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Volumn 1850, Issue 4, 2015, Pages 742-749

Evolution of the active site of human glutathione transferase A2-2 for enhanced activity with dietary isothiocyanates

Author keywords

Detoxication; Directed evolution; Enzyme engineering; Glutathione transferase; Isothiocyanate

Indexed keywords

ENZYME VARIANT; GLUTATHIONE TRANSFERASE A2; GLUTATHIONE TRANSFERASE A2 2; GLYCINE; HISTIDINE; ISOTHIOCYANIC ACID; MUTANT PROTEIN; UNCLASSIFIED DRUG; GLUTATHIONE S-TRANSFERASE ALPHA; GLUTATHIONE TRANSFERASE; ISOENZYME; ISOTHIOCYANIC ACID DERIVATIVE;

EID: 84921327786     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.12.021     Document Type: Article
Times cited : (11)

References (55)
  • 1
    • 0028326168 scopus 로고
    • Anticarcinogenic activities of organic isothiocyanates: Chemistry and mechanisms
    • Y. Zhang, P. Talalay, Anticarcinogenic activities of organic isothiocyanates: chemistry and mechanisms, Cancer Res. 54 (1994) 1976s-1981s.
    • (1994) Cancer Res. , vol.54 , pp. 1976s-1981s
    • Zhang, Y.1    Talalay, P.2
  • 2
    • 33747419497 scopus 로고    scopus 로고
    • Characterization of two Arabidopsis thaliana glutathione S-transferases
    • E. Nutricati, A. Miceli, F. Blando, L. De Bellis, Characterization of two Arabidopsis thaliana glutathione S-transferases, Plant Cell Rep. 25 (2006) 997-1005.
    • (2006) Plant Cell Rep. , vol.25 , pp. 997-1005
    • Nutricati, E.1    Miceli, A.2    Blando, F.3    De Bellis, L.4
  • 3
    • 16244399219 scopus 로고    scopus 로고
    • Glutathione S-transferases in the adaptation to plant secondary metabolites in the Myzus persicae aphid
    • F. Francis, N. Vanhaelen, E. Haubruge, Glutathione S-transferases in the adaptation to plant secondary metabolites in the Myzus persicae aphid, Arch. Insect Biochem. Physiol. 58 (2005) 166-174.
    • (2005) Arch. Insect Biochem. Physiol. , vol.58 , pp. 166-174
    • Francis, F.1    Vanhaelen, N.2    Haubruge, E.3
  • 4
    • 34547842543 scopus 로고    scopus 로고
    • Novel class of glutathione transferases from cyanobacteria exhibit high catalytic activities towards naturally occurring isothiocyanates
    • E. Wiktelius, G. Stenberg, Novel class of glutathione transferases from cyanobacteria exhibit high catalytic activities towards naturally occurring isothiocyanates, Biochem. J. 406 (2007) 115-123.
    • (2007) Biochem. J. , vol.406 , pp. 115-123
    • Wiktelius, E.1    Stenberg, G.2
  • 5
    • 77955277097 scopus 로고    scopus 로고
    • A novel quasi-species of glutathione transferase with high activity towards naturally occurring isothiocyanates evolves from promiscuous low-activity variants
    • A. Runarsdottir, B. Mannervik, A novel quasi-species of glutathione transferase with high activity towards naturally occurring isothiocyanates evolves from promiscuous low-activity variants, J. Mol. Biol. 401 (2010) 451-464.
    • (2010) J. Mol. Biol. , vol.401 , pp. 451-464
    • Runarsdottir, A.1    Mannervik, B.2
  • 7
    • 0023192524 scopus 로고
    • Peptide quantitative structure-activity relationships, a multivariate approach
    • S. Hellberg, M. Sjostrom, B. Skagerberg, S. Wold, Peptide quantitative structure-activity relationships, a multivariate approach, J. Med. Chem. 30 (1987) 1126-1135.
