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Volumn 43, Issue 2, 2011, Pages 138-151

Glutathione transferases: A structural perspective

Author keywords

catalytic mechanism; function; Glutathione transferase; GST; structure

Indexed keywords

ANTINEOPLASTIC AGENT; CHLORAMBUCIL; ENZYME INHIBITOR; GAMMA GLUTAMYL (S BENZYL)CYSTEINYL DEXTRO PHENYLGLYCINE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; LEUKOTRIENE; LIGANDIN; MEMBRANE PROTEIN; PEROXIDE; STEROID; TLK 117; TYROSINE; UNCLASSIFIED DRUG;

EID: 79954572279     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.3109/03602532.2011.558093     Document Type: Review
Times cited : (301)

References (81)
  • 2
    • 34547631962 scopus 로고    scopus 로고
    • Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis
    • DOI 10.1038/nature05936, PII NATURE05936
    • Ago, H., Kanaoka, Y., Irikura, D., Lam, B. K., Shimamura, T., Austen, K. F., et al. (2007). Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature 448:609-612. (Pubitemid 47206929)
    • (2007) Nature , vol.448 , Issue.7153 , pp. 609-612
    • Ago, H.1    Kanaoka, Y.2    Irikura, D.3    Lam, B.K.4    Shimamura, T.5    Austen, K.F.6    Miyano, M.7
  • 3
    • 0034667663 scopus 로고    scopus 로고
    • Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases
    • Allocati, N., Casalone, E., Masulli, M., Polekhina, G., Rossjohn, J., Parker, M. W., et al. (2000). Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases. Biochem J 351(Pt 2):341-346.
    • (2000) Biochem J , vol.351 , Issue.PART 2 , pp. 341-346
    • Allocati, N.1    Casalone, E.2    Masulli, M.3    Polekhina, G.4    Rossjohn, J.5    Parker, M.W.6
  • 5
    • 72749095187 scopus 로고    scopus 로고
    • Glutathione transferases are structural and functional outliers in the thioredoxin fold
    • Atkinson, H. J., Babbitt, P. C. (2009). Glutathione transferases are structural and functional outliers in the thioredoxin fold. Biochemistry 48:11108-11116.
    • (2009) Biochemistry , vol.48 , pp. 11108-11116
    • Atkinson, H.J.1    Babbitt, P.C.2
  • 6
    • 77449135890 scopus 로고    scopus 로고
    • Substrate specifcity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal
    • Balogh, L. M., Le Trong, I., Kripps, K. A., Shireman, L. M., Stenkamp, R. E., Zhang, W., et al. (2010). Substrate specifcity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal. Biochemistry 49:1541-1548.
    • (2010) Biochemistry , vol.49 , pp. 1541-1548
    • Balogh, L.M.1    Le Trong, I.2    Kripps, K.A.3    Shireman, L.M.4    Stenkamp, R.E.5    Zhang, W.6
  • 8
    • 0141679076 scopus 로고    scopus 로고
    • Clarification of the role of key active site residues of glutathione transferase Zeta/maleylacetoacetate isomerase by a new spectrophotometric technique
    • DOI 10.1042/BJ20030625
    • Board, P. G., Taylor, M. C., Coggan, M., Parker, M. W., Lantum, H. B., Anders, M. W. (2003). Clarifcation of the role of key active site residues of glutathionetransferase zeta/maleylacetoacetate isomerase by a new spectrophotometric technique. Biochem J 374:731-737. (Pubitemid 37163918)
    • (2003) Biochemical Journal , vol.374 , Issue.3 , pp. 731-737
    • Board, P.G.1    Taylor, M.C.2    Coggan, M.3    Parker, M.W.4    Lantum, H.B.5    Anders, M.W.6
  • 9
    • 0021772873 scopus 로고
    • Investigation of the kinetic and stereochemical recognition of arene and azaarene oxides by isozymes A2 and C2 of glutathione S-transferase
    • Boehlert, C. C., Armstrong, R. N. (1984). Investigation of the kinetic and stereochemical recognition of arene and azaarene oxides by isozymes A2 and C2 of glutathione S-transferase. Biochem Biophys Res Commun 121:980-986.
