-
1
-
-
0031021397
-
Structure, catalytic mechanism and evolution of the glutathione transferases
-
Armstrong RN: Structure, catalytic mechanism and evolution of the glutathione transferases. Chem Res Toxicol 1997, 10:2-18.
-
(1997)
Chem Res Toxicol
, vol.10
, pp. 2-18
-
-
Armstrong, R.N.1
-
2
-
-
0031056720
-
Bacterial glutathione S-transferases: What are they good for?
-
Vuilleumier S: Bacterial glutathione S-transferases: What are they good for? J Bacteriol 1997, 179:1431-1441.
-
(1997)
J Bacteriol
, vol.179
, pp. 1431-1441
-
-
Vuilleumier, S.1
-
3
-
-
0000313919
-
Glutathione transferases
-
Edited by Guengerich FR Oxford: Elsevier Science
-
Armstrong RN: Glutathione transferases. In Comprehensive Toxicology, vol 3, Biotransformation. Edited by Guengerich FR Oxford: Elsevier Science; 1997:307-327.
-
(1997)
Comprehensive Toxicology, Vol 3, Biotransformation
, vol.3
, pp. 307-327
-
-
Armstrong, R.N.1
-
4
-
-
0006762268
-
Nucleophilic epoxide openings
-
Edited by Poulter CD. Oxford: Elsevier Science; in press
-
Armstrong RN: Nucleophilic epoxide openings. In Comprehensive Natural Products Chemistry, vol 5. Edited by Poulter CD. Oxford: Elsevier Science; 1998:in press.
-
(1998)
Comprehensive Natural Products Chemistry, Vol 5
, vol.5
-
-
Armstrong, R.N.1
-
5
-
-
0025816448
-
The three-dimensional structure of class-pi glutathione S-transferase in complex with glutathione sulfonate at 2.8 A resolution
-
Reinemer P, Dirr HW, Ladenstein R, Schaffer J, Gallay O, Huber R: The three-dimensional structure of class-pi glutathione S-transferase in complex with glutathione sulfonate at 2.8 A resolution. EMBO J 1991, 10:1997-2005.
-
(1991)
EMBO J
, vol.10
, pp. 1997-2005
-
-
Reinemer, P.1
Dirr, H.W.2
Ladenstein, R.3
Schaffer, J.4
Gallay, O.5
Huber, R.6
-
6
-
-
0030670259
-
Identification of a covalent intermediate between glutathione and cysteine 13 formed during catalysis by tetrachlorohydroquinone dehalogenase
-
McCarthy DL, Louie DF, Copley SD: Identification of a covalent intermediate between glutathione and cysteine 13 formed during catalysis by tetrachlorohydroquinone dehalogenase. J Am Chem Soc 1997, 119:11337-11338. The mechanistic hypothesis advanced in this paper suggests a possible mechanistic link between the canonical glutathione transferases and the redox proteins, thioredoxin and glutaredoxin, to which they are structurally related.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 11337-11338
-
-
McCarthy, D.L.1
Louie, D.F.2
Copley, S.D.3
-
7
-
-
0032175395
-
Microbial dehalogenases: Enzymes recruited to convert xenobiotic substrates
-
Copley SD: Microbial dehalogenases: enzymes recruited to convert xenobiotic substrates. Curr Opin Chem Biol 1998, 2:613-617.
-
(1998)
Curr Opin Chem Biol
, vol.2
, pp. 613-617
-
-
Copley, S.D.1
-
8
-
-
0030445133
-
Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily
-
McCarthy DL, Navarrete S, Willett WS, Babbitt P, Copley SD: Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily. Biochemistry 1996, 35:14634-14642.
-
(1996)
Biochemistry
, vol.35
, pp. 14634-14642
-
-
McCarthy, D.L.1
Navarrete, S.2
Willett, W.S.3
Babbitt, P.4
Copley, S.D.5
-
9
-
-
0032526942
-
A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications
-
Rossjohn J, Polekhina G, Feil SC, Allocati N, Masulli M, Di Ilio C, Parker MW: A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 1998, 6:721-734. This paper provides additional, and very provocative, structural evidence for an evolutionary link between redox proteins of the thioredoxin fold and glutathione transferases. Even though the functional importance of the mixed disulfide is not clear, the evolutionary implications are.
