메뉴 건너뛰기




Volumn 374, Issue 3, 2003, Pages 731-737

Clarification of the role of key active site residues of glutathione transferase Zeta/maleylacetoacetate isomerase by a new spectrophotometric technique

Author keywords

Catalysis; Glutathione transferase (GST); Maleylacetate isomerase (MAAI); Site directed mutagenesis; Spectrophotometry; Zeta class glutathione transferase

Indexed keywords

CARBOXYLIC ACIDS; CATALYSIS; METABOLISM; MUTAGENESIS; REACTION KINETICS; SPECTROPHOTOMETRY;

EID: 0141679076     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030625     Document Type: Article
Times cited : (34)

References (37)
  • 1
    • 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. and Jermiin, L. S. (1997) Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 328, 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
  • 2
    • 0040942636 scopus 로고    scopus 로고
    • Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue
    • Fernandez-Canon, J. M. and Penalva, M. A. (1998) Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue. J. Biol. Chem. 273, 329-337
    • (1998) J. Biol. Chem. , vol.273 , pp. 329-337
    • Fernandez-Canon, J.M.1    Penalva, M.A.2
  • 3
    • 0031741776 scopus 로고    scopus 로고
    • Glutathione transferase Zeta-catalyzed biotransformation of dichloroacetic acid and other alpha-haloacids
    • Tong, Z., Board, P. G. and Anders, M. W. (1998) Glutathione transferase Zeta-catalyzed biotransformation of dichloroacetic acid and other alpha-haloacids. Chem. Res. Toxicol. 11, 1332-1338
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 1332-1338
    • Tong, Z.1    Board, P.G.2    Anders, M.W.3
  • 4
    • 0032522741 scopus 로고    scopus 로고
    • Glutathione transferase Zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid
    • Tong, Z., Board, P. G. and Anders, M. W. (1998) Glutathione transferase Zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid. Biochem. J. 331, 371-374
    • (1998) Biochem. J. , vol.331 , pp. 371-374
    • Tong, Z.1    Board, P.G.2    Anders, M.W.3
  • 5
    • 0025005335 scopus 로고
    • Liver tumor induction in B6C3F1 mice by dichloroacetate and trichloroacetate
    • Bull, R. J., Sanchez, I. M., Nelson, M. A., Larson, J. L. and Lansing, A. J. (1990) Liver tumor induction in B6C3F1 mice by dichloroacetate and trichloroacetate. Toxicology 63, 341-359
    • (1990) Toxicology , vol.63 , pp. 341-359
    • Bull, R.J.1    Sanchez, I.M.2    Nelson, M.A.3    Larson, J.L.4    Lansing, A.J.5
  • 6
    • 0030592952 scopus 로고    scopus 로고
    • The carcinogenicity of dichloroacetic acid in the male Fischer 344 rat
    • DeAngelo, A. B., Daniel, F. B., Most, B. M. and Olson, G. R. (1996) The carcinogenicity of dichloroacetic acid in the male Fischer 344 rat. Toxicology 114, 207-221
    • (1996) Toxicology , vol.114 , pp. 207-221
    • DeAngelo, A.B.1    Daniel, F.B.2    Most, B.M.3    Olson, G.R.4
  • 7
    • 0032579746 scopus 로고    scopus 로고
    • Mutagenicity of three disinfection by-products: di- and trichloroacetic acid and chloral hydrate in L5178Y/TK +/-(-)3.7.2C mouse lymphoma cells
    • Harrington-Brock, K., Doerr, C. L. and Moore, M. M. (1998) Mutagenicity of three disinfection by-products: di- and trichloroacetic acid and chloral hydrate in L5178Y/TK +/-(-)3.7.2C mouse lymphoma cells. Mutat. Res. 413, 265-276
    • (1998) Mutat. Res. , vol.413 , pp. 265-276
    • Harrington-Brock, K.1    Doerr, C.L.2    Moore, M.M.3
  • 8
    • 0031879943 scopus 로고    scopus 로고
    • Effect of dichloroacetic acid and trichloroacetic acid on DNA methylation in liver and tumors of female B6C3F1 mice