    • (1984) Biochem Biophys Res Commun , vol.121 , pp. 980-986
    • Boehlert, C.C.1    Armstrong, R.N.2
  • 10
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • DOI 10.1016/S0969-2126(00)00553-0, PII S0969212600005530
    • Bousset, L., Belrhali, H., Janin, J., Melki, R., Morera, S. (2001). Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9:39-46. (Pubitemid 32064348)
    • (2001) Structure , vol.9 , Issue.1 , pp. 39-46
    • Bousset, L.1    Belrhali, H.2    Janin, J.3    Melki, R.4    Morera, S.5
  • 11
    • 0033531970 scopus 로고    scopus 로고
    • Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products
    • DOI 10.1006/jmbi.1999.2697
    • Bruns, C. M., Hubatsch, I., Ridderstrom, M., Mannervik, B., Tainer, J. A. (1999). Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efciency with toxic lipid peroxidation products. J Mol Biol 288:427-439. (Pubitemid 29221812)
    • (1999) Journal of Molecular Biology , vol.288 , Issue.3 , pp. 427-439
    • Bruns, C.M.1    Hubatsch, I.2    Ridderstrom, M.3    Mannervik, B.4    Tainer, J.A.5
  • 12
    • 0029645124 scopus 로고
    • Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate
    • Cameron, A. D., Sinning, I., L'Hermite, G., Olin, B., Board, P. G., Mannervik, B., et al. (1995). Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure 3:717-727.
    • (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
  • 16
    • 10844293503 scopus 로고    scopus 로고
    • Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity
    • DOI 10.1021/bi048757g
    • Gu, Y., Guo, J., Pal, A., Pan, S. S., Zimniak, P., Singh, S. V., et al. (2004). Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity. Biochemistry 43:15673-15679. (Pubitemid 39665067)
    • (2004) Biochemistry , vol.43 , Issue.50 , pp. 15673-15679
    • Gu, Y.1    Guo, J.2    Pal, A.3    Pan, S.-S.4    Zimniak, P.5    Singh, S.V.6    Ji, X.7
  • 17
    • 0034680363 scopus 로고    scopus 로고
    • Residue R216 and catalytic efciency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R) 8(S)-diol 9(S) 10(R)-epoxide
    • Gu, Y., Singh, S. V., Ji, X. (2000). Residue R216 and catalytic efciency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide. Biochemistry 39:12552-12557.
    • (2000) Biochemistry , vol.39 , pp. 12552-12557
    • Gu, Y.1    Singh, S.V.2    Ji, X.3
  • 18
    • 0037417766 scopus 로고    scopus 로고
    • Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide
    • DOI 10.1021/bi026778+
    • Gu, Y., Xiao, B., Wargo, H. L., Bucher, M. H., Singh, S. V., Ji, X. (2003). Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide. Biochemistry 42:917-921. (Pubitemid 36159523)
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 917-921
    • Gu, Y.1    Xiao, B.2    Wargo, H.L.3    Bucher, M.H.4    Singh, S.V.5    Ji, X.6
  • 20
    • 20444476586 scopus 로고    scopus 로고
    • Structural basis for the function of stringent starvation protein A as a transcription factor
    • DOI 10.1074/jbc.M501444200
    • Hansen, A. M., Gu, Y., Li, M., Andrykovitch, M., Waugh, D. S., Jin, D. J., et al. (2005). Structural basis for the function of stringent starvation protein a as a transcription factor. J Biol Chem 280:17380-17391. (Pubitemid 41389208)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17380-17391
    • Hansen, A.-M.1    Gu, Y.2    Li, M.3    Andrykovitch, M.4    Waugh, D.S.5    Jin, D.J.6    Ji, X.7
  • 21
    • 0035976922 scopus 로고    scopus 로고
    • Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution
    • Harrop, S. J., DeMaere, M. Z., Fairlie, W. D., Reztsova, T., Valenzuela, S. M., Mazzanti, M., et al. (2001). Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution. J Biol Chem 276:44993-45000.