    • (1987) J. Med. Chem. , vol.30 , pp. 1126-1135
    • Hellberg, S.1    Sjostrom, M.2    Skagerberg, B.3    Wold, S.4
  • 8
    • 0032474777 scopus 로고    scopus 로고
    • New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids
    • M. Sandberg, L. Eriksson, J. Jonsson, M. Sjostrom, S. Wold, New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids, J. Med. Chem. 41 (1998) 2481-2491.
    • (1998) J. Med. Chem. , vol.41 , pp. 2481-2491
    • Sandberg, M.1    Eriksson, L.2    Jonsson, J.3    Sjostrom, M.4    Wold, S.5
  • 9
    • 0035789124 scopus 로고    scopus 로고
    • New quantitative descriptors of amino acids based on multidimensional scaling of a large number of physical-chemical properties
    • W. Braun, M.S. Venkatarajan, New quantitative descriptors of amino acids based on multidimensional scaling of a large number of physical-chemical properties, J. Mol. Model. 7 (2001) 445-453.
    • (2001) J. Mol. Model. , vol.7 , pp. 445-453
    • Braun, W.1    Venkatarajan, M.S.2
  • 10
    • 70350077283 scopus 로고    scopus 로고
    • Identification of emerging quasi-species in directed enzyme evolution
    • S. Kurtovic, B. Mannervik, Identification of emerging quasi-species in directed enzyme evolution, Biochemistry 48 (2009) 9330-9339.
    • (2009) Biochemistry , vol.48 , pp. 9330-9339
    • Kurtovic, S.1    Mannervik, B.2
  • 11
    • 77449106593 scopus 로고    scopus 로고
    • Molecular targets of dietary phenethyl isothiocyanate and sulforaphane for cancer chemoprevention
    • K.L. Cheung, A.N. Kong, Molecular targets of dietary phenethyl isothiocyanate and sulforaphane for cancer chemoprevention, AAPS J. 12 (2010) 87-97.
    • (2010) AAPS J. , vol.12 , pp. 87-97
    • Cheung, K.L.1    Kong, A.N.2
  • 12
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • R. Guerois, J.E. Nielsen, L. Serrano, Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations, J. Mol. Biol. 320 (2002) 369-387.
    • (2002) J. Mol. Biol. , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 14
    • 0029047391 scopus 로고
    • Chemoprevention by isothiocyanates
    • S.S. Hecht, Chemoprevention by isothiocyanates, J. Cell. Biochem. Suppl. 22 (1995) 195-209.
    • (1995) J. Cell. Biochem. Suppl. , vol.22 , pp. 195-209
    • Hecht, S.S.1
  • 15
    • 80054848925 scopus 로고    scopus 로고
    • Mechanisms of action of isothiocyanates in cancer chemoprevention: An update
    • S.L. Navarro, F. Li, J.W. Lampe, Mechanisms of action of isothiocyanates in cancer chemoprevention: an update, Food Funct. 2 (2011) 579-587.
    • (2011) Food Funct. , vol.2 , pp. 579-587
    • Navarro, S.L.1    Li, F.2    Lampe, J.W.3
  • 16
    • 84866122895 scopus 로고    scopus 로고
    • Cancer chemoprevention with dietary isothiocyanates mature for clinical translational research
    • S.V. Singh, K. Singh, Cancer chemoprevention with dietary isothiocyanates mature for clinical translational research, Carcinogenesis 33 (2012) 1833-1842.
    • (2012) Carcinogenesis , vol.33 , pp. 1833-1842
    • Singh, S.V.1    Singh, K.2
  • 18
    • 84861875282 scopus 로고    scopus 로고
    • Glucosinolates and isothiocyanates in health and disease
    • A.T. Dinkova-Kostova, R.V. Kostov, Glucosinolates and isothiocyanates in health and disease, Trends Mol. Med. 18 (2012) 337-347.
    • (2012) Trends Mol. Med. , vol.18 , pp. 337-347
    • Dinkova-Kostova, A.T.1    Kostov, R.V.2
  • 20
    • 84859102919 scopus 로고    scopus 로고
    • Natural isothiocyanates: Genotoxic potential versus chemoprevention
    • C. Fimognari, E. Turrini, L. Ferruzzi, M. Lenzi, P. Hrelia, Natural isothiocyanates: genotoxic potential versus chemoprevention, Mutat. Res. 750 (2012) 107-131.