    • Tao, L., Kramer, P. M., Ge, R. and Pereira, M. A. (1998) Effect of dichloroacetic acid and trichloroacetic acid on DNA methylation in liver and tumors of female B6C3F1 mice. Toxicol. Sci. 43, 139-144
    • (1998) Toxicol. Sci. , vol.43 , pp. 139-144
    • Tao, L.1    Kramer, P.M.2    Ge, R.3    Pereira, M.A.4
  • 11
    • 0035852844 scopus 로고    scopus 로고
    • Crystal structure of maleylacetoacetate isomerase/glutathione transferase Zeta reveals the molecular basis for its remarkable catalytic promiscuity
    • Polekhina, G., Board, P. G., Blackburn, A. C. and Parker, M. W. (2001) Crystal structure of maleylacetoacetate isomerase/glutathione transferase Zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry 40, 1567-1576
    • (2001) Biochemistry , vol.40 , pp. 1567-1576
    • Polekhina, G.1    Board, P.G.2    Blackburn, A.C.3    Parker, M.W.4
  • 12
    • 0035906701 scopus 로고    scopus 로고
    • The structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana: Characterisation of a GST with novel active-site architecture and a putative role in tyrosine catabolism
    • Thom, R., Dixon, D. P., Edwards, R., Cole, D. J. and Lapthorn, A. J. (2001) The structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana: characterisation of a GST with novel active-site architecture and a putative role in tyrosine catabolism. J. Mol. Biol. 308, 949-962
    • (2001) J. Mol. Biol. , vol.308 , pp. 949-962
    • Thom, R.1    Dixon, D.P.2    Edwards, R.3    Cole, D.J.4    Lapthorn, A.J.5
  • 13
    • 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
  • 14
    • 0030662474 scopus 로고    scopus 로고
    • 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, A. M., Antonini, G., Nicotra, M., Battistoni, A., Bello, M. L., Board, P. G., Parker, M. W. and Ricci, G. (1997) 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. 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
  • 15
    • 0028924699 scopus 로고
    • Functional significance of arginine 15 in the active site of human class α glutathione transferase A1-1
    • Bjornestedt, R., Stenberg, G., Widersten, M., Board, P. G., Sinning, I., Jones, T. A. and Mannervik, B. (1995) Functional significance of arginine 15 in the active site of human class α glutathione transferase A1-1. J. Mol. Biol. 247, 765-773
    • (1995) J. Mol. Biol. , vol.247 , pp. 765-773
    • Bjornestedt, R.1    Stenberg, G.2    Widersten, M.3    Board, P.G.4    Sinning, I.5    Jones, T.A.6    Mannervik, B.7
  • 17
    • 0032526942 scopus 로고    scopus 로고
    • A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications
    • Rossjohn, J., Polekhina, G., Feil, S. C., Allocati, N., Masulli, M., De Illio, C. and Parker, M. W. (1998) A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6, 721-734
    • (1998) Structure , vol.6 , pp. 721-734
    • Rossjohn, J.1    Polekhina, G.2    Feil, S.C.3    Allocati, N.4    Masulli, M.5    De Illio, C.6    Parker, M.W.7
  • 18
    • 0015918820 scopus 로고
    • Purification and properties of maleylacetone cis-trans isomerase from vibrio 01
    • Seltzer, S. (1973) Purification and properties of maleylacetone cis-trans isomerase from vibrio 01. J. Biol. Chem. 248, 215-222
    • (1973) J. Biol. Chem. , vol.248 , pp. 215-222
    • Seltzer, S.1
  • 19
    • 0001752925 scopus 로고
    • Synthesis of model compounds for maleylacetoacetic acid
    • Fowler, J. and Seltzer, S. (1970) Synthesis of model compounds for maleylacetoacetic acid. J. Org. Chem. 35, 3529-3532
    • (1970) J. Org. Chem. , vol.35 , pp. 3529-3532
