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Volumn 412, Issue 2, 2011, Pages 204-211

Structure-guided activity restoration of the silkworm glutathione transferase Omega GSTO3-3

Author keywords

Bombyx mori; crystal structure; enzymatic activity; glutathione transferase Omega; site directed mutagenesis

Indexed keywords

ASPARAGINE; CYSTEINE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE OMEGA 3; UNCLASSIFIED DRUG;

EID: 80052036835     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.019     Document Type: Article
Times cited : (9)

References (36)
  • 2
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • DOI 10.1042/0264-6021:3600001
    • Sheehan D., Meade G., Foley V.M., and Dowd C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily Biochem. J. 360 2001 1 16 (Pubitemid 33081943)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 3
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • DOI 10.1021/tx960072x
    • Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases Chem. Res. Toxicol. 10 1997 2 18 (Pubitemid 27044902)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.1 , pp. 2-18
    • Armstrong, R.N.1
  • 4
    • 0000120689 scopus 로고
    • Detection and biochemical characterization of insecticide resistance in fall armyworm (Lepidoptera: Noctuidae)
    • Yu S.J. Detection and biochemical characterization of insecticide resistance in fall armyworm (Lepidoptera: Noctuidae) J. Econ. Entomol. 85 1992 675 682
    • (1992) J. Econ. Entomol. , vol.85 , pp. 675-682
    • Yu, S.J.1
  • 5
    • 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. 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
  • 7
    • 73849112021 scopus 로고    scopus 로고
    • Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family
    • Ma X.X., Jiang Y.L., He Y.X., Bao R., Chen Y., and Zhou C.Z. Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family EMBO Rep. 10 2009 1320 1326
    • (2009) EMBO Rep. , vol.10 , pp. 1320-1326
    • Ma, X.X.1    Jiang, Y.L.2    He, Y.X.3    Bao, R.4    Chen, Y.5    Zhou, C.Z.6
  • 8
    • 0032548807 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site
    • DOI 10.1016/S0014-5793(98)00080-5, PII S0014579398000805
    • Casalone E., Allocati N., Ceccarelli I., Masulli M., Rossjohn J., Parker M.W., and Di Ilio C. Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site FEBS Lett. 423 1998 122 124 (Pubitemid 28343193)
    • (1998) FEBS Letters , vol.423 , Issue.2 , pp. 122-124
    • Casalone, E.1    Allocati, N.2    Ceccarelli, I.3    Michele Masulli4    Rossjohn, J.5    Parker, M.W.6    Di Ilio, C.7
  • 9
    • 22944473357 scopus 로고    scopus 로고
    • Insect Glutathione S-Transferases
    • Yu S.J. Insect glutathione S-transferases Zool. Stud. 35 1996 9 19 (Pubitemid 126062901)
    • (1996) Zoological Studies , vol.35 , Issue.1 , pp. 9-19
    • Yu, S.J.1
  • 10
    • 0030695430 scopus 로고    scopus 로고
    • A complex glutathione transferase gene family in the housefly Musca domestica
    • Zhou Z.H., and Syvanen M. A complex glutathione transferase gene family in the housefly Musca domestica Mol. Gen. Genet. 256 1997 187 194
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 187-194
    • Zhou, Z.H.1    Syvanen, M.2
  • 11
    • 59649107036 scopus 로고    scopus 로고
    • Identification, genomic organization and expression pattern of glutathione S-transferase in the silkworm, Bombyx mori
    • Yu Q., Lu C., Li B., Fang S., Zuo W., and Dai F. Identification, genomic organization and expression pattern of glutathione S-transferase in the silkworm, Bombyx mori Insect Biochem. Mol. Biol. 38 2008 1158 1164
    • (2008) Insect Biochem. Mol. Biol. , vol.38 , pp. 1158-1164
    • Yu, Q.1    Lu, C.2    Li, B.3    Fang, S.4    Zuo, W.5    Dai, F.6
  • 12
    • 9144243812 scopus 로고    scopus 로고