    • (2001) J Biol Chem , vol.276 , pp. 44993-45000
    • Harrop, S.J.1    Demaere, M.Z.2    Fairlie, W.D.3    Reztsova, T.4    Valenzuela, S.M.5    Mazzanti, M.6
  • 26
    • 0033011878 scopus 로고    scopus 로고
    • Common structural features of MAPEG - A widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
    • Jakobsson, P. J., Morgenstern, R., Mancini, J., Ford-Hutchinson, A., Persson, B. (1999a). Common structural features of MAPEG-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Prot Sci 8:689-692. (Pubitemid 29117984)
    • (1999) Protein Science , vol.8 , Issue.3 , pp. 689-692
    • Jakobsson, P.-J.1    Morgenstern, R.2    Mancini, J.3    Ford-Hutchinson, A.4    Persson, B.5
  • 28
    • 0345306580 scopus 로고    scopus 로고
    • The Crystal Structure of the Glutathione S-Transferase-like Domain of Elongation Factor 1Bγ from Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M306630200
    • Jeppesen, M. G., Ortiz, P., Shepard, W., Kinzy, T. G., Nyborg, J., Andersen, G. R. (2003). The crystal structure of the glutathione S-transferase-like domain of elongation factor 1B gamma from Saccharomyces cerevisiae. J Biol Chem 278:47190-47198. (Pubitemid 37452305)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47190-47198
    • Jeppesen, M.G.1    Ortiz, P.2    Shepard, W.3    Kinzy, T.G.4    Nyborg, J.5    Andersen, G.R.6
  • 29
    • 0027788045 scopus 로고
    • Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase
    • Ji, X., Armstrong, R. N., Gilliland, G. L. (1993). Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase. Biochemistry 32:12949-12954. (Pubitemid 2020112)
    • (1993) Biochemistry , vol.32 , Issue.48 , pp. 12949-12954
    • Ji Xinhua1    Armstrong, R.N.2    Gilliland, G.L.3
  • 30
    • 0033543218 scopus 로고    scopus 로고
    • Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1
    • Ji, X., Blaszczyk, J., Xiao, B., O'Donnell, R., Hu, X., Herzog, C., et al. (1999). Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1. Biochemistry 38:10231-10238.
    • (1999) Biochemistry , vol.38 , pp. 10231-10238
    • Ji, X.1    Blaszczyk, J.2    Xiao, B.3    O'Donnell, R.4    Hu, X.5    Herzog, C.6
  • 31
    • 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
    • Ji, X., Johnson, W. W., Sesay, M. A., Dickert, L., Prasad, S. M., Ammon, H. L., et al. (1994). 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. (Pubitemid 24072432)
    • (1994) Biochemistry , vol.33 , Issue.5 , 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
  • 32
    • 0030748102 scopus 로고    scopus 로고
    • Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class π glutathione S-transferase
    • DOI 10.1021/bi970805s
    • Ji, X., Tordova, M., O'Donnell, R., Parsons, J. F., Hayden, J. B., Gilliland, G. L., et al. (1997). Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry 36:9690-9702. (Pubitemid 27364680)
    • (1997) Biochemistry , vol.36 , Issue.32 , pp. 9690-9702
    • Ji, X.1    Tordova, M.2    O'Donnell, R.3    Parsons, J.F.4    Hayden, J.B.5    Gilliland, G.L.6    Zimniak, P.7
  • 34
    • 0029064985 scopus 로고
    • Tree-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods
    • Ji, X., von Rosenvinge, E. C., Johnson, W. W., Tomarev, S. I., Piatigorsky, J., Armstrong, R. N., et al. (1995). Tree-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) 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
  • 35
    • 0035980083 scopus 로고    scopus 로고
    • Human glutathione transferase A3-3, a highly efcient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones
    • Johansson, A. S., Mannervik, B. (2001). Human glutathione transferase A3-3, a highly efcient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J Biol Chem 276:33061-33065.
