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Volumn 15, Issue 4, 2004, Pages 718-727

Combinatorial chemical reengineering of the alpha class glutathione transferases

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL MODIFICATION; CHEMICAL REACTIONS; ENZYMES; PEPTIDES;

EID: 3242760692     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc034192+     Document Type: Article
Times cited : (11)

References (45)
  • 2
    • 0035471134 scopus 로고    scopus 로고
    • Enzyme redesign
    • Penning, T. M., and Jez, J. M. (2001) Enzyme redesign. Chem. Rev. 101, 3027-3046.
    • (2001) Chem. Rev. , vol.101 , pp. 3027-3046
    • Penning, T.M.1    Jez, J.M.2
  • 3
  • 4
    • 0033791659 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • Hilvert, D. (2000) Critical analysis of antibody catalysis. Annu. Rev. Biochem. 69, 751-793.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 751-793
    • Hilvert, D.1
  • 6
    • 0035471137 scopus 로고    scopus 로고
    • Generation of new enzymes via covalent modification of existing proteins
    • Qi, D., Tann, C. M., Haring, D., and Distefano, M. D. (2001) Generation of new enzymes via covalent modification of existing proteins. Chem. Rev. 101, 3081-3111.
    • (2001) Chem. Rev. , vol.101 , pp. 3081-3111
    • Qi, D.1    Tann, C.M.2    Haring, D.3    Distefano, M.D.4
  • 7
    • 0035989963 scopus 로고    scopus 로고
    • A semisynthetic glutathione peroxidase with high catalytic efficiency. Selenoglutathione transferase
    • Ren, X., Jemth, P., Board, P. G., Luo, G., Mannervik, B., Liu, J., Zhang, K., and Shen, J. (2002) A semisynthetic glutathione peroxidase with high catalytic efficiency. Selenoglutathione transferase. Chem. Biol. 9, 789-794.
    • (2002) Chem. Biol. , vol.9 , pp. 789-794
    • Ren, X.1    Jemth, P.2    Board, P.G.3    Luo, G.4    Mannervik, B.5    Liu, J.6    Zhang, K.7    Shen, J.8
  • 8
    • 0033178813 scopus 로고    scopus 로고
    • Chemical modification of enzymes for enhanced functionality
    • DeSantis, G., and Jones, J. B. (1999) Chemical modification of enzymes for enhanced functionality. Curr. Opin. Biotechnol. 10, 324-330.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 324-330
    • DeSantis, G.1    Jones, J.B.2
  • 9
    • 0031281620 scopus 로고    scopus 로고
    • Incorporation of an artificial receptor into a native protein: New strategy for the design of semisynthetic enzymes with allosteric properties
    • Hamachi, I., Nagase, T., Tajiri, Y., and Shinkai, S. (1997) Incorporation of an artificial receptor into a native protein: new strategy for the design of semisynthetic enzymes with allosteric properties. Bioconjugate Chem. 8, 862-868.
    • (1997) Bioconjugate Chem. , vol.8 , pp. 862-868
    • Hamachi, I.1    Nagase, T.2    Tajiri, Y.3    Shinkai, S.4
  • 10
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of nonmammalian members of an ancient enzyme superfamily
    • Sheehan, D., Meade, G., Foley, V. M., and Dowd, C. A. (2001) Structure, function and evolution of glutathione transferases: implications for classification of nonmammalian members of an ancient enzyme superfamily. Biochem. J. 360, 1-16.
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 12
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong, R. N. (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10, 2-18.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 13
    • 0029840092 scopus 로고    scopus 로고
    • Evolution of glutathione transferases and related enzymes for the protection of cells against electrophiles
    • Mannervik, B. (1996) Evolution of glutathione transferases and related enzymes for the protection of cells against electrophiles. Biochem. Soc. Trans. 24, 878-880.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 878-880
    • Mannervik, B.1
  • 14
    • 0035894563 scopus 로고    scopus 로고
    • Heterodimers of glutathione S-transferase can form between isoenzyme classes pi and mu
    • Pettigrew, N. E., and Colman, R. F. (2001) Heterodimers of glutathione S-transferase can form between isoenzyme classes pi and mu. Arch. Biochem. Biophys. 396, 225-230.
    • (2001) Arch. Biochem. Biophys. , vol.396 , pp. 225-230
    • Pettigrew, N.E.1    Colman, R.F.2
  • 15
    • 0027209602 scopus 로고
    • Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes
    • Sinning, I., Kleywegt, G. J., Cowan, S. W., Reinemer, P., Dirr, H. W., Huber, R., Gilliland, G. L., Armstrong, R. N., Ji, X., Board, P. G., and et al. (1993) Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J. Mol. Biol. 232, 192-212.
    • (1993) J. Mol. Biol. , vol.232 , pp. 192-212