    • (2012) Mutat. Res. , vol.750 , pp. 107-131
    • Fimognari, C.1    Turrini, E.2    Ferruzzi, L.3    Lenzi, M.4    Hrelia, P.5
  • 21
    • 0035170990 scopus 로고    scopus 로고
    • Phytochemicals fromcruciferous plants protect against cancer by modulating carcinogen metabolism
    • P. Talalay, J.W. Fahey, Phytochemicals fromcruciferous plants protect against cancer by modulating carcinogen metabolism, J. Nutr. 131 (2001) 3027S-3033S.
    • (2001) J. Nutr. , vol.131 , pp. 3027S-3033S
    • Talalay, P.1    Fahey, J.W.2
  • 22
    • 63049134716 scopus 로고    scopus 로고
    • GST polymorphism and excretion of heterocyclic aromatic amine and isothiocyanate metabolites after Brassica consumption
    • S.E. Steck, J.R. Hebert, GST polymorphism and excretion of heterocyclic aromatic amine and isothiocyanate metabolites after Brassica consumption, Environ. Mol. Mutagen. 50 (2009) 238-246.
    • (2009) Environ. Mol. Mutagen. , vol.50 , pp. 238-246
    • Steck, S.E.1    Hebert, J.R.2
  • 23
    • 0028179830 scopus 로고
    • Consumption of Brussels sprouts results in elevated alpha-class glutathione S-transferase levels in human blood plasma
    • J.J. Bogaards, H. Verhagen, M.I. Willems, G. van Poppel, P.J. van Bladeren, Consumption of Brussels sprouts results in elevated alpha-class glutathione S-transferase levels in human blood plasma, Carcinogenesis 15 (1994) 1073-1075.
    • (1994) Carcinogenesis , vol.15 , pp. 1073-1075
    • Bogaards, J.J.1    Verhagen, H.2    Willems, M.I.3    Van Poppel, G.4    Van Bladeren, P.J.5
  • 25
    • 33846153232 scopus 로고    scopus 로고
    • Induction of GST and NQO1 in cultured bladder cells and in the urinary bladders of rats by an extract of broccoli (Brassica oleracea italica) sprouts
    • Y. Zhang, R. Munday, H.E. Jobson, C.M. Munday, C. Lister, P. Wilson, J.W. Fahey, P. Mhawech-Fauceglia, Induction of GST and NQO1 in cultured bladder cells and in the urinary bladders of rats by an extract of broccoli (Brassica oleracea italica) sprouts, J. Agric. Food Chem. 54 (2006) 9370-9376.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 9370-9376
    • Zhang, Y.1    Munday, R.2    Jobson, H.E.3    Munday, C.M.4    Lister, C.5    Wilson, P.6    Fahey, J.W.7    Mhawech-Fauceglia, P.8
  • 26
    • 0036708902 scopus 로고    scopus 로고
    • Antioxidants and oxidants regulated signal transduction pathways
    • E.D. Owuor, A.N. Kong, Antioxidants and oxidants regulated signal transduction pathways, Biochem. Pharmacol. 64 (2002) 765-770.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 765-770
    • Owuor, E.D.1    Kong, A.N.2
  • 27
    • 9644272830 scopus 로고    scopus 로고
    • Protection against electrophile and oxidative stress by induction of phase 2 genes: The quest for the elusive sensor that responds to inducers
    • W.D. Holtzclaw, A.T. Dinkova-Kostova, P. Talalay, Protection against electrophile and oxidative stress by induction of phase 2 genes: the quest for the elusive sensor that responds to inducers, Adv. Enzyme Regul. 44 (2004) 335-367.
    • (2004) Adv. Enzyme Regul. , vol.44 , pp. 335-367
    • Holtzclaw, W.D.1    Dinkova-Kostova, A.T.2    Talalay, P.3
  • 28
    • 0028892567 scopus 로고
    • Isothiocyanates as substrates for human glutathione transferases: Structure-activity studies
    • R.H. Kolm, U.H. Danielson, Y. Zhang, P. Talalay, B. Mannervik, Isothiocyanates as substrates for human glutathione transferases: structure-activity studies, Biochem. J. 311 (1995) 453-459.
