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Volumn 287, Issue 2, 1999, Pages 265-276

Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling

Author keywords

Chimera; DNA shuffling; Glutathione transferase; Mutant library; Screening

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; BACTERIAL DNA; BACTERIUM LYSATE; CHROMIUM DERIVATIVE; DOPAMINE; GLUTATHIONE TRANSFERASE; NITROSO DERIVATIVE; NITROSOGUANIDINE;

EID: 0033605826     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2607     Document Type: Article
Times cited : (47)

References (46)
  • 1
    • 0028965835 scopus 로고
    • Superoxide dismutase and catalase enhance autooxidation during one-electron reduction of aminochrome by NADPH-cytochrome P-450 reductase
    • Baez S., Linderson Y., Segura-Aguilar J. Superoxide dismutase and catalase enhance autooxidation during one-electron reduction of aminochrome by NADPH-cytochrome P-450 reductase. Biochem. Mol. Med. 54:1995;12-18.
    • (1995) Biochem. Mol. Med. , vol.54 , pp. 12-18
    • Baez, S.1    Linderson, Y.2    Segura-Aguilar, J.3
  • 2
    • 0030967073 scopus 로고    scopus 로고
    • 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., Segura-Aguilar J., Widersten M., Johansson A.-S., 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. 324:1997;25-28.
    • (1997) Biochem. J. , vol.324 , pp. 25-28
    • Baez, S.1    Segura-Aguilar, J.2    Widersten, M.3    Johansson, A.-S.4    Mannervik, B.5
  • 3
    • 0028036292 scopus 로고
    • Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases
    • Berhane K., Widersten M., Engström Å., Kozarich J. W., Mannervik B. Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proc. Natl Acad. Sci. USA. 91:1994;1480-1484.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1480-1484
    • Berhane, K.1    Widersten, M.2    Engström, Å.3    Kozarich, J.W.4    Mannervik, B.5
  • 4
    • 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
    • Björnestedt R., Widersten M., Board P. G., Mannervik B. 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. 282:1992;505-510.
    • (1992) Biochem. J. , vol.282 , pp. 505-510
    • Björnestedt, R.1    Widersten, M.2    Board, P.G.3    Mannervik, B.4
  • 5
    • 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
    • Björnestedt R., Tardioli S., Mannervik B. 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. 270:1995;29705-29709.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29705-29709
    • Björnestedt, R.1    Tardioli, S.2    Mannervik, B.3
  • 6
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board P. G., Baker R. T., Chelvanayagam G., Jermiin L. S. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 328:1997;929-935.
    • (1997) Biochem. J. , vol.328 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 7
    • 0027058697 scopus 로고
    • Glutathione S-transferases: Amino acid sequence comparison, classification and phylogenetic relationship
    • Buetler T. M., Eaton D. L. Glutathione S-transferases: amino acid sequence comparison, classification and phylogenetic relationship. Environ. Carcin. Ecotoxicol. Rev. C10:1992;181-203.
    • (1992) Environ. Carcin. Ecotoxicol. Rev. , vol.10 , pp. 181-203
    • Buetler, T.M.1    Eaton, D.L.2
  • 8
    • 0028245964 scopus 로고
    • A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes
    • Comstock K. E., Widersten M., Hao X.-Y., Henner W. D., Mannervik B. A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes. Arch. Biochem. Biophys. 311:1994;487-495.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 487-495
    • Comstock, K.E.1    Widersten, M.2    Hao, X.-Y.3    Henner, W.D.4    Mannervik, B.5
  • 9
    • 0030048583 scopus 로고    scopus 로고
    • Construction and evolution of antibody-phage libraries by DNA shuffling
    • Crameri A., Cwirla S., Stemmer W. P. C. Construction and evolution of antibody-phage libraries by DNA shuffling. Nature Med. 2:1996a;100-102.
    • (1996) Nature Med. , vol.2 , pp. 100-102
    • Crameri, A.1    Cwirla, S.2    Stemmer, W.P.C.3
  • 10
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri A., Whitehorn E. A., Tate E., Stemmer W. P. C. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nature Biotechnol. 14:1996b;315-319.
    • (1996) Nature Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.C.4
  • 12
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri A., Raillard S.-A., Bermudez E., Stemmer W. P. C. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature. 391:1998;288-291.
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.-A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 15
    • 0018263844 scopus 로고
    • Why genes in pieces?
    • Gilbert W. Why genes in pieces? Nature. 271:1978;501.
    • (1978) Nature , vol.271 , pp. 501
    • Gilbert, W.1
  • 16
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W. H., Pabst M. J., Jakoby W. B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:1974;7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 17