    • (2001) J Biol Chem , vol.276 , pp. 33061-33065
    • Johansson, A.S.1    Mannervik, B.2
  • 37
    • 0026529977 scopus 로고
    • Tyrosine-7 is an essential residue for the catalytic activity of human class pi glutathione-S-transferase-chemical modifcation and site-directed mutagenesis studies
    • Kong, K. H., Nishida, M., Inoue, H., Takahashi, K. (1992a). Tyrosine-7 is an essential residue for the catalytic activity of human class pi glutathione-S-transferase-chemical modifcation and site-directed mutagenesis studies. Biochem Biophys Res Commun 182:1122-1129.
    • (1992) Biochem Biophys Res Commun , vol.182 , pp. 1122-1129
    • Kong, K.H.1    Nishida, M.2    Inoue, H.3    Takahashi, K.4
  • 38
    • 0026624869 scopus 로고
    • Tyrosine-7 in human class-pi glutathione-S-transferase is important for lowering the pKa of the thiol-group of glutathione in the enzyme-glutathione complex
    • Kong, K. H., Takasu, K., Inoue, H., Takahashi, K. (1992b). Tyrosine-7 in human class-pi glutathione-S-transferase is important for lowering the pKa of the thiol-group of glutathione in the enzyme-glutathione complex. Biochem Biophys Res Commun 184:194-197.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 194-197
    • Kong, K.H.1    Takasu, K.2    Inoue, H.3    Takahashi, K.4
  • 39
    • 77955713764 scopus 로고    scopus 로고
    • Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death
    • Laborde, E. (2010). Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death. Cell Death Difer 17:1373-1380.
    • (2010) Cell Death Difer , vol.17 , pp. 1373-1380
    • Laborde, E.1
  • 40
    • 0345832239 scopus 로고    scopus 로고
    • Parallel Evolutionary Pathways for Glutathione Transferases: Structure and Mechanism of the Mitochondrial Class Kappa Enzyme rGSTK1-1
    • DOI 10.1021/bi035832z
    • Ladner, J. E., Parsons, J. F., Rife, C. L., Gilliland, G. L., Armstrong, R. N. (2004). Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry 43:352-361. (Pubitemid 38082557)
    • (2004) Biochemistry , vol.43 , Issue.2 , pp. 352-361
    • Ladner, J.E.1    Parsons, J.F.2    Rife, C.L.3    Gilliland, G.L.4    Armstrong, R.N.5
  • 41
    • 24344480389 scopus 로고    scopus 로고
    • Thioredoxin-like domain of human κ class glutathione transferase reveals sequence homology and structure similarity to the θ class enzyme
    • DOI 10.1110/ps.051463905
    • Li, J., Xia, Z., Ding, J. (2005). Tioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme. Prot Sci 14:2361-2369. (Pubitemid 41252805)
    • (2005) Protein Science , vol.14 , Issue.9 , pp. 2361-2369
    • Li, J.1    Xia, Z.2    Ding, J.3
  • 43
    • 0030923311 scopus 로고    scopus 로고
    • Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme
    • DOI 10.1021/bi962813z
    • LoBello, M., Oakley, A. J., Battistoni, A., Mazzetti, A. P., Nuccetelli, M., Mazzarese, G., et al. (1997). Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme. Biochemistry 36:6207-6217. (Pubitemid 27257889)
    • (1997) Biochemistry , vol.36 , Issue.20 , pp. 6207-6217
    • Lo Bello, M.1    Oakley, A.J.2    Battistoni, A.3    Mazzetti, A.P.4    Nuccetelli, M.5    Mazzarese, G.6    Rossjohn, J.7    Parker, M.W.8    Ricci, G.9
  • 45
    • 54249134375 scopus 로고    scopus 로고
    • Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation
    • Marsh, M., Shoemark, D. K., Jacob, A., Robinson, C., Cahill, B., Zhou, N.-Y., et al. (2008). Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation. J Mol Biol 384:165-177.