    • Fowler, J.1    Seltzer, S.2
  • 20
    • 0033391126 scopus 로고    scopus 로고
    • Inactivation of glutathione transferase Zeta by dichloroacetic acid and other fluorine-lacking α-haloalkanoic acids
    • Anderson, W. B., Board, P. G., Gargano, B. and Anders, M. W. (1999) Inactivation of glutathione transferase Zeta by dichloroacetic acid and other fluorine-lacking α-haloalkanoic acids. Chem. Res. Toxicol. 12, 1144-1149
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 1144-1149
    • Anderson, W.B.1    Board, P.G.2    Gargano, B.3    Anders, M.W.4
  • 21
    • 0035852844 scopus 로고    scopus 로고
    • GSTZ1d: A new allele of glutathione transferase Zeta and maleylacetoacetate isomerase
    • Polekhina, G., Board, P. G., Blackburn, A. C. and Parker, M. W. (2001) GSTZ1d: a new allele of glutathione transferase Zeta and maleylacetoacetate isomerase. Biochemistry 40, 1567-1576
    • (2001) Biochemistry , vol.40 , pp. 1567-1576
    • Polekhina, G.1    Board, P.G.2    Blackburn, A.C.3    Parker, M.W.4
  • 22
    • 0014247508 scopus 로고
    • Biochemical variants of glucose-6-phosphate dehydrogenase giving rise to congenital nonspherocytic hemolytic disease
    • Beutler, E., Mathai, C. K. and Smith, J. E. (1968) Biochemical variants of glucose-6-phosphate dehydrogenase giving rise to congenital nonspherocytic hemolytic disease. Blood 31, 131-150
    • (1968) Blood , vol.31 , pp. 131-150
    • Beutler, E.1    Mathai, C.K.2    Smith, J.E.3
  • 23
    • 0034009330 scopus 로고    scopus 로고
    • Discovery of a functional polymorphism in human glutathione transferase Zeta by expressed sequence tag database analysis
    • Blackburn, A. C., Tzeng, H. F., Anders, M. W. and Board, P. G. (2000) Discovery of a functional polymorphism in human glutathione transferase Zeta by expressed sequence tag database analysis. Pharmacogenetics 10, 49-57
    • (2000) Pharmacogenetics , vol.10 , pp. 49-57
    • Blackburn, A.C.1    Tzeng, H.F.2    Anders, M.W.3    Board, P.G.4
  • 24
    • 0034625156 scopus 로고    scopus 로고
    • Recruitment of a double bond isomerase to serve as a reductive dehalogenase during biodegradation of pentachlorophenol
    • Anandarajah, K., Kiefer, P. M., Jr., Donohoe, B. S. and Copley, S. D. (2000) Recruitment of a double bond isomerase to serve as a reductive dehalogenase during biodegradation of pentachlorophenol. Biochemistry 39, 5303-5311
    • (2000) Biochemistry , vol.39 , pp. 5303-5311
    • Anandarajah, K.1    Kiefer P.M., Jr.2    Donohoe, B.S.3    Copley, S.D.4
  • 25
    • 0035996338 scopus 로고    scopus 로고
    • Kinetics of the biotransformation of maleylacetone and chlorofluoroacetic acid by polymorphic variants of human glutathione transferase zeta (hGSTZ1-1)
    • Lantum, H. B., Board, P. G. and Anders, M. W. (2002) Kinetics of the biotransformation of maleylacetone and chlorofluoroacetic acid by polymorphic variants of human glutathione transferase zeta (hGSTZ1-1). Chem. Res. Toxicol. 15, 957-963
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 957-963
    • Lantum, H.B.1    Board, P.G.2    Anders, M.W.3
  • 26
    • 0034053786 scopus 로고    scopus 로고
    • Polymorphism- and species-dependent inactivation of glutathione transferase Zeta by dichloroacetate
    • Tzeng, H. F., Blackburn, A. C., Board, P. G. and Anders, M. W. (2000) Polymorphism- and species-dependent inactivation of glutathione transferase Zeta by dichloroacetate. Chem. Res. Toxicol. 13, 231-236
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 231-236
    • Tzeng, H.F.1    Blackburn, A.C.2    Board, P.G.3    Anders, M.W.4