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J. D., Pulford D. J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30:1995;445-600.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 18
    • 0023641071 scopus 로고
    • Evidence for cytosolic glutathione transferase-mediated denitrosation of nitrosocimetidine and 1-methyl-2-nitro-1-nitrosoguanidine
    • Jensen D. E., Stelman G. J. Evidence for cytosolic glutathione transferase-mediated denitrosation of nitrosocimetidine and 1-methyl-2-nitro-1-nitrosoguanidine. Carcinoginesis. 8:1987;1791-1800.
    • (1987) Carcinoginesis , vol.8 , pp. 1791-1800
    • Jensen, D.E.1    Stelman, G.J.2
  • 19
    • 0030812312 scopus 로고    scopus 로고
    • Denitrosation of 1,3-dimethyl-2-cyano-1-nitrosoguanidine in rat primary hepatocyte cultures
    • Jensen D. E., Belka G. K., Dworkin C. Denitrosation of 1,3-dimethyl-2-cyano-1-nitrosoguanidine in rat primary hepatocyte cultures. Biochem. Pharmacol. 53:1997;1297-1306.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1297-1306
    • Jensen, D.E.1    Belka, G.K.2    Dworkin, C.3
  • 20
    • 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
    • Ji X., Zhang P., Armstrong R. N., Gilliland G. L. 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. 31:1992;10169-10184.
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 24
    • 0029840092 scopus 로고    scopus 로고
    • Evolution of glutathione transferases and related enzymes for the protection of cells against electrophiles
    • Mannervik B. Evolution of glutathione transferases and related enzymes for the protection of cells against electrophiles. Biochem. Soc. Trans. 24:1996;878-880.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 878-880
    • Mannervik, B.1
  • 25
    • 0024269217 scopus 로고
    • Glutathione transferases - structure and catalytic activity
    • Mannervik B., Danielson U. H. Glutathione transferases - structure and catalytic activity. CRC Crit. Rev. Biochem. 23:1988;283-337.
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 26
    • 0001306237 scopus 로고
    • Human glutathione transferases: Classification, tissue distribution, structure and functional properties
    • G. M. Pacifici, & G. N. Fracchia. Luxembourg: European Commission
    • Mannervik B., Widersten M. Human glutathione transferases: classification, tissue distribution, structure and functional properties. Pacifici G. M., Fracchia G. N. Advances in Drug Metabolism in Man. 1995;407-459 European Commission, Luxembourg.
    • (1995) Advances in Drug Metabolism in Man , pp. 407-459
    • Mannervik, B.1    Widersten, M.2
  • 27
    • 0000107746 scopus 로고
    • Identification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties
    • Mannervik B., Ålin P., Guthenberg C., Jensson H., Tahir M. K., Warholm M., Jörnvall H. 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. 82:1985;7202-7206.
    • (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    Jörnvall, H.7
  • 29
    • 0028871969 scopus 로고
    • Characterization of rat spleen prostaglandin H D -isomerase as a sigma-class GSH transferase
    • Meyer D. J., Thomas M. Characterization of rat spleen prostaglandin H D -isomerase as a sigma-class GSH transferase. Biochem. J. 311:1995;739-742.
    • (1995) Biochem. J. , vol.311 , pp. 739-742
    • Meyer, D.J.1    Thomas, M.2
  • 31
    • 0029854518 scopus 로고    scopus 로고
    • Glutathione S-transferase class Kappa: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue
    • Pemble S. E., Wardle A. F., Taylor J. B. Glutathione S-transferase class Kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem. J. 319:1996;749-751.
    • (1996) Biochem. J. , vol.319 , pp. 749-751
    • Pemble, S.E.1    Wardle, A.F.2    Taylor, J.B.3
  • 32
    • 0028244183 scopus 로고
    • Crystal structure of human class Mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity
    • Raghunathan S., Chandross R. J., Kretsinger R. H., Allison T. J., Penington C. J., Rule G. S. Crystal structure of human class Mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J. Mol. Biol. 238:1994;815-832.
    • (1994) J. Mol. 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
  • 33
    • 0024854643 scopus 로고
    • 3+-induced neurotoxicity of dopamine: Prevention of quinone-derived oxygen toxicity by DT diaphorase and superoxide dismutase
    • 3+-induced neurotoxicity of dopamine: prevention of quinone-derived oxygen toxicity by DT diaphorase and superoxide dismutase. Chem. Biol. Int. 72:1989;309-324.
    • (1989) Chem. Biol. Int. , vol.72 , pp. 309-324
    • Segura-Aguilar, J.1    Lind, C.2
  • 34
    • 0031041078 scopus 로고    scopus 로고
    • Human class Mu glutathione transferases, in particular isoenzyme M2-2, catalyze detoxication of the dopamine metabolite aminochrome
    • Segura-Aguilar J., Baez S., Widersten M., Welch C., Mannervik B. Human class Mu glutathione transferases, in particular isoenzyme M2-2, catalyze detoxication of the dopamine metabolite aminochrome. J. Biol. Chem. 272:1997;5727-5731.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5727-5731