-
(1998)
Structure
, vol.6
, pp. 721-734
-
-
Rossjohn, J.1
Polekhina, G.2
Feil, S.C.3
Allocati, N.4
Masulli, M.5
Di Ilio, C.6
Parker, M.W.7
-
10
-
-
0029960278
-
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
-
Parsons JF, Armstrong RN: 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 1996, 118:2295-2296.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 2295-2296
-
-
Parsons, J.F.1
Armstrong, R.N.2
-
11
-
-
0032554059
-
Analysis of the role of the active site tyrosine in human glutathione transferase A1-1 by unnatural amino acid mutagenesis
-
Thorson JS, Shin I, Chapman E, Stenberg G, Mannervik B, Schultz PG: Analysis of the role of the active site tyrosine in human glutathione transferase A1-1 by unnatural amino acid mutagenesis. J Am Chem Soc 1998, 120:451-452. An excellent and rare example of the use of site-specific mutagenesis using unnatural amino acids to investigate enzyme mechanisms with linear free energy relationships. The results are again highly suggestive of electrophilic stabilization of the thiolate group of glutathione by the enzyme (see [10] for earlier work in this area).
-
(1998)
J Am Chem Soc
, vol.120
, pp. 451-452
-
-
Thorson, J.S.1
Shin, I.2
Chapman, E.3
Stenberg, G.4
Mannervik, B.5
Schultz, P.G.6
-
12
-
-
0032478199
-
Proton release upon glutathione binding to glutathione transferase P1-1 -kinetic analysis of a multistep glutathione binding process
-
- being the primary species in the enzyme-substrate complex.
-
(1998)
Biochemistry
, vol.37
, pp. 3028-3034
-
-
Caccuri, A.M.1
Lobello, M.2
Nuccetelli, M.3
Nicotra, M.4
Rossi, P.5
Antonini, G.6
Federici, G.7
Ricci, G.8
-
13
-
-
0032478261
-
Solution structure of glutathione bound to human glutathione transferase P1-1 - Comparison of NMR measurements with the crystal structure
-
Nicotra M, Paci M, Sette M, Oakley AJ, Parker MW, Lobello M, Caccuri AM, Federici G, Ricci G: Solution structure of glutathione bound to human glutathione transferase P1-1 - comparison of NMR measurements with the crystal structure. Biochemistry 1998, 37:3020-3027. A very interesting contrast of the structures of glutathione (GSH)-bound to GSH transferase as determined by crystallography and NMR. The NMR results are taken to suggest a 'precomplex' between the enzyme and GSH but the identity and importance of the binding site giving rise to the transfer nuclear Overhauser effects is not clear.
-
(1998)
Biochemistry
, vol.37
, pp. 3020-3027
-
-
Nicotra, M.1
Paci, M.2
Sette, M.3
Oakley, A.J.4
Parker, M.W.5
Lobello, M.6
Caccuri, A.M.7
Federici, G.8
Ricci, G.9
-
14
-
-
0032485881
-
Enzymes harboring unnatural amino acids. Mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan
-
Parsons JF, Xiao G, Gilliland GL, Armstrong RN: Enzymes harboring unnatural amino acids. Mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan. Biochemistry 1998, 37:6286-6294. Substitution of 5-fluorotryptophan for tryptophan results in enhanced catalytic activity due to increased rates of product release that can be traced to subtle structural changes in the carboxy-terminal domain of the enzyme. Fluorine is not isosteric with hydrogen! The kinetic mechanism for binding glutathione is unaffected.
-
(1998)
Biochemistry
, vol.37
, pp. 6286-6294
-
-
Parsons, J.F.1
Xiao, G.2
Gilliland, G.L.3
Armstrong, R.N.4
-
15
-
-
0031017331
-
Three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate
-
Oakley AJ, Rossjohn J, Lobello M, Caccuri AM, Federici G, Parker MW: Three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry 1997, 36:576-585.
-
(1997)
Biochemistry
, vol.36
, pp. 576-585
-
-
Oakley, A.J.1
Rossjohn, J.2
Lobello, M.3
Caccuri, A.M.4
Federici, G.5
Parker, M.W.6
-
16
-
-
0031572846
-
Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor
-
Prade L, Huber R, Manoharan TH, Fahl WE, Reuter W: Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor. Structure 1997, 5:1287-1295.