    • (2008) J Mol Biol , vol.384 , pp. 165-177
    • Marsh, M.1    Shoemark, D.K.2    Jacob, A.3    Robinson, C.4    Cahill, B.5    Zhou, N.-Y.6
  • 47
    • 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
    • McTigue, M. A., Williams, D. R., Tainer, J. A. (1995). 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 Mol Biol 246:21-27.
    • (1995) J Mol Biol , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 48
    • 0034778978 scopus 로고    scopus 로고
    • The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B
    • DOI 10.1110/ps.21201
    • Oakley, A. J., Harnnoi, T., Udomsinprasert, R., Jirajaroenrat, K., Ketterman, A. J., Wilce, M. C. J. (2001). The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B. Prot Sci 10:2176-2185. (Pubitemid 32988634)
    • (2001) Protein Science , vol.10 , Issue.11 , pp. 2176-2185
    • Oakley, A.J.1    Harnnoi, T.2    Udomsinprasert, R.3    Jirajaroenrat, K.4    Ketterman, A.J.5    Wilce, M.C.J.6
  • 49
    • 0344352500 scopus 로고    scopus 로고
    • The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes
    • DOI 10.1016/S0014-5793(97)01424-5, PII S0014579397014245
    • Oakley, A. J., Lo Bello, M., Mazzetti, A. P., Federici, G., Parker, M. W. (1997a). The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two diferent modes. FEBS Lett 419:32-36. (Pubitemid 28011211)
    • (1997) FEBS Letters , vol.419 , Issue.1 , pp. 32-36
    • Oakley, A.J.1    Lo Bello, M.2    Mazzetti, A.P.3    Federici, G.4    Parker, M.W.5
  • 50
    • 0033609951 scopus 로고    scopus 로고
    • The ligandin (non-substrate) binding site of human pi class glutathione transferase is located in the electrophile binding site (H-site)
    • DOI 10.1006/jmbi.1999.3029
    • Oakley, A. J., Lo Bello, M., Nuccetelli, M., Mazzetti, A.P., Parker, M. W. (1999). The ligandin (non-substrate) binding site of human pi class glutathione transferase is located in the electrophile binding site (H-site). J Mol Biol 291:913-926. (Pubitemid 29403620)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.4 , pp. 913-926
    • Oakley, A.J.1    Lo Bello, M.2    Nuccetelli, M.3    Mazzetti, A.P.4    Parker, M.W.5
  • 51
    • 0141648082 scopus 로고    scopus 로고
    • The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution
    • DOI 10.1006/jmbi.1997.1364
    • Oakley, A. J., LoBello, M., Battistoni, A., Ricci, G., Rossjohn, J., Villar, H. O., et al. (1997b). The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J Mol Biol 274:84-100. (Pubitemid 27519459)
    • (1997) Journal of Molecular Biology , vol.274 , Issue.1 , pp. 84-100
    • Oakley, A.J.1    Bello, M.L.2    Battistoni, A.3    Ricci, G.4    Rossjohn, J.5    Villar, H.O.6    Parker, M.W.7
  • 52
    • 0031017331 scopus 로고    scopus 로고
    • The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate
    • DOI 10.1021/bi962316i
    • Oakley, A. J., Rossjohn, J., LoBello, M., Caccuri, A. M., Federici, G., Parker, M. W. (1997c). The three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione. Biochemistry 36:576-585. (Pubitemid 27057005)
    • (1997) Biochemistry , vol.36 , Issue.3 , pp. 576-585
    • Oakley, A.J.1    Rossjohn, J.2    Lo Bello, M.3    Caccuri, A.M.4    Federici, G.5    Parker, M.W.6
  • 53
    • 44649175626 scopus 로고    scopus 로고
    • The anti-cancer drug chlorambucil as a substrate for the human polymorphic enzyme glutathione transferase P1-1: Kinetic properties and crystallographic characterisation of allelic variants
    • Parker, L. J., Ciccone, S., Italiano, L. C., Primavera, A., Oakley, A. J., Morton, C. J., et al. (2008). The anti-cancer drug chlorambucil as a substrate for the human polymorphic enzyme glutathione transferase P1-1: kinetic properties and crystallographic characterisation of allelic variants. J Mol Biol 380:131-144.