    • Sinning, I.1    Kleywegt, G.J.2    Cowan, S.W.3    Reinemer, P.4    Dirr, H.W.5    Huber, R.6    Gilliland, G.L.7    Armstrong, R.N.8    Ji, X.9    Board, P.G.10
  • 16
    • 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., and Pulford, D. J. (1995) 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, 445-600.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 17
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV
    • Lim, K., Ho, J. X., Keeling, K., Gilliland, G. L., Ji, X., Ruker, F., and Carter, D. C. (1994) Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 3, 2233-2244.
    • (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    Ruker, F.6    Carter, D.C.7
  • 18
    • 0035950458 scopus 로고    scopus 로고
    • A bird's eye view of the glutathione transferase field
    • Ketterer, B. (2001) A bird's eye view of the glutathione transferase field. Chem. Biol. Interact. 138, 27-42.
    • (2001) Chem. Biol. Interact. , vol.138 , pp. 27-42
    • Ketterer, B.1
  • 21
    • 0037119451 scopus 로고    scopus 로고
    • Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase
    • Pettersson, P. L., Johansson, A. S., and Mannervik, B. (2002) Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase. J. Biol. Chem. 277, 30019-30022.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30019-30022
    • Pettersson, P.L.1    Johansson, A.S.2    Mannervik, B.3
  • 22
    • 0033751393 scopus 로고    scopus 로고
    • Use of phage display and transition-state analogues to select enzyme variants with altered catalytic properties: Glutathione transferase as an example
    • Widersten, M., Hansson, L. O., Tronstad, L., and Mannervik, B. (2000) Use of phage display and transition-state analogues to select enzyme variants with altered catalytic properties: glutathione transferase as an example. Methods Enzymol. 328, 389-404.
    • (2000) Methods Enzymol. , vol.328 , pp. 389-404
    • Widersten, M.1    Hansson, L.O.2    Tronstad, L.3    Mannervik, B.4
  • 23
    • 0034662931 scopus 로고    scopus 로고
    • Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation
    • Nilsson, L. O., Gustafsson, A., and Mannervik, B. (2000) Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation. Proc. Natl. Acad. Sci. U.S.A. 97, 9408-9412.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9408-9412
    • Nilsson, L.O.1    Gustafsson, A.2    Mannervik, B.3
  • 24
    • 0033751372 scopus 로고    scopus 로고
    • Use of chimeras generated by DNA shuffling: Probing structure-function relationships among glutathione transferases
    • Hansson, L. O., and Mannervik, B. (2000) Use of chimeras generated by DNA shuffling: probing structure-function relationships among glutathione transferases. Methods Enzymol. 328, 463-477.
    • (2000) Methods Enzymol. , vol.328 , pp. 463-477
    • Hansson, L.O.1    Mannervik, B.2
  • 25
    • 0033571041 scopus 로고    scopus 로고
    • An approach to optimizing the active site in a glutathione transferase by evolution in vitro
    • Hansson, L. O., Widersten, M., and Mannervik, B. (1999) An approach to optimizing the active site in a glutathione transferase by evolution in vitro. Biochem. J. 344 Pt 1, 93-100.
    • (1999) Biochem. J. , vol.344 , Issue.PART 1 , pp. 93-100
    • Hansson, L.O.1    Widersten, M.2    Mannervik, B.3
  • 27
    • 0042825474 scopus 로고    scopus 로고
    • Programmed delivery of novel functional groups to the alpha class glutathione transferases
    • Häkansson, S., Viljanen, J., Broo, K. S. (2003) Programmed delivery of novel functional groups to the alpha class glutathione transferases. Biochemistry 42, 10260-10268.
    • (2003) Biochemistry , vol.42 , pp. 10260-10268
    • Häkansson, S.1    Viljanen, J.2    Broo, K.S.3
  • 28
    • 0031439169 scopus 로고    scopus 로고
    • A semisynthetic metalloenzyme based on a protein cavity that catalyzes the enantioselective hydrolysis of ester and amide substrates
    • Davies, R. R., and Distefano, M. D. (1997) A semisynthetic metalloenzyme based on a protein cavity that catalyzes the enantioselective hydrolysis of ester and amide substrates. J. Am. Chem. Soc. 119, 11643-11652.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11643-11652
    • Davies, R.R.1    Distefano, M.D.2
  • 29
    • 0242449394 scopus 로고    scopus 로고
    • Enzymes by design: Chemogenetic assembly of transamination active sites containing lysine residues for covalent catalysis
    • Haring, D., and Distefano, M. D. (2001) Enzymes by design: chemogenetic assembly of transamination active sites containing lysine residues for covalent catalysis. Bioconjug. Chem. 12, 385-390.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 385-390
    • Haring, D.1    Distefano, M.D.2
  • 30