    • (1995) Biochem. J. , vol.311 , pp. 453-459
    • Kolm, R.H.1    Danielson, U.H.2    Zhang, Y.3    Talalay, P.4    Mannervik, B.5
  • 29
    • 0028898483 scopus 로고
    • Reversible conjugation of isothiocyanates with glutathione catalyzed by human glutathione transferases
    • Y. Zhang, R.H. Kolm, B. Mannervik, P. Talalay, 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
  • 30
    • 0031711928 scopus 로고    scopus 로고
    • Urinary total isothiocyanate (ITC) in a population-based sample of middle-aged and older Chinese in Singapore: Relationship with dietary total ITC and glutathione S-transferase M1/T1/P1 genotypes
    • A. Seow, C.Y. Shi, F.L. Chung, D. Jiao, J.H. Hankin, H.P. Lee, G.A. Coetzee, M.C. Yu, Urinary total isothiocyanate (ITC) in a population-based sample of middle-aged and older Chinese in Singapore: relationship with dietary total ITC and glutathione S-transferase M1/T1/P1 genotypes, Cancer Epidemiol. Biomarkers Prev. 7 (1998) 775-781.
    • (1998) Cancer Epidemiol. Biomarkers Prev. , vol.7 , pp. 775-781
    • Seow, A.1    Shi, C.Y.2    Chung, F.L.3    Jiao, D.4    Hankin, J.H.5    Lee, H.P.6    Coetzee, G.A.7    Yu, M.C.8
  • 31
    • 34247370640 scopus 로고    scopus 로고
    • Location and volume of the active site of chymotrypsin
    • P.V. Kostetsky, Location and volume of the active site of chymotrypsin, Biochem. Biokhim. 72 (2007) 392-397.
    • (2007) Biochem. Biokhim. , vol.72 , pp. 392-397
    • Kostetsky, P.V.1
  • 32
    • 79954510706 scopus 로고    scopus 로고
    • Altered architecture of substrate binding region defines the unique specificity of UDP-GalNAc 4-epimerases
    • V.S. Bhatt, C.Y. Guo, W. Guan, G. Zhao, W. Yi, Z.J. Liu, P.G. Wang, Altered architecture of substrate binding region defines the unique specificity of UDP-GalNAc 4-epimerases, Protein Sci. 20 (2011) 856-866.
    • (2011) Protein Sci. , vol.20 , pp. 856-866
    • Bhatt, V.S.1    Guo, C.Y.2    Guan, W.3    Zhao, G.4    Yi, W.5    Liu, Z.J.6    Wang, P.G.7
  • 33
    • 84858964863 scopus 로고    scopus 로고
    • Structure-based redesign of GST A2-2 for enhanced catalytic efficiency with azathioprine
    • W. Zhang, O. Moden, K. Tars, B. Mannervik, Structure-based redesign of GST A2-2 for enhanced catalytic efficiency with azathioprine, Chem. Biol. 19 (2012) 414-421.
    • (2012) Chem. Biol. , vol.19 , pp. 414-421
    • Zhang, W.1    Moden, O.2    Tars, K.3    Mannervik, B.4
  • 35
    • 77956234144 scopus 로고    scopus 로고
    • Natural diversity to guide focused directed evolution
    • H. Jochens, U.T. Bornscheuer, Natural diversity to guide focused directed evolution, ChemBioChem 11 (2010) 1861-1866.
    • (2010) ChemBioChem , vol.11 , pp. 1861-1866
    • Jochens, H.1    Bornscheuer, U.T.2
  • 36
    • 84873823168 scopus 로고    scopus 로고
    • Evolution of broad spectrum beta-lactam resistance in an engineered metallo-beta-lactamase
    • S. Sun, W. Zhang, B. Mannervik, D.I. Andersson, Evolution of broad spectrum beta-lactam resistance in an engineered metallo-beta-lactamase, J. Biol. Chem. 288 (2013) 2314-2324.