    • (2008) J Mol Biol , vol.380 , pp. 131-144
    • Parker, L.J.1    Ciccone, S.2    Italiano, L.C.3    Primavera, A.4    Oakley, A.J.5    Morton, C.J.6
  • 55
    • 0035852844 scopus 로고    scopus 로고
    • Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity
    • DOI 10.1021/bi002249z
    • Polekhina, G., Board, P. G., Blackburn, A. C., Parker, M. W. (2001). Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry 40:1567-1576. (Pubitemid 32144025)
    • (2001) Biochemistry , vol.40 , Issue.6 , pp. 1567-1576
    • Polekhina, G.1    Board, P.G.2    Blackburn, A.C.3    Parker, M.W.4
  • 56
    • 0031572846 scopus 로고    scopus 로고
    • Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor
    • Prade, L., Huber, R., Manoharan, T. H., Fahl, W. E., Reuter, W. (1997). Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue, and inhibitor. Structure 5:1287-1295. (Pubitemid 27484472)
    • (1997) Structure , vol.5 , Issue.10 , pp. 1287-1295
    • Prade, L.1    Huber, R.2    Manoharan, T.H.3    Fahl, W.E.4    Reuter, W.5
  • 57
    • 0026722795 scopus 로고
    • Tree-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution
    • Reinemer, P., Dirr, H. W., Ladenstein, R., Huber, R., Lo Bello, M., Federici, G., et al. (1992). Tree-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol 227:214-226.
    • (1992) J Mol 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
  • 58
    • 0025816448 scopus 로고
    • The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution
    • Reinemer, P., Dirr, H. W., Ladenstein, R., Schafer, J., Gallay, O., Huber, R. (1991). The 3-dimensional structure of class-pi glutathione-S- transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J 10:1997-2005. (Pubitemid 21905669)
    • (1991) EMBO Journal , vol.10 , Issue.8 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schaffer, J.4    Gallay, O.5    Huber, R.6
  • 59
    • 0029914965 scopus 로고    scopus 로고
    • Tree-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: Structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture
    • Reinemer, P., Prade, L., Hof, P., Neuefeind, T., Huber, R., Zettl, R., et al. (1996). Tree-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. J Mol Biol 255:289-309.
    • (1996) J Mol Biol , vol.255 , pp. 289-309
    • Reinemer, P.1    Prade, L.2    Hof, P.3    Neuefeind, T.4    Huber, R.5    Zettl, R.6
  • 61
    • 0032526942 scopus 로고    scopus 로고
    • A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications
    • Rossjohn, J., Polekhina, G., Feil, S. C., Allocati, N., Masulli, M., De Illio, C., et al. (1998b). A mixed disulfde bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6:721-734. (Pubitemid 28301206)
    • (1998) Structure , vol.6 , Issue.6 , pp. 721-734
    • Rossjohn, J.1    Polekhina, G.2    Feil, S.C.3    Allocati, N.4    Masulli, M.5    Di Iiio, C.6    Parker, M.W.7
  • 62
    • 0037337927 scopus 로고    scopus 로고
    • Cloning, expression and biochemical characterization of one epsilon-class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the epsilon class
    • DOI 10.1042/BJ20021287
    • Sawicki, R., Singh, S. P., Mondal, A. K., Benes, H., Zimniak, P. (2003). Cloning, expression, and biochemical characterization of one epsilon-class (GST-3) and ten delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identifcation of additional nine members of the epsilon class. Biochem J 370:661-669. (Pubitemid 36315154)
    • (2003) Biochemical Journal , vol.370 , Issue.2 , pp. 661-669
    • Sawicki, R.1    Singh, S.P.2    Mondal, A.K.3    Benes, H.4    Zimniak, P.5
  • 65
    • 0018754417 scopus 로고
    • Marked differences in the skin tumor-initiating activities of the optical enantiomers of the diastereomeric benzo(a)pyrene 7,8-diol-9,10-epoxides
    • Slaga, T. J., Bracken, W. J., Gleason, G., Levin, W., Yagi, H., Jerina, D. M., et al. (1979). Marked diferences in the skin tumor-initiating activities of the optical enantiomers of the diastereomeric benzo(a) pyrene 7,8-diol-9,10-epoxides. Cancer Res 39:67-71. (Pubitemid 9090414)