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser, E., Colescott, R. L., Bossinger, C. D., and Cook, P. I. (1970) Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 34, 595-598.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 31
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 32
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione S-transferases
    • Habig, W. H., and Jakoby, W. B. (1981) Assays for differentiation of glutathione S-transferases. Methods Enzymol. 77, 398-405.
    • (1981) Methods Enzymol. , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 33
    • 0033045871 scopus 로고    scopus 로고
    • Benzoic acid derivatives induce recovery of catalytic activity in the partially inactive Met208Lys mutant of human glutathione transferase, A1-1
    • Gustafsson, A., and Mannervik, B. (1999) Benzoic acid derivatives induce recovery of catalytic activity in the partially inactive Met208Lys mutant of human glutathione transferase A1-1. J. Mol. Biol. 288, 787-800.
    • (1999) J. Mol. Biol. , vol.288 , pp. 787-800
    • Gustafsson, A.1    Mannervik, B.2
  • 34
    • 0035853725 scopus 로고    scopus 로고
    • The role of glutathione in the isomerization of delta 5-androstene-3, 17-dione catalyzed by human glutathione transferase, A1-1
    • Pettersson, P. L., and Mannervik, B. (2001) The role of glutathione in the isomerization of delta 5-androstene-3, 17-dione catalyzed by human glutathione transferase A1-1. J. Biol. Chem. 276, 11698-704.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11698-11704
    • Pettersson, P.L.1    Mannervik, B.2
  • 35
    • 0035980083 scopus 로고    scopus 로고
    • Human glutathione transferase, A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones
    • Johansson, A. S., and Mannervik, B. (2001) Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J. Biol. Chem. 276, 33061-5.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33061-33065
    • Johansson, A.S.1    Mannervik, B.2
  • 37
    • 0037053335 scopus 로고    scopus 로고
    • Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3
    • Johansson, A. S., and Mannervik, B. (2002) Active-site Residues Governing High Steroid Isomerase Activity in Human Glutathione Transferase A3-3. J. Biol. Chem. 277, 16648-54.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16648-16654
    • Johansson, A.S.1    Mannervik, B.2
  • 39
    • 0032519517 scopus 로고    scopus 로고
    • Human glutathione transferase A4-4: An alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation
    • Hubatsch, I., Ridderstrom, M., and Mannervik, B. (1998) Human glutathione transferase A4-4: An alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation. Biochem. J. 330 (Pt 1), 175-9.
    • (1998) Biochem. J. , vol.330 , Issue.PART 1 , pp. 175-179
    • Hubatsch, I.1    Ridderstrom, M.2    Mannervik, B.3
  • 40
    • 0034052843 scopus 로고    scopus 로고
    • Probing subunit interactions in alpha class rat liver glutathione S-transferase with the photoaffinity label glutathionyl S-[4-(succinimidyl) benzophenone]
    • Wang, J., Bauman, S., and Colman, R. F. (2000) Probing subunit interactions in alpha class rat liver glutathione S-transferase with the photoaffinity label glutathionyl S-[4-(succinimidyl)benzophenone]. J. Biol. Chem. 275, 5493-503.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5493-5503
    • Wang, J.1    Bauman, S.2    Colman, R.F.3
  • 41
    • 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
    • Bruns, C. M., Hubatsch, I., Ridderstrom, M., Mannervik, B., and Tainer, J. A. (1999) Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. J. Mol. Biol. 288, 427-39.
    • (1999) J. Mol. Biol. , vol.288 , pp. 427-439
    • Bruns, C.M.1    Hubatsch, I.2    Ridderstrom, M.3    Mannervik, B.4    Tainer, J.A.5
  • 42
    • 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., and Jones, T. A. (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, 717-27.
    • (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
  • 43
    • 0035014185 scopus 로고    scopus 로고
    • Directed evolution of proteins by exon shuffling
    • Kolkman, J. A., and Stemmer, W. P. (2001) Directed evolution of proteins by exon shuffling. Nat. Biotechnol. 19, 423-8.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 423-428
    • Kolkman, J.A.1    Stemmer, W.P.2
  • 44
    • 3242799265 scopus 로고    scopus 로고
    • http://chemfinder.cambridgesoft.com/result.asp.
  • 45
    • 3242782054 scopus 로고    scopus 로고
    • CompuDrug, I., Inc. (1995), 705, Grandview Drive, South San Francisco, CA 94080
    • CompuDrug, I., Inc. (1995), 705, Grandview Drive, South San Francisco, CA 94080.


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