-
(1997)
Structure
, vol.5
, pp. 1287-1295
-
-
Prade, L.1
Huber, R.2
Manoharan, T.H.3
Fahl, W.E.4
Reuter, W.5
-
17
-
-
0032579563
-
The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-31 OB region
-
Vega MC, Walsh SB, Mantle TJ, Coll M: The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-31 OB region. J Biol Chem 1998, 273:2844-2850.
-
(1998)
J Biol Chem
, vol.273
, pp. 2844-2850
-
-
Vega, M.C.1
Walsh, S.B.2
Mantle, T.J.3
Coll, M.4
-
18
-
-
0344352500
-
The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes
-
Oakley AJ, Lo Bello M, Mazzetti AP, Federici G, Parker MW: The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes. FEBS Lett 1997, 419:32-36.
-
(1997)
FEBS Lett
, vol.419
, pp. 32-36
-
-
Oakley, A.J.1
Lo Bello, M.2
Mazzetti, A.P.3
Federici, G.4
Parker, M.W.5
-
19
-
-
0141648082
-
The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution
-
Oakley AJ, Bello ML, Battistoni A, Ricci G, Rossjohn J, Villar HO, Parker MW: The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J Mol Biol 1997, 274:84-100.
-
(1997)
J Mol Biol
, vol.274
, 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
-
20
-
-
0030748102
-
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
-
Ji X, Tordova M, O'Donnell R, Parsons JF, Hayden JB, Gilliland GL, Zimniak P: 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 1997 36:9690-9702.
-
(1997)
Biochemistry
, vol.36
, 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
-
21
-
-
0030923311
-
Multifunctional role of tyr 108 in the catalytic mechanism of human glutathione transferase P1-1 - Crystallographic and kinetic studies on the Y108F mutant enzyme
-
Lobello M, Oakley AJ, Battistoni A, Mazzetti AP, Nuccetelli M, Mazzarese G, Rossjohn J, Parker MW, Ricci G: 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 1997, 36:6207-6217.
-
(1997)
Biochemistry
, vol.36
, pp. 6207-6217
-
-
Lobello, 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
-
22
-
-
0031566035
-
Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: A leading enzyme in detoxification of maize herbicides
-
Neuefeind T, Huber R, Reinemer P, Knablein J, Prade L, Mann K, Bieseler B: Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides. J Mol Biol 1997, 274:577-587.
-
(1997)
J Mol Biol
, vol.274
, pp. 577-587
-
-
Neuefeind, T.1
Huber, R.2
Reinemer, P.3
Knablein, J.4
Prade, L.5
Mann, K.6
Bieseler, B.7
-
23
-
-
0031565823
-
Crystal structure of herbicide-detoxifying maize glutathione S-transferase-l in complex with lactoylglutathione: Evidence for an induced-fit mechanism
-
Neuefeind T, Huber R, Dasenbrock H, Prade L, Bieseler B: Crystal structure of herbicide-detoxifying maize glutathione S-transferase-l in complex with lactoylglutathione: evidence for an induced-fit mechanism. J Mol Biol 1997, 274:446-453.
-
(1997)
J Mol Biol
, vol.274
, pp. 446-453
-
-
Neuefeind, T.1
Huber, R.2
Dasenbrock, H.3
Prade, L.4
Bieseler, B.5
-
24
-
-
0031558812
-
Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase
-
Rossjohn J, Feil SC, Wilce MCJ, Sexton JL, Spithill TW, Parker MW: Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase. J Mol Biol 1997, 273:857-872.
-
(1997)
J Mol Biol
, vol.273
, pp. 857-872
-
-
Rossjohn, J.1
Feil, S.C.2
Wilce, M.C.J.3
Sexton, J.L.4
Spithill, T.W.5
Parker, M.W.6
-
25
-
-
0032548807
-
Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site
-
Casalone E, Allocati N, Ceccarelli I, Masulli M, Rossjohn J, Parker MW, Diilio C: Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site. FEBS Lett 1998, 423:122-124.