    • The Anopheles gambiae glutathione transferase supergene family: Annotation, phylogeny and expression profiles
    • Ding Y., Ortelli F., Rossiter L.C., Hemingway J., and Ranson H. The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny and expression profiles BMC Genomics 4 2003 35
    • (2003) BMC Genomics , vol.4 , pp. 35
    • Ding, Y.1    Ortelli, F.2    Rossiter, L.C.3    Hemingway, J.4    Ranson, H.5
  • 14
    • 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. A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications Structure 6 1998 721 734 (Pubitemid 28301206)
    • (1998) Structure , vol.6 , Issue.6 , pp. 721-734
    • Rossjohn, J.1    Polekhina, G.2    Feil, S.C.3    Allocati, N.4    Masulli, M.5    Di Iiio, C.6    Parker, M.W.7
  • 15
    • 55149089058 scopus 로고    scopus 로고
    • "restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2
    • Zhang Z.R., Bai M., Wang X.Y., Zhou J.M., and Perrett S. "Restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2 J. Mol. Biol. 384 2008 641 651
    • (2008) J. Mol. Biol. , vol.384 , pp. 641-651
    • Zhang, Z.R.1    Bai, M.2    Wang, X.Y.3    Zhou, J.M.4    Perrett, S.5
  • 16
    • 34848858489 scopus 로고    scopus 로고
    • Molecular cloning and characterization of omega class glutathione S-transferase (GST-O) from the polychaete Neanthes succinea: Biochemical comparison with theta class glutathione S-transferase (GST-T)
    • Rhee J.S., Lee Y.M., Hwang D.S., Lee K.W., Kim I.C., and Shin K.H. Molecular cloning and characterization of omega class glutathione S-transferase (GST-O) from the polychaete Neanthes succinea: biochemical comparison with theta class glutathione S-transferase (GST-T) Comp. Biochem. Physiol., Toxicol. Pharmacol. 146 2007 471 477
    • (2007) Comp. Biochem. Physiol., Toxicol. Pharmacol. , vol.146 , pp. 471-477
    • Rhee, J.S.1    Lee, Y.M.2    Hwang, D.S.3    Lee, K.W.4    Kim, I.C.5    Shin, K.H.6
  • 17
    • 40549133470 scopus 로고    scopus 로고
    • Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site
    • DOI 10.1002/prot.21835
    • Allocati N., Federici L., Masulli M., Favaloro B., and Di Ilio C. Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site Proteins 71 2008 16 23 (Pubitemid 351358587)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.1 , pp. 16-23
    • Allocati, N.1    Federici, L.2    Masulli, M.3    Favaloro, B.4    Di Ilio, C.5
  • 18
    • 34548169608 scopus 로고    scopus 로고
    • A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis
    • DOI 10.1042/BJ20070422
    • Vararattanavech A., and Ketterman A.J. A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis Biochem. J. 406 2007 247 256 (Pubitemid 47310955)
    • (2007) Biochemical Journal , vol.406 , Issue.2 , pp. 247-256
    • Vararattanavech, A.1    Ketterman, A.J.2
  • 19
    • 0037954199 scopus 로고    scopus 로고
    • The role of an evolutionarily conserved cis-proline in the thioredoxin-like domain of human class Alpha glutathione transferase A1-1
    • DOI 10.1042/BJ20021765
    • Nathaniel C., Wallace L.A., Burke J., and Dirr H.W. The role of an evolutionarily conserved cis-proline in the thioredoxin-like domain of human class Alpha glutathione transferase A1-1 Biochem. J. 372 2003 241 246 (Pubitemid 36609627)
    • (2003) Biochemical Journal , vol.372 , Issue.1 , pp. 241-246
    • Nathaniel, C.1    Wallace, L.A.2    Burke, J.3    Dirr, H.W.4
  • 20
    • 1542304694 scopus 로고    scopus 로고
    • Functional Role of the Lock and Key Motif at the Subunit Interface of Glutathione Transferase P1-1
    • DOI 10.1074/jbc.M312320200
    • Hegazy U.M., Mannervik B., and Stenberg G. Functional role of the lock and key motif at the subunit interface of glutathione transferase P1-1 J. Biol. Chem. 279 2004 9586 9596 (Pubitemid 38296027)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 9586-9596
    • Hegazy, U.M.1    Mannervik, B.2    Stenberg, G.3