  • 27
    • 0037192150 scopus 로고    scopus 로고
    • Characterization of the initial steps in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase
    • Kiefer, P. M., Jr. and Copley, S. D. (2002) Characterization of the initial steps in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase. Biochemistry 41, 1315-1322
    • (2002) Biochemistry , vol.41 , pp. 1315-1322
    • Kiefer P.M., Jr.1    Copley, S.D.2
  • 28
    • 0036852695 scopus 로고    scopus 로고
    • Mass spectral characterization of dichloroacetic acid-modified human glutathione transferase Zeta
    • Anderson, W. B., Liebler, D. C., Board, P. G. and Anders, M. W. (2002) Mass spectral characterization of dichloroacetic acid-modified human glutathione transferase Zeta. Chem. Res. Toxicol. 15, 1387-1397
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 1387-1397
    • Anderson, W.B.1    Liebler, D.C.2    Board, P.G.3    Anders, M.W.4
  • 30
    • 0029003807 scopus 로고
    • Crystal structure of a Theta-class glutathione transferase
    • Wilce, M. C., Board, P.G., Feil, S. C. and Parker, M. W. (1995) Crystal structure of a Theta-class glutathione transferase. EMBO J. 14, 2133-2143
    • (1995) EMBO J. , vol.14 , pp. 2133-2143
    • Wilce, M.C.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 31
    • 0029853099 scopus 로고    scopus 로고
    • Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: Catalysis with different substrates involves different residues
    • Tan, K. L., Chelvanayagam, G., Parker, M. W. and Board, P. G. (1996) Mutagenesis of the active site of the human Theta-class glutathione transferase GSTT2-2: catalysis with different substrates involves different residues. Biochem. J. 319, 315-321
    • (1996) Biochem. J. , vol.319 , pp. 315-321
    • Tan, K.L.1    Chelvanayagam, G.2    Parker, M.W.3    Board, P.G.4
  • 32
    • 0034708616 scopus 로고    scopus 로고
    • Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme
    • Jemth, P. and Mannervik, B. (2000) Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme. J. Biol. Chem. 275, 8618-8624
    • (2000) J. Biol. Chem. , vol.275 , pp. 8618-8624
    • Jemth, P.1    Mannervik, B.2
  • 33
    • 0028886558 scopus 로고
    • Ionisation of cysteine residues at the termini of model α-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family
    • Kortemme, T. and Creighton, T. E. (1995) Ionisation of cysteine residues at the termini of model α-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family. J. Mol. Biol. 253, 799-812
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 34
    • 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., Dirt, H. W., Huber, R., Gilliland, G. L., Armstrong, R. N., Ji, X., Board, P. G. 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    Dirt, H.W.5    Huber, R.6    Gilliland, G.L.7    Armstrong, R.N.8    Ji, X.9    Board, P.G.10
  • 37
    • 0036272942 scopus 로고    scopus 로고
    • Maleylacetoacetate isomerase (MAAI/GSTZ)-deficient mice reveal a glutathione-dependent nonenzymatic bypass in tyrosine catabolism
    • Fernandez-Canon, J. M., Baetscher, M. W., Finegold, M., Burlingame, T., Gibson, K. M. and Grompe, M. (2002) Maleylacetoacetate isomerase (MAAI/GSTZ)-deficient mice reveal a glutathione-dependent nonenzymatic bypass in tyrosine catabolism. Mol. Cell. Biol. 22, 4943-4951
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4943-4951
    • Fernandez-Canon, J.M.1    Baetscher, M.W.2    Finegold, M.3    Burlingame, T.4    Gibson, K.M.5    Grompe, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.