-
(1998)
FEBS Lett
, vol.423
, pp. 122-124
-
-
Casalone, E.1
Allocati, N.2
Ceccarelli, I.3
Masulli, M.4
Rossjohn, J.5
Parker, M.W.6
Diilio, C.7
-
26
-
-
0030826237
-
Crystal structure of tetradeca(3-fluorotyrosyl)glutathione transferase
-
Xiao G, Parsons, JF, Armstrong RN, Gilliland GL: Crystal structure of tetradeca(3-fluorotyrosyl)glutathione transferase. J Am Chem Soc 1997, 119:9325-9326. This paper describes the first crystal structure of an enzyme globally substituted with an unnatural amino acid, 3-fluorotyrosine, and sounds a cautionary note concerning possible structural consequences of fluorine-for-hydrogen substitutions in proteins.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 9325-9326
-
-
Xiao, G.1
Parsons, J.F.2
Armstrong, R.N.3
Gilliland, G.L.4
-
27
-
-
0032516767
-
Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine
-
in press
-
Xiao G, Parsons JF, Tesh K, Armstrong RN, Gilliland GL: Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine. J Mol Biol 1998, in press.
-
(1998)
J Mol Biol
-
-
Xiao, G.1
Parsons, J.F.2
Tesh, K.3
Armstrong, R.N.4
Gilliland, G.L.5
-
28
-
-
0030910555
-
Pressure-dependent ionization of Tyr9 in glutathione S-transferase A1-1: Contribution of the C-terminal helix to a 'soff active site
-
Atkins WM, Dietze EC, Ibarra C: Pressure-dependent ionization of Tyr9 in glutathione S-transferase A1-1: contribution of the C-terminal helix to a 'soff active site. Protein Sci 1997, 6:873-881. Put an enzyme under pressure and there is no telling what it will do. Pressure tactics force the enzyme to reveal the movements of a portion of its structure.
-
(1997)
Protein Sci
, vol.6
, pp. 873-881
-
-
Atkins, W.M.1
Dietze, E.C.2
Ibarra, C.3
-
29
-
-
0030824202
-
The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability
-
Dragani B, Stenberg G, Melino S, Petruzzelli R, Mannervik B, Aceto A: The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability. J Biol Chem 1997, 272:25518-25523.
-
(1997)
J Biol Chem
, vol.272
, pp. 25518-25523
-
-
Dragani, B.1
Stenberg, G.2
Melino, S.3
Petruzzelli, R.4
Mannervik, B.5
Aceto, A.6
-
30
-
-
0032515932
-
Equilibrium and kinetic unfolding properties of dimeric human glutathione transferase A1-1
-
Wallace LA, Sluis-Cremer N, Dirr HW: Equilibrium and kinetic unfolding properties of dimeric human glutathione transferase A1-1. Biochemistry 1998, 37:5320-5328. Perhaps the most informative study yet of dimer assembly and folding of a glutathione transferase.
-
(1998)
Biochemistry
, vol.37
, pp. 5320-5328
-
-
Wallace, L.A.1
Sluis-Cremer, N.2
Dirr, H.W.3
-
31
-
-
0030985001
-
4-Substituted 1-chloro-2-nitrobenzenes: Structure-activity relationships and extension of the substrate model of rat glutathione S-transferase 4-4
-
Van der Aar EM, de Groot MJ, Bouwman T, Bijloo GJ, Commandeur JN, Vermeulen NP: 4-Substituted 1-chloro-2-nitrobenzenes: structure-activity relationships and extension of the substrate model of rat glutathione S-transferase 4-4. Chem Res Toxicol-1997, 10:439-449.
-
(1997)
Chem Res Toxicol
, vol.10
, pp. 439-449
-
-
Van Der Aar, E.M.1
De Groot, M.J.2
Bouwman, T.3
Bijloo, G.J.4
Commandeur, J.N.5
Vermeulen, N.P.6
-
32
-
-
0031010027
-
Ligand-based protein alignment and isozyme specificity of glutathione S-transferase inhibitors
-
Koehler RT, Villar HO, Bauer KE, Higgins DL: Ligand-based protein alignment and isozyme specificity of glutathione S-transferase inhibitors. Proteins 1997, 28:202-216.