  • 21
    • 0037342498 scopus 로고    scopus 로고
    • Characterization of the human Omega class glutathione transferase genes and associated polymorphisms
    • DOI 10.1097/00008571-200303000-00003
    • Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., and Board P.G. Characterization of the human Omega class glutathione transferase genes and associated polymorphisms Pharmacogenetics 13 2003 131 144 (Pubitemid 36324243)
    • (2003) Pharmacogenetics , vol.13 , Issue.3 , pp. 131-144
    • Whitbread, A.K.1    Tetlow, N.2    Eyre, H.J.3    Sutherland, G.R.4    Board, P.G.5
  • 22
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • DOI 10.1006/jmbi.1999.3091
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202 (Pubitemid 29435759)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 23
    • 0024473664 scopus 로고
    • Glutathione-S-transferase are major cytosolic thyroid hormone binding proteins
    • Ishigaki S., Abramovitz M., and Listowsky I. Glutathione-S-transferases are major cytosolic thyroid hormone binding proteins Arch. Biochem. Biophys. 273 1989 265 272 (Pubitemid 19221980)
    • (1989) Archives of Biochemistry and Biophysics , vol.273 , Issue.2 , pp. 265-272
    • Ishigaki, S.1    Abramovitz, M.2    Listowsky, I.3
  • 24
    • 0017845354 scopus 로고
    • The binding of porphyrins by ligandin
    • Tipping E., Ketterer B., and Koskelo P. The binding of porphyrins by ligandin Biochem. J. 169 1978 509 516 (Pubitemid 8281756)
    • (1978) Biochemical Journal , vol.169 , Issue.3 , pp. 509-516
    • Tipping, E.1    Ketterer, B.2    Koskelo, P.3
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode Macromol. Crystallogr., Part A, 1997 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser Acta Crystallogr., Sect. D: Biol. Crystallogr. 63 2007 32 41
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 32
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione S-transferases
    • Habig W.H., and Jakoby W.B. Assays for differentiation of glutathione S-transferases Methods Enzymol. 77 1981 398 405
    • (1981) Methods Enzymol. , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 33
    • 33748755738 scopus 로고    scopus 로고
    • Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the Omega class glutathione S-transferases
    • DOI 10.1042/BJ20060424
    • Kim J., Suh H., Kim S., Kim K., Ahn C., and Yim J. Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the Omega class glutathione S-transferases Biochem. J. 398 2006 451 460 (Pubitemid 44453389)
    • (2006) Biochemical Journal , vol.398 , Issue.3 , pp. 451-460
    • Kim, J.1    Suh, H.2    Kim, S.3    Kim, K.4    Ahn, C.5    Yim, J.6
  • 34
    • 33846859089 scopus 로고    scopus 로고
    • Glutathione transferase omega 1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones
    • DOI 10.1021/tx600305y
    • Board P.G., and Anders M.W. Glutathione transferase omega 1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones Chem. Res. Toxicol. 20 2007 149 154 (Pubitemid 46220165)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.1 , pp. 149-154
    • Board, P.G.1    Anders, M.W.2
  • 35
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang J.T., Wu C.S., and Martinez H.M. Calculation of protein conformation from circular dichroism Methods Enzymol. 130 1986 208 269
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 36
    • 0028347388 scopus 로고
    • 264 with diiodofluorescein iodacetamide as a tool to study the membrane topology of cytochrome P450scc (CYP11A1)
    • 264 with diiodofluorescein iodacetamide as a tool to study the membrane topology of cytochrome P450scc (CYP11A1) FEBS Lett. 340 1994 83-88
    • (1994) FEBS Lett. , vol.340 , pp. 83-88
    • Chernogolov, A.1    Usanov, S.2    Kraft, R.3    Schwartz, D.4


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