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Volumn 1780, Issue 12, 2008, Pages 1458-1463

Emergence of a novel highly specific and catalytically efficient enzyme from a naturally promiscuous glutathione transferase

Author keywords

Multivariate data analysis; Protein evolution; Rational design; Substrate selectivity

Indexed keywords

ANDROSTENEDIONE; CUMENE; CUMENE HYDROPEROXIDE; ETACRYNIC ACID; GIMFHELIX ENZYME; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE A1; GLUTATHIONE TRANSFERASE A4; HYDROPEROXIDE; PHENETHYL ISOTHIOCYANATE; UNCLASSIFIED DRUG;

EID: 52949090842     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.07.007     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0000263297 scopus 로고
    • Bar duplication
    • Muller H.J. Bar duplication. Science 83 (1936) 528-530
    • (1936) Science , vol.83 , pp. 528-530
    • Muller, H.J.1
  • 2
    • 0017771466 scopus 로고
    • Evolution and tinkering
    • Jacob F. Evolution and tinkering. Science 196 (1977) 1161-1166
    • (1977) Science , vol.196 , pp. 1161-1166
    • Jacob, F.1
  • 3
    • 52949151925 scopus 로고    scopus 로고
    • Combinatorial protein chemistry in three dimensions: a paradigm for the evolution of glutathione transferases with novel activities
    • Awasthi Y.C. (Ed), CRC Taylor and Francis Boca Raton
    • Ivarsson Y., and Mannervik B. Combinatorial protein chemistry in three dimensions: a paradigm for the evolution of glutathione transferases with novel activities. In: Awasthi Y.C. (Ed). Toxicology of Glutathione Transferases (2006), CRC Taylor and Francis Boca Raton 47-69
    • (2006) Toxicology of Glutathione Transferases , pp. 47-69
    • Ivarsson, Y.1    Mannervik, B.2
  • 4
    • 34247874698 scopus 로고    scopus 로고
    • Current topics in genome evolution: molecular mechanisms of new gene formation
    • Babushok D.V., Ostertag E.M., and Kazazian Jr. H.H. Current topics in genome evolution: molecular mechanisms of new gene formation. Cell Mol. Life Sci. 64 (2007) 542-554
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 542-554
    • Babushok, D.V.1    Ostertag, E.M.2    Kazazian Jr., H.H.3
  • 5
    • 19544365689 scopus 로고    scopus 로고
    • Residue 234 in glutathione transferase T1-1 plays a pivotal role in the catalytic activity and the selectivity against alternative substrates
    • Shokeer A., Larsson A.K., and Mannervik B. Residue 234 in glutathione transferase T1-1 plays a pivotal role in the catalytic activity and the selectivity against alternative substrates. Biochem. J. 388 (2005) 387-392
    • (2005) Biochem. J. , vol.388 , pp. 387-392
    • Shokeer, A.1    Larsson, A.K.2    Mannervik, B.3
  • 6
    • 0037424257 scopus 로고    scopus 로고
    • Identification of residues in glutathione transferase capable of driving functional diversification in evolution
    • Ivarsson Y., Mackey A.J., Edalat M., Pearson W.R., and Mannervik B. Identification of residues in glutathione transferase capable of driving functional diversification in evolution. J. Biol. Chem. 278 (2003) 8733-8738
    • (2003) J. Biol. Chem. , vol.278 , pp. 8733-8738
    • Ivarsson, Y.1    Mackey, A.J.2    Edalat, M.3    Pearson, W.R.4    Mannervik, B.5
  • 7
    • 0033605826 scopus 로고    scopus 로고
    • Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling
    • Hansson L.O., Bolton-Grob R., Massoud T., and Mannervik B. Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling. J. Mol. Biol. 287 (1999) 265-276
    • (1999) J. Mol. Biol. , vol.287 , pp. 265-276
    • Hansson, L.O.1    Bolton-Grob, R.2    Massoud, T.3    Mannervik, B.4
  • 8
    • 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.J., and 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.J.4    Mannervik, B.5
  • 9
    • 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., and 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
  • 10
    • 0021107919 scopus 로고
    • Molecular and catalytic properties of glutathione transferase μ from human liver: an enzyme efficiently conjugating epoxides
    • Warholm M., Guthenberg C., and Mannervik B. Molecular and catalytic properties of glutathione transferase μ from human liver: an enzyme efficiently conjugating epoxides. Biochemistry 22 (1983) 3610-3617
    • (1983) Biochemistry , vol.22 , pp. 3610-3617
    • Warholm, M.1    Guthenberg, C.2    Mannervik, B.3
  • 11
    • 33645529663 scopus 로고    scopus 로고
    • Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution
    • Norrgård M.A., Ivarsson Y., Tars K., and Mannervik B. Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 4876-4881
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4876-4881
    • Norrgård, M.A.1    Ivarsson, Y.2    Tars, K.3    Mannervik, B.4
  • 12
    • 40849124503 scopus 로고    scopus 로고
    • The molecular basis of host adaptation in cactophilic Drosophila: molecular evolution of a glutathione S-transferase gene (GstD1) in Drosophila mojavensis
    • Matzkin L.M. The molecular basis of host adaptation in cactophilic Drosophila: molecular evolution of a glutathione S-transferase gene (GstD1) in Drosophila mojavensis. Genetics 178 (2008) 1073-1083
    • (2008) Genetics , vol.178 , pp. 1073-1083
    • Matzkin, L.M.1
  • 13
    • 37249085022 scopus 로고    scopus 로고
    • Molecular evolution of glutathione S-transferases in the genus Drosophila
    • Low W.Y., Ng H.L., Morton C.J., Parker M.W., Batterham P., and Robin C. Molecular evolution of glutathione S-transferases in the genus Drosophila. Genetics 177 (2007) 1363-1375