-
(1997)
Proteins
, vol.28
, pp. 202-216
-
-
Koehler, R.T.1
Villar, H.O.2
Bauer, K.E.3
Higgins, D.L.4
-
33
-
-
0031032284
-
Homology model for the human GSTT2 theta class glutathione transferase
-
Chelvanayagam G, Wilce MCJ, Parker MW, Tan KL, Board PG: Homology model for the human GSTT2 theta class glutathione transferase. Proteins 1997, 27:118-130.
-
(1997)
Proteins
, vol.27
, pp. 118-130
-
-
Chelvanayagam, G.1
Wilce, M.C.J.2
Parker, M.W.3
Tan, K.L.4
Board, P.G.5
-
34
-
-
0031439569
-
Zeta, a novel class of glutathione transferases in a range of species from plants to humans
-
Board PG, Baker RT, Chelvanayagam G, Jermiin LS: Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem J 1997, 328:929-935. Yet another class of glutathione transferase and one that appears to have been around for a long time. Will we run out of Greek letters before all of the classes are discovered?
-
(1997)
Biochem J
, vol.328
, pp. 929-935
-
-
Board, P.G.1
Baker, R.T.2
Chelvanayagam, G.3
Jermiin, L.S.4
-
35
-
-
0030662474
-
Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina
-
Caccuri AM, Antonini G, Nicotra M, Battistoni A, Bello ML, Board PG, Parker MW, Ricci G: Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina. J Biol Chem 1997, 272:29681-29686.
-
(1997)
J Biol Chem
, vol.272
, pp. 29681-29686
-
-
Caccuri, A.M.1
Antonini, G.2
Nicotra, M.3
Battistoni, A.4
Bello, M.L.5
Board, P.G.6
Parker, M.W.7
Ricci, G.8
-
36
-
-
0031033654
-
Resonance energy transfer between sites in rat liver glutathione S-transferase, 1-1, selectively modified at cysteine-17 and cysteine-111
-
Hu L, Colman RF: Resonance energy transfer between sites in rat liver glutathione S-transferase, 1-1, selectively modified at cysteine-17 and cysteine-111. Biochemistry 1997, 36:1635-1645.
-
(1997)
Biochemistry
, vol.36
, pp. 1635-1645
-
-
Hu, L.1
Colman, R.F.2
-
37
-
-
0031239839
-
Identification of the nonsubstrate steroid binding site of rat liver glutathione S-transferase, isozyme 1-1, by the steroid affinity label, 3β-(iodoacetoxy)dehydroisoandrosterone
-
Barycki JJ, Colman RF: Identification of the nonsubstrate steroid binding site of rat liver glutathione S-transferase, isozyme 1-1, by the steroid affinity label, 3β-(iodoacetoxy)dehydroisoandrosterone. Arch Biochem Biophys 1997, 345:16-31. Provides evidence from affinity labeling for the location of a nonsubstrate ligand-binding site. Recall that early examples of glutathione transferases were isolated as ligand-binding proteins.
-
(1997)
Arch Biochem Biophys
, vol.345
, pp. 16-31
-
-
Barycki, J.J.1
Colman, R.F.2
-
38
-
-
0030778937
-
Evidence that human class theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GST T1-1 with that of classes alpha, mu and pi GST in human
-
Sherratt PJ, Pulford DJ, Harrison DJ, Green T, Hayes JD: Evidence that human class theta glutathione S-transferase T1-1 can catalyse the activation of dichloromethane, a liver and lung carcinogen in the mouse. Comparison of the tissue distribution of GST T1-1 with that of classes alpha, mu and pi GST in human. Biochem J 1997, 326:837-846.
-
(1997)
Biochem J
, vol.326
, pp. 837-846
-
-
Sherratt, P.J.1
Pulford, D.J.2
Harrison, D.J.3
Green, T.4
Hayes, J.D.5
-
39
-
-
0031565995
-
Interactions of alpha, beta-unsaturated aldehydes and ketones with human glutathione S-transferase P1-1
-
Van Iersel ML, Ploemen JP, Lo Bello M, Federici G, van Bladeren PJ: Interactions of alpha, beta-unsaturated aldehydes and ketones with human glutathione S-transferase P1-1. Chem Biol Interact 1997, 108:67-78.