    • (1979) Cancer Research , vol.39 , Issue.1 , pp. 67-71
    • Slaga, T.J.1    Bracken, W.J.2    Gleason, G.3
  • 67
    • 0035210464 scopus 로고    scopus 로고
    • The MRP family and anticancer drug metabolism
    • DOI 10.2174/1389200013338289
    • Suzuki, T., Nishio, K., Tanabe, S. (2001). The MRP family and anticancer drug metabolism. Curr Drug Metab 2:367-377. (Pubitemid 33133981)
    • (2001) Current Drug Metabolism , vol.2 , Issue.4 , pp. 367-377
    • Suzuki, T.1    Nishio, K.2    Tanabe, S.3
  • 68
    • 0029853099 scopus 로고    scopus 로고
    • Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: Catalysis with different substrates involves different residues
    • Tan, K. L., Chelvanayagam, G., Parker, M. W., Board, P. G. (1996). Mutagenesis of the active site of the human theta-class glutathione transferase GSTT2-2: catalysis with diferent substrates involves diferent residues. Biochem J 319:315-321. (Pubitemid 26394774)
    • (1996) Biochemical Journal , vol.319 , Issue.1 , pp. 315-321
    • Tan, K.-L.1    Chelvanayagam, G.2    Parker, M.W.3    Board, P.G.4
  • 70
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew, K. D. (1994). Glutathione-associated enzymes in anticancer drug resistance. Cancer Res 54:4313-4320. (Pubitemid 24273141)
    • (1994) Cancer Research , vol.54 , Issue.16 , pp. 4313-4320
    • Tew, K.D.1
  • 71
    • 0037018936 scopus 로고    scopus 로고
    • Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification
    • DOI 10.1021/bi015964x
    • Tom, R., Cummins, I., Dixon, D. P., Edwards, R., Cole, D. J., Lapthorn, A. J. (2002). Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxifcation. Biochemistry 41:7008-7020. (Pubitemid 34575673)
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 7008-7020
    • Thom, R.1    Cummins, I.2    Dixon, D.P.3    Edwards, R.4    Cole, D.J.5    Lapthorn, A.J.6
  • 72
    • 34250211811 scopus 로고    scopus 로고
    • 2-Hydroxychromene-2-carboxylic acid isomerase: A kappa class glutathione transferase from Pseudomonas putida
    • DOI 10.1021/bi700356u
    • Tompson, L. C., Ladner, J. E., Codreanu, S. G., Harp, J., Gilliland, G. L., Armstrong, R. N. (2007). 2-hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida. Biochemistry 46:6710-6722. (Pubitemid 46906402)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6710-6722
    • Thompson, L.C.1    Ladner, J.E.2    Codreanu, S.G.3    Harp, J.4    Gilliland, G.L.5    Armstrong, R.N.6
  • 73
    • 33750044065 scopus 로고    scopus 로고
    • Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites
    • DOI 10.1074/jbc.M603125200
    • Tocheva, E. I., Fortin, P. D., Eltis, L. D., Murphy, M. E. (2006). Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites. J Biol Chem 281:30933-30940. (Pubitemid 44582148)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.41 , pp. 30933-30940
    • Tocheva, E.I.1    Fortin, P.D.2    Eltis, L.D.3    Murphy, M.E.P.4
  • 74
    • 0035910421 scopus 로고    scopus 로고
    • Affinity labeling of rat glutathione S-transferase isozyme 1-1 by 17β-iodoacetoxy-estradiol-3-sulfate
    • DOI 10.1074/jbc.M008212200
    • Vargo, M. A., Colman, R. F. (2001). Afnity labeling of rat glutathione S-transferase isozyme 1-1 by 17 beta-iodoacetoxy-estradiol-3-sulfate. J Biol Chem 276:2031-2036. (Pubitemid 32109683)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 2031-2036
    • Vargo, M.A.1    Colman, R.F.2
  • 75
    • 38649131959 scopus 로고    scopus 로고
    • Studies on membrane-associated prostaglandin e synthase-2 with reference to production of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT)
    • Watanabe, K., Ito, S., Yamamoto, S. (2008). Studies on membrane-associated prostaglandin E synthase-2 with reference to production of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT). Biochem Biophys Res Commun 367:782-786.