    • (2007) Genetics , vol.177 , pp. 1363-1375
    • Low, W.Y.1    Ng, H.L.2    Morton, C.J.3    Parker, M.W.4    Batterham, P.5    Robin, C.6
  • 14
    • 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., Ridderström M., and Mannervik B. 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 (1998) 175-179
    • (1998) Biochem. J. , vol.330 , pp. 175-179
    • Hubatsch, I.1    Ridderström, M.2    Mannervik, B.3
  • 15
    • 0022534948 scopus 로고
    • Rat glutathione transferase 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals
    • Jensson H., Guthenberg C., Ålin P., and Mannervik B. Rat glutathione transferase 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals. FEBS Lett. 203 (1986) 207-209
    • (1986) FEBS Lett. , vol.203 , pp. 207-209
    • Jensson, H.1    Guthenberg, C.2    Ålin, P.3    Mannervik, B.4
  • 16
    • 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. 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 (2000) 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
  • 17
    • 37549056237 scopus 로고    scopus 로고
    • Structural determinants of glutathione transferases with azathioprine activity identified by DNA shuffling of alpha class members
    • Kurtovic S., Modén O., Shokeer A., and Mannervik B. Structural determinants of glutathione transferases with azathioprine activity identified by DNA shuffling of alpha class members. J. Mol. Biol. 375 (2008) 1365-1379
    • (2008) J. Mol. Biol. , vol.375 , pp. 1365-1379
    • Kurtovic, S.1    Modén, O.2    Shokeer, A.3    Mannervik, B.4
  • 18
    • 78049357148 scopus 로고    scopus 로고
    • Measurement of glutathione transferases
    • Maines M.D., Costa L.G., Reed D.J., Sassa S., and Sipes I.G. (Eds), Wiley, New York
    • Mannervik B., and Jemth P. Measurement of glutathione transferases. In: Maines M.D., Costa L.G., Reed D.J., Sassa S., and Sipes I.G. (Eds). in Current Protocols in Toxicology (1999), Wiley, New York 6.4.1-6.4.10
    • (1999) in Current Protocols in Toxicology
    • Mannervik, B.1    Jemth, P.2
  • 19
    • 40849083515 scopus 로고    scopus 로고
    • Glutathione transferase activity with a novel substrate mimics the activation of the prodrug azathioprine
    • Kurtovic S., Grehn L., Karlsson A., Hellman U., and Mannervik B. Glutathione transferase activity with a novel substrate mimics the activation of the prodrug azathioprine. Anal. Biochem. 375 (2008) 339-344
    • (2008) Anal. Biochem. , vol.375 , pp. 339-344
    • Kurtovic, S.1    Grehn, L.2    Karlsson, A.3    Hellman, U.4    Mannervik, B.5
  • 20
    • 0028898483 scopus 로고
    • Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases
    • Zhang Y., Kolm R.H., Mannervik B., and Talalay P. Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases. Biochem. Biophys. Res. Commun. 206 (1995) 748-755
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 748-755
    • Zhang, Y.1    Kolm, R.H.2    Mannervik, B.3    Talalay, P.4
  • 22
    • 0027934013 scopus 로고
    • Human glutathione transferase catalysis of the formation of S-nitrosoglutathione from organic nitrites plus glutathione
    • Meyer D.J., Kramer H., and Ketterer B. Human glutathione transferase catalysis of the formation of S-nitrosoglutathione from organic nitrites plus glutathione. FEBS Lett. 351 (1994) 427-428
    • (1994) FEBS Lett. , vol.351 , pp. 427-428
    • Meyer, D.J.1    Kramer, H.2    Ketterer, B.3
  • 24
    • 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. Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase. J. Biol. Chem. 277 (2002) 30019-30022
    • (2002) J. Biol. Chem. , vol.277 , pp. 30019-30022
    • Pettersson, P.L.1    Johansson, A.S.2    Mannervik, B.3
  • 28
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen R.A. Enzyme recruitment in evolution of new function. Annu. Rev. Microbiol. 30 (1976) 409-425
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 30
    • 0025611278 scopus 로고
    • The enzymes of detoxication
    • Jakoby W.B., and Ziegler D.M. The enzymes of detoxication. J. Biol. Chem. 265 (1990) 20715-20718
    • (1990) J. Biol. Chem. , vol.265 , pp. 20715-20718
    • Jakoby, W.B.1    Ziegler, D.M.2
  • 31
    • 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., Ridderström M., Mannervik B., and Tainer J.A. 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 (1999) 427-439
    • (1999) J. Mol. Biol. , vol.288 , pp. 427-439
    • Bruns, C.M.1    Hubatsch, I.2    Ridderström, M.3    Mannervik, B.4    Tainer, J.A.5
  • 33
    • 0000535586 scopus 로고
    • Multiple forms of enzymes: tissue, ontogenetic, and species specific patterns
    • Market C.L., and Möller P. Multiple forms of enzymes: tissue, ontogenetic, and species specific patterns. Proc. Natl. Acad. Sci. U. S. A. 45 (1959) 753-763
    • (1959) Proc. Natl. Acad. Sci. U. S. A. , vol.45 , pp. 753-763
    • Market, C.L.1    Möller, P.2
  • 34
    • 37049236727 scopus 로고
    • Nature and development of lactic dehydrogenases: the two major types of this enzyme form molecular hybrids which change in makeup during development
    • Cahn R.D., Zwilling E., Kaplan N.O., and Levine L. Nature and development of lactic dehydrogenases: the two major types of this enzyme form molecular hybrids which change in makeup during development. Science 136 (1962) 962-969
    • (1962) Science , vol.136 , pp. 962-969
    • Cahn, R.D.1    Zwilling, E.2    Kaplan, N.O.3    Levine, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.