-
(1997)
Chem Biol Interact
, vol.108
, pp. 67-78
-
-
Van Iersel, M.L.1
Ploemen, J.P.2
Lo Bello, M.3
Federici, G.4
Van Bladeren, P.J.5
-
40
-
-
0030781225
-
Biotransformation of the naturally occurring isothiocyanate sulforaphane in the rat: Identification of phase I metabolites and glutathione conjugates
-
Kassahun K, Davis M, Hu P, Martin B, Baillie T: Biotransformation of the naturally occurring isothiocyanate sulforaphane in the rat: identification of phase I metabolites and glutathione conjugates. Chem Res Toxicol 1997, 10:1228-1233.
-
(1997)
Chem Res Toxicol
, vol.10
, pp. 1228-1233
-
-
Kassahun, K.1
Davis, M.2
Hu, P.3
Martin, B.4
Baillie, T.5
-
41
-
-
0030822939
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Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1
-
Sundberg K, Widersten M, Seidel A, Mannervik B, Jernstrom B: Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1. Chem Res Toxicol 1997, 10:1221-1227.
-
(1997)
Chem Res Toxicol
, vol.10
, pp. 1221-1227
-
-
Sundberg, K.1
Widersten, M.2
Seidel, A.3
Mannervik, B.4
Jernstrom, B.5
-
42
-
-
0030967073
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Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes
-
Baez S, Seguraaguilar J, Widersten M, Johansson AS, Mannervik B: Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes. Biochem J 1997 324:25-28.
-
(1997)
Biochem J
, vol.324
, pp. 25-28
-
-
Baez, S.1
Seguraaguilar, J.2
Widersten, M.3
Johansson, A.S.4
Mannervik, B.5
-
43
-
-
0031041078
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Human class mu glutathione transferases, in particular isoenzyme M2-2, catalyze detoxication of the dopamine metabolite aminochrome
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Segura-Aguilar J, Baez S, Widersten M, Welch CJ, Mannervik B: Human class mu glutathione transferases, in particular isoenzyme M2-2, catalyze detoxication of the dopamine metabolite aminochrome. J Biol Chem 1997, 272:5727-5731. This proposes a possible link between specific glutathione transferases and the detoxication of oxidized metabolites of neurotransmitters. The enzyme could be involved in neurodegenerative processes.
-
(1997)
J Biol Chem
, vol.272
, pp. 5727-5731
-
-
Segura-Aguilar, J.1
Baez, S.2
Widersten, M.3
Welch, C.J.4
Mannervik, B.5
-
45
-
-
17944397403
-
An evolutionary approach to the design of glutathione-linked enzymes
-
Mannervik B, Cameron AD, Fernandez E, Gustafsson A, Hansson LO, Jemth P, Jiang F, Jones TA, Larsson A, Nilsson LO et al.: An evolutionary approach to the design of glutathione-linked enzymes. Chem Biol Interact 1998, 112:15-21.
-
(1998)
Chem Biol Interact
, vol.112
, pp. 15-21
-
-
Mannervik, B.1
Cameron, A.D.2
Fernandez, E.3
Gustafsson, A.4
Hansson, L.O.5
Jemth, P.6
Jiang, F.7
Jones, T.A.8
Larsson, A.9
Nilsson, L.O.10
-
46
-
-
0342618500
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Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases
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Bernat BA, Laughlin LT, Armstrong RN: Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry 1997, 36:3050-3055. This paper provides the first evidence for a metal-dependent glutathione transferase and proposes a new protein superfamily to which it belongs, based on structural and mechanistic considerations.
-
(1997)
Biochemistry
, vol.36
, pp. 3050-3055
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-
Bernat, B.A.1
Laughlin, L.T.2
Armstrong, R.N.3
-
47
-
-
17944386988
-
Mechanistic imperative for the evolution of a metalloglutathione transferase of the vicinal oxygen chelate superfamily
-
Laughlin LT, Bernat BA, Armstrong RN: Mechanistic imperative for the evolution of a metalloglutathione transferase of the vicinal oxygen chelate superfamily. Chem Biol Interact 1998, 111:41-50.
