Bladeren, Irreversible inhibition of rat glutathione S-transferase 1-1 by quinones and their glutathione conjugates, Biochem. J., 276, 661-666 (1991).
    • (1991) Biochem. J. , vol.276 , pp. 661-666
    • Van Ommen, B.1    Ploemen, J.H.T.M.2    Bogaards, J.J.P.3    Monks, T.J.4    Lau, S.S.5    Van Bladeren, P.J.6
  • 160
    • 0022368012 scopus 로고
    • Synthesis and characterization of the oxygen and desthio analogues of glutathione as dead-end inhibitors of glutathione S-transferase
    • W.-J. Chen, C. C. Boehlert, K. Rider, and R. N. Armstrong, Synthesis and characterization of the oxygen and desthio analogues of glutathione as dead-end inhibitors of glutathione S-transferase, Biochem. Biophys. Res. Commun., 128, 233-240 (1985).
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 233-240
    • Chen, W.-J.1    Boehlert, C.C.2    Rider, K.3    Armstrong, R.N.4
  • 161
    • 0023687171 scopus 로고
    • Substrate specificity of rat liver glutathione S-transferase isoenzymes for a series of glutathione analogues, modified at the γ-glutamyl moiety
    • A. E. P. Adang, J. Brussee, D. J. Meyer, B. Coles, B. Ketterer, A. Van der Gen, and G. J. Mulder, Substrate specificity of rat liver glutathione S-transferase isoenzymes for a series of glutathione analogues, modified at the γ-glutamyl moiety, Biochem. J., 255, 721-724 (1988).
    • (1988) Biochem. J. , vol.255 , pp. 721-724
    • Adang, A.E.P.1    Brussee, J.2    Meyer, D.J.3    Coles, B.4    Ketterer, B.5    Van Der Gen, A.6    Mulder, G.J.7
  • 162
    • 0025340142 scopus 로고
    • The glutathione binding site in glutathione S-transferases: Investigation of the cysteinyl, glycyl and γ-glutamyl domains
    • A. E. P. Adang, J. Brussee, A. Van der Gen, and G. J. Mulder, The glutathione binding site in glutathione S-transferases: investigation of the cysteinyl, glycyl and γ-glutamyl domains, Biochem. J., 269, 47-54 (1990).
    • (1990) Biochem. J. , vol.269 , pp. 47-54
    • Adang, A.E.P.1    Brussee, J.2    Van Der Gen, A.3    Mulder, G.J.4
  • 163
    • 0017105696 scopus 로고
    • Mechanism for the several activities of the glutathione S-transferases
    • J. H. Keen, W. H. Habig, and W. B. Jakoby, Mechanism for the several activities of the glutathione S-transferases, J. Biol. Chem., 251, 6183-6188 (1976).
    • (1976) J. Biol. Chem. , vol.251 , pp. 6183-6188
    • Keen, J.H.1    Habig, W.H.2    Jakoby, W.B.3
  • 164
    • 0002595845 scopus 로고
    • (C. Eaborn and N. B. Chapman, eds.), Elsevier, New York
    • J. Miller, Reaction Mechanisms in Organic Chemistry (C. Eaborn and N. B. Chapman, eds.), Vol. 8, Elsevier, New York, 1968, pp. 137-179.
    • (1968) Reaction Mechanisms in Organic Chemistry , vol.8 , pp. 137-179
    • Miller, J.1
  • 165
    • 0029001803 scopus 로고
    • Quantitative structure-activity relationships based on computer calculated parameters for the overall rate of glutathione S-transferase catalyzed conjugation of a series of fluoronitrobenzenes
    • I. M. C. M. Rietjens, A. E. M. F. Soffers, G. J. E. J. Hooiveld, C. Veeger, and J. Vervoort, Quantitative structure-activity relationships based on computer calculated parameters for the overall rate of glutathione S-transferase catalyzed conjugation of a series of fluoronitrobenzenes, Chem. Res. Toxicol., 8, 481-488 (1995).
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 481-488
    • Rietjens, I.M.C.M.1    Soffers, A.E.M.F.2    Hooiveld, G.J.E.J.3    Veeger, C.4    Vervoort, J.5
  • 166
    • 0029924063 scopus 로고    scopus 로고
    • Regioselectivity and quantitative structure-activity relationships for the conjugation of a series of fluoronitrobenzenes by purified glutathione S-transferase enzymes from rat and man
    • A. E. M. F. Soffers, J. H. T. M. Ploemen, M. J. H. Moonen, T. Wobbes, B. Van Ommen, J. Vervoort, P. J. Van Bladeren, and I. M. C. M. Rietjens, Regioselectivity and quantitative structure-activity relationships for the conjugation of a series of fluoronitrobenzenes by purified glutathione S-transferase enzymes from rat and man, Chem. Res. Toxicol., 9, 638-646 (1996).
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 638-646
    • Soffers, A.E.M.F.1    Ploemen, J.H.T.M.2    Moonen, M.J.H.3    Wobbes, T.4    Van Ommen, B.5    Vervoort, J.6    Van Bladeren, P.J.7    Rietjens, I.M.C.M.8
  • 167
    • 0029876262 scopus 로고    scopus 로고
    • Structure-activity relationships for the glutathione conjugation of 2-substituted 1-chloro-4-nitrobenzenes by rat glutathione S-transferase 4-4
    • E. M. Van der Aar, M. J. De Groot, G. J. Bijloo, H. Van der Goot, and N. P. E. Vermeulen, Structure-activity relationships for the glutathione conjugation of 2-substituted 1-chloro-4-nitrobenzenes by rat glutathione S-transferase 4-4, Chem. Res. Toxicol., 9, 527-534 (1996).
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 527-534
    • Van Der Aar, E.M.1    De Groot, M.J.2    Bijloo, G.J.3    Van Der Goot, H.4    Vermeulen, N.P.E.5
  • 168
    • 0029853943 scopus 로고    scopus 로고
    • Structure-activity relationships for chemical and glutathione S-transferase-catalyzed glutathione conjugation reactions of a series of 2-substituted 1-chloro-4-nitrobenzenes
    • E. M. Van der Aar, T. Bouwman, J. N. M. Commandeur, and N. P. E. Vermeulen, Structure-activity relationships for chemical and glutathione S-transferase-catalyzed glutathione conjugation reactions of a series of 2-substituted 1-chloro-4-nitrobenzenes, Biochem. J., 320, 531-540 (1996).
    • (1996) Biochem. J. , vol.320 , pp. 531-540
    • Van Der Aar, E.M.1    Bouwman, T.2    Commandeur, J.N.M.3    Vermeulen, N.P.E.4
  • 169
    • 0024334728 scopus 로고
    • Observation of a substituent effect on the stereoselectivity of glutathione S-transferases toward para-substituted 4-phenyl-3-buten-2-ones
    • Y. Kubo and R. N. Armstrong, Observation of a substituent effect on the stereoselectivity of glutathione S-transferases toward para-substituted 4-phenyl-3-buten-2-ones, Chem. Res. Toxicol., 2, 144-145 (1989).
    • (1989) Chem. Res. Toxicol. , vol.2 , pp. 144-145
    • Kubo, Y.1    Armstrong, R.N.2


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