    • Segura-Aguilar, J.1    Baez, S.2    Widersten, M.3    Welch, C.4    Mannervik, B.5
  • 35
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W. P. C. Rapid evolution of a protein in vitro by DNA shuffling. Nature. 370:1994a;389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 36
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer W. P. C. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl Acad. Sci. USA. 91:1994b;10747-10751.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 37
    • 0025975957 scopus 로고
    • Structure of human glutathione S-transferase class Mu genes
    • Taylor J. B., Oliver J., Sherrington R., Pemble S. E. Structure of human glutathione S-transferase class Mu genes. Biochem. J. 274:1991;587-593.
    • (1991) Biochem. J. , vol.274 , pp. 587-593
    • Taylor, J.B.1    Oliver, J.2    Sherrington, R.3    Pemble, S.E.4
  • 38
    • 0025778535 scopus 로고
    • Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of theGST4 locus
    • Vorachek W. R., Pearson W. R., Rule G. S. Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of theGST4 locus. Proc. Natl Acad. Sci. USA. 88:1991;4443-4447.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4443-4447
    • Vorachek, W.R.1    Pearson, W.R.2    Rule, G.S.3
  • 39
    • 0025812157 scopus 로고
    • Heterologous expression of the allelic variant Mu-class glutathione transferases μ and ψ
    • Widersten M., Pearson W. R., Engström Å., Mannervik B. Heterologous expression of the allelic variant Mu-class glutathione transferases μ and ψ Biochem J. 276:1991;519-524.
    • (1991) Biochem J. , vol.276 , pp. 519-524
    • Widersten, M.1    Pearson, W.R.2    Engström, Å.3    Mannervik, B.4
  • 40
    • 0030175041 scopus 로고    scopus 로고
    • Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNA
    • Widersten M., Huang M., Mannervik B. Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNA. Protein Expres. Purif. 7:1996;367-372.
    • (1996) Protein Expres. Purif. , vol.7 , pp. 367-372
    • Widersten, M.1    Huang, M.2    Mannervik, B.3
  • 41
    • 0013611419 scopus 로고    scopus 로고
    • Characterization of the polymorphic human class mu GSTM1-0 deletion
    • N. P. E. Vermeulen, G. J. Mulder, H. Nieuwenhuyse, W. H. M. Peters, & P. J. van Bladeren. London: Taylor & Francis Ltd
    • Xu S.-J., Pearson W. R. Characterization of the polymorphic human class mu GSTM1-0 deletion. Vermeulen N. P. E., Mulder G. J., Nieuwenhuyse H., Peters W. H. M., van Bladeren P. J. Glutathione S-Transferases. Structure, Function and Clinical Implications. 1996;227-238 Taylor & Francis Ltd, London.
    • (1996) Glutathione S-Transferases. Structure, Function and Clinical Implications , pp. 227-238
    • Xu, S.-J.1    Pearson, W.R.2
  • 42
    • 0032488893 scopus 로고    scopus 로고
    • Characterization of the human class mu glutathione S-transferase gene cluster and the GSTM1 deletion
    • Xu S.-J., Wang Y.-P., Roe B., Pearson W. P. Characterization of the human class mu glutathione S-transferase gene cluster and the GSTM1 deletion. J. Biol. Chem. 273:1998;3517-3527.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3517-3527
    • Xu, S.-J.1    Wang, Y.-P.2    Roe, B.3    Pearson, W.P.4
  • 43
    • 0032510667 scopus 로고    scopus 로고
    • Directed evolution of an aspartate aminotransferase with new substrate specificities
    • Yano T., Oue S., Kagamiyama H. Directed evolution of an aspartate aminotransferase with new substrate specificities. Proc. Natl Acad. Sci. USA. 95:1998;5511-5515.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5511-5515
    • Yano, T.1    Oue, S.2    Kagamiyama, H.3
  • 44
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang J.-H., Dawes G., Stemmer W. P. C. Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl Acad. Sci. USA. 94:1997;4504-4509.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.-H.1    Dawes, G.2    Stemmer, W.P.C.3
  • 45
    • 0026464467 scopus 로고
    • Modular mutagenesis of exons 1, 2, and 8 of a glutathione S-transferase from the mu class. Mechanistic and structural consequences for chimeras of isoenzyme 3-3
    • Zhang P., Liu S., Shan S., Ji X., Gilliland G. L., Armstrong R. N. Modular mutagenesis of exons 1, 2, and 8 of a glutathione S-transferase from the mu class. Mechanistic and structural consequences for chimeras of isoenzyme 3-3. Biochemistry. 31:1992;10185-10193.
    • (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
  • 46
    • 0030858562 scopus 로고    scopus 로고
    • Functional and nonfunctional mutations distinguished by random recombination of homologous genes
    • Zhao H., Arnold F. H. Functional and nonfunctional mutations distinguished by random recombination of homologous genes. Proc. Natl Acad. Sci. USA. 94:1997;7997-8000.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7997-8000
    • Zhao, H.1    Arnold, F.H.2


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