-
(1998)
Chem Biol Interact
, vol.111
, pp. 41-50
-
-
Laughlin, L.T.1
Bernat, B.A.2
Armstrong, R.N.3
-
48
-
-
0030667789
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Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities
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Babbitt PC, Gerlt JA: Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities. J Biol Chem 1997, 272:30591-30594. A lucid and provocative article underwriting the fact that chemical mechanism is an important determinant in the evolution of enzyme function. Understanding chemistry is important for understanding genomics.
-
(1997)
J Biol Chem
, vol.272
, pp. 30591-30594
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-
Babbitt, P.C.1
Gerlt, J.A.2
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49
-
-
0030927104
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Crystal structure of human glyoxalase I - Evidence for gene duplication and 3D domain swapping
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Cameron AD, Olin B, Ridderström M, Mannervik B, Jones TA: Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping. EMBO J 1997, 16:3386-3395. The first crystal structure of a glyoxalase helps to define a new superfamily of metalloenzymes, some of which are glutathione transferases.
-
(1997)
EMBO J
, vol.16
, pp. 3386-3395
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-
Cameron, A.D.1
Olin, B.2
Ridderström, M.3
Mannervik, B.4
Jones, T.A.5
-
50
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0032577620
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Regiochemical and stereochemical course of the reaction catalyzed by the fosfomycin resistance protein, FosA
-
Bernat BA, Laughlin LT, Armstrong RN: Regiochemical and stereochemical course of the reaction catalyzed by the fosfomycin resistance protein, FosA. J Org Chem 1998, 63:3778-3780.
-
(1998)
J Org Chem
, vol.63
, pp. 3778-3780
-
-
Bernat, B.A.1
Laughlin, L.T.2
Armstrong, R.N.3
-
51
-
-
0030923439
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Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase activities
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Jakobsson PJ, Mancini JA, Riendeau D, Ford-Hutchinson AW: Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase activities. J Biol Chem 1997, 272:22934-22939.
-
(1997)
J Biol Chem
, vol.272
, pp. 22934-22939
-
-
Jakobsson, P.J.1
Mancini, J.A.2
Riendeau, D.3
Ford-Hutchinson, A.W.4
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52
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0031554721
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The 3.0 Angstrom projection structure of microsomal glutathione transferase as determined by electron crystallography of P2(1)2(1)2 two-dimensional crystals
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Hebert H, Schmidtkrey I, Morgenstern R, Murata K. Hirai T, Mitsuoka K, Fujiyoshi Y: The 3.0 Angstrom projection structure of microsomal glutathione transferase as determined by electron crystallography of P2(1)2(1)2 two-dimensional crystals. J Mol Biol 1997, 271:751-758. Improvements in the resolution of the two-dimensional projection structure of microsomal glutathione transferase bode well for the ultimate solution of its three-dimensional structure by electron crystallography.
-
(1997)
J Mol Biol
, vol.271
, pp. 751-758
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-
Hebert, H.1
Schmidtkrey, I.2
Morgenstern, R.3
Murata, K.4
Hirai, T.5
Mitsuoka, K.6
Fujiyoshi, Y.7
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53
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0030911870
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Structural and functional aspects of rat microsomal glutathione transferase -the roles of cysteine 49, arginine 107, lysine 67, histidine, and tyrosine residues
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Weinander R, Ekstrom L, Andersson C, Raza H, Bergman T, Morgenstern R: Structural and functional aspects of rat microsomal glutathione transferase -the roles of cysteine 49, arginine 107, lysine 67, histidine, and tyrosine residues. J Biol Chem 1997, 272:8871-8877.
-
(1997)
J Biol Chem
, vol.272
, pp. 8871-8877
-
-
Weinander, R.1
Ekstrom, L.2
Andersson, C.3
Raza, H.4
Bergman, T.5
Morgenstern, R.6
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54
-
-
0030882948
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Binding of glutathione and an inhibitor to microsomal glutathione transferase
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Sun TH, Morgenstern R: Binding of glutathione and an inhibitor to microsomal glutathione transferase. Biochem J 1997, 326:193-196. This paper provides solid evidence that the active sites of the microsomal enzyme (which is a trimer) do not behave independently.
-
(1997)
Biochem J
, vol.326
, pp. 193-196
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Sun, T.H.1
Morgenstern, R.2
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