    • (2008) Biochem Biophys Res Commun , vol.367 , pp. 782-786
    • Watanabe, K.1    Ito, S.2    Yamamoto, S.3
  • 76
    • 73549084724 scopus 로고    scopus 로고
    • Identifcation and characterisation of new inhibitors for the human hematopoietic prostaglandin D2 synthase
    • Weber, J. E., Oakley, A. J., Christ, A. N., Clark, A. G., Hayes, J. D., Hall, R., et al. (2010). Identifcation and characterisation of new inhibitors for the human hematopoietic prostaglandin D2 synthase. Eur J Med Chem 45:447-454.
    • (2010) Eur J Med Chem , vol.45 , pp. 447-454
    • Weber, J.E.1    Oakley, A.J.2    Christ, A.N.3    Clark, A.G.4    Hayes, J.D.5    Hall, R.6
  • 77
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • Wilce, M. C., Board, P. G., Feil, S. C., Parker, M. W. (1995). Crystal structure of a theta-class glutathione transferase. EMBO J 14:2133-2143.
    • (1995) EMBO J , vol.14 , pp. 2133-2143
    • Wilce, M.C.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 78
    • 0033554428 scopus 로고    scopus 로고
    • Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: Evidence of signaling across the dimer interface
    • Xiao, B., Singh, S. P., Nanduri, B., Awasthi, Y. C., Zimniak, P., Ji, X. (1999). Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface. Biochemistry 38:11887-11894.
    • (1999) Biochemistry , vol.38 , pp. 11887-11894
    • Xiao, B.1    Singh, S.P.2    Nanduri, B.3    Awasthi, Y.C.4    Zimniak, P.5    Ji, X.6
  • 79
    • 18044367744 scopus 로고    scopus 로고
    • Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2)
    • DOI 10.1016/j.jmb.2005.03.035
    • Yamada, T., Komoto, J., Watanabe, K., Ohmiya, Y., Takusagawa, F. (2005). Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2). J Mol Biol 348:1163-1176. (Pubitemid 40602374)
    • (2005) Journal of Molecular Biology , vol.348 , Issue.5 , pp. 1163-1176
    • Yamada, T.1    Komoto, J.2    Watanabe, K.3    Ohmiya, Y.4    Takusagawa, F.5
  • 80
    • 34447579119 scopus 로고    scopus 로고
    • 2 synthase type 2: The first example of a dual-function enzyme
    • DOI 10.1021/bi700605m
    • Yamada, T., Takusagawa, F. (2007). PGH2 degradation pathway catalyzed by GSH-heme complex bound microsomal prostaglandin E2 synthase type 2: the frst example of a dual-function enzyme. Biochemistry 46:8414-8424. (Pubitemid 47075978)
    • (2007) Biochemistry , vol.46 , Issue.28 , pp. 8414-8424
    • Yamada, T.1    Takusagawa, F.2
  • 81
    • 55149089058 scopus 로고    scopus 로고
    • "Restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2
    • Zhang, Z. R., Bai, M., Wang, X. Y., Zhou, J. M., Perrett, S. (2008). "Restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2. J Mol Biol 384:641-651.
    • (2008) J Mol Biol , vol.384 , pp. 641-651
    • Zhang, Z.R.1    Bai, M.2    Wang, X.Y.3    Zhou, J.M.4    Perrett, S.5


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