    • (2013) J. Biol. Chem. , vol.288 , pp. 2314-2324
    • Sun, S.1    Zhang, W.2    Mannervik, B.3    Andersson, D.I.4
  • 37
  • 38
    • 82755163096 scopus 로고    scopus 로고
    • Ensemble perspective for catalytic promiscuity: Calorimetric analysis of the active site conformational landscape of a detoxification enzyme
    • M.T. Honaker, M. Acchione, J.P. Sumida, W.M. Atkins, Ensemble perspective for catalytic promiscuity: calorimetric analysis of the active site conformational landscape of a detoxification enzyme, J. Biol. Chem. 286 (2011) 42770-42776.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42770-42776
    • Honaker, M.T.1    Acchione, M.2    Sumida, J.P.3    Atkins, W.M.4
  • 39
    • 84880052696 scopus 로고    scopus 로고
    • Enzymatic detoxication, conformational selection, and the role of molten globule active sites
    • M.T. Honaker, M. Acchione, W. Zhang, B. Mannervik, W.M. Atkins, Enzymatic detoxication, conformational selection, and the role of molten globule active sites, J. Biol. Chem. 288 (2013) 18599-18611.
    • (2013) J. Biol. Chem. , vol.288 , pp. 18599-18611
    • Honaker, M.T.1    Acchione, M.2    Zhang, W.3    Mannervik, B.4    Atkins, W.M.5
  • 40
    • 0029008514 scopus 로고
    • Glutathione transferases with novel active sites isolated by phage display froma library of random mutants
    • M. Widersten, B. Mannervik, Glutathione transferases with novel active sites isolated by phage display froma library of random mutants, J. Mol. Biol. 250 (1995) 115-122.
    • (1995) J. Mol. Biol. , vol.250 , pp. 115-122
    • Widersten, M.1    Mannervik, B.2
  • 41
    • 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
    • A. Shokeer, A.K. Larsson, B. Mannervik, 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
  • 42
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • N. Tokuriki, D.S. Tawfik, Chaperonin overexpression promotes genetic variation and enzyme evolution, Nature 459 (2009) 668-673.
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 43
    • 55049084123 scopus 로고    scopus 로고
    • Glutathione transferase: New model for glutathione activation
    • D.F. Dourado, P.A. Fernandes, B. Mannervik, M.J. Ramos, Glutathione transferase: new model for glutathione activation, Chem. Eur. J. 14 (2008) 9591-9598.
    • (2008) Chem. Eur. J. , vol.14 , pp. 9591-9598
    • Dourado, D.F.1    Fernandes, P.A.2    Mannervik, B.3    Ramos, M.J.4
  • 45
    • 11144347566 scopus 로고    scopus 로고
    • Development and testing of a general amber force field (vol 25, pg 1157- 1174, 2004)
    • J.M. Wang, R.M. Wolf, J.W. Caldwell, P.A. Kollman, D.A. Case, Development and testing of a general amber force field (vol 25, pg 1157- 1174, 2004), J. Comp. Chem. 26 (2005) 114.
    • (2005) J. Comp. Chem. , vol.26 , pp. 114
    • Wang, J.M.1    Wolf, R.M.2    Caldwell, J.W.3    Kollman, P.A.4    Case, D.A.5
  • 48
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals - A new molecular-dynamics method
    • M. Parrinello, A. Rahman, Polymorphic transitions in single-crystals - a new molecular-dynamics method, J. Appl. Phys. 52 (1981) 7182-7190.
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 50
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • B. Hess, H. Bekker, H. Berendsen, J. Fraaije, LINCS: a linear constraint solver for molecular simulations, J. Comp. Chem. 18 (1997) 1463-1472.
    • (1997) J. Comp. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.3    Fraaije, J.4
  • 51
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • E. Lindahl, B. Hess, D. Van der Spoel, GROMACS 3.0: a package for molecular simulation and trajectory analysis, J. Mol. Model. 7 (2001) 306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 52
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • E.J. Sorin, V.S. Pande, Exploring the helix-coil transition via all-atom equilibrium ensemble simulations, Biophys. J. 88 (2005) 2472-2493.
    • (2005) Biophys. J. , vol.88 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2


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