메뉴 건너뛰기




Volumn 39, Issue 3, 2000, Pages 235-243

Ab initio calculations on hidden modulators of theta class glutathione transferase activity

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE;

EID: 0034657549     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000515)39:3<235::AID-PROT60>3.0.CO;2-Z     Document Type: Article
Times cited : (3)

References (35)
  • 1
    • 0033452853 scopus 로고    scopus 로고
    • Proton release upon binding of glutathione to Alpha, Mu and Delta class glutathione transferases
    • Caccuri AM, Antonini G, Board PG, Parker MW, et al. Proton release upon binding of glutathione to Alpha, Mu and Delta class glutathione transferases. Bochem J 1999;344:419-425.
    • (1999) Bochem J , vol.344 , pp. 419-425
    • Caccuri, A.M.1    Antonini, G.2    Board, P.G.3    Parker, M.W.4
  • 2
    • 0032478199 scopus 로고    scopus 로고
    • Proton release upon glutathione binding to glutathione transferase P1-1: Kinetic analysis of a multistep glutathione binding process
    • Caccuri AM, Lo Bello M, Nuccetelli M, et al. Proton release upon glutathione binding to glutathione transferase P1-1: kinetic analysis of a multistep glutathione binding process. Biochemistry 1998;37:3028-3034.
    • (1998) Biochemistry , vol.37 , pp. 3028-3034
    • Caccuri, A.M.1    Lo Bello, M.2    Nuccetelli, M.3
  • 3
    • 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 AM, Antonini G, Nicotra M, et al. 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 1997;272:29681-29686.
    • (1997) J Biol Chem , vol.272 , pp. 29681-29686
    • Caccuri, A.M.1    Antonini, G.2    Nicotra, M.3
  • 4
    • 0032548807 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site
    • Casalone E, Allocati N, Ceccarelli I, et al. Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site. FEES Lett 1998;423:122-124.
    • (1998) Fees Lett , vol.423 , pp. 122-124
    • Casalone, E.1    Allocati, N.2    Ceccarelli, I.3
  • 5
    • 0029064985 scopus 로고
    • Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods
    • Ji X, von Rosenvinge EC, Johnson WW, et al. Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry 1995;34:5317-5328.
    • (1995) Biochemistry , vol.34 , pp. 5317-5328
    • Ji, X.1    Von Rosenvinge, E.C.2    Johnson, W.W.3
  • 6
    • 0031574268 scopus 로고    scopus 로고
    • Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme
    • Jemth P, Mannervik B. Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Arch Biochem Biophys 1997;348:247-254.
    • (1997) Arch Biochem Biophys , vol.348 , pp. 247-254
    • Jemth, P.1    Mannervik, B.2
  • 7
    • 0001457141 scopus 로고
    • Second sphere electrostatic effects in the active site of glutathione S-transferase. Observations of an on face hydrogen bond between the side chain of threonine 13 and the π-cloud of tyrosine 6 and its influence on catalysis
    • Liu S, Ji X, Gilliland G, Stevens W, Armstrong RN. Second sphere electrostatic effects in the active site of glutathione S-transferase. Observations of an on face hydrogen bond between the side chain of threonine 13 and the π-cloud of tyrosine 6 and its influence on catalysis. J Am Chem Soc 1993;115:7910-7911.
    • (1993) J Am Chem Soc , vol.115 , pp. 7910-7911
    • Liu, S.1    Ji, X.2    Gilliland, G.3    Stevens, W.4    Armstrong, R.N.5
  • 8
    • 0025816448 scopus 로고
    • The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution
    • Reinemer P, Dirr HW, Ladenstein R, Schaffer J, Gallay O, Huber R. The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. Embo J 1991;10:1997-2005.
    • (1991) Embo J , vol.10 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schaffer, J.4    Gallay, O.5    Huber, R.6
  • 9
    • 0026460365 scopus 로고
    • The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution
    • Ji X, Zhang P, Armstrong RN, Gilliland GL. The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution. Biochemistry 1992;31:10169-10184.
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 10
    • 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 GJ, Cowan SW, et al. 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 1993;232:192-212.
    • (1993) J Mol Biol , vol.232 , pp. 192-212
    • Sinning, I.1    Kleywegt, G.J.2    Cowan, S.W.3
  • 11
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • Wilce MCJ, Board PG, Feil SC, Parker MW. Crystal structure of a theta-class glutathione transferase. EMBO J 1995;14:2133-2143.
    • (1995) EMBO J , vol.14 , pp. 2133-2143
    • Wilce, M.C.J.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 12
    • 0032520952 scopus 로고    scopus 로고
    • Human theta class glutathione transferase: The crystal structure reveals a sulfate-binding pocket within a buried active site
    • Rossjohn J, McKinstry WJ, Oakley AJ, et al. Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure 1998;6:309-322.
    • (1998) Structure , vol.6 , pp. 309-322
    • Rossjohn, J.1    McKinstry, W.J.2    Oakley, A.J.3
  • 13
    • 18844467911 scopus 로고    scopus 로고
    • Cloning and crystal structure of hematopoietic prostaglandin D synthase
    • Kanaoka Y, Ago H, Inagaki E, et al. Cloning and crystal structure of hematopoietic prostaglandin D synthase. Cell 1997;90:1085-1095.
    • (1997) Cell , vol.90 , pp. 1085-1095
    • Kanaoka, Y.1    Ago, H.2    Inagaki, E.3
  • 14
    • 0029853099 scopus 로고    scopus 로고
    • Mutagenesis of the active site of the human Theta class glutathione transferase GSTT2-2: Identification of a novel function as a glutathione dependant sulphatase
    • Tan KL, Chelvanayagam G, Parker MW, Board PG. Mutagenesis of the active site of the human Theta class glutathione transferase GSTT2-2: identification of a novel function as a glutathione dependant sulphatase. Biochem J 1996;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
  • 15
    • 0026705291 scopus 로고
    • Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase
    • Liu S, Zhang P, Ji X, Johnson WW, Gilliland GL, Armstrong RN. Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase. J Biol Chem 1992;267:4296-4299.
    • (1992) J Biol Chem , vol.267 , pp. 4296-4299
    • Liu, S.1    Zhang, P.2    Ji, X.3    Johnson, W.W.4    Gilliland, G.L.5    Armstrong, R.N.6
  • 16
    • 0026640526 scopus 로고
    • Site-directed mutagenesis of glutathione S-transferase YaYa. Important roles of tyrosine 9 and aspartic acid 101 in catalysis
    • Wang RW, Newton DJ, Huskey SE, McKeever BM, Pickett CB, Lu AY. Site-directed mutagenesis of glutathione S-transferase YaYa. Important roles of tyrosine 9 and aspartic acid 101 in catalysis. J Biol Chem 1992;267:19866-19871.
    • (1992) J Biol Chem , vol.267 , pp. 19866-19871
    • Wang, R.W.1    Newton, D.J.2    Huskey, S.E.3    McKeever, B.M.4    Pickett, C.B.5    Lu, A.Y.6
  • 17
    • 0026624869 scopus 로고
    • Tyrosine-7 in human class Pi glutathione S-transferase is important for lowering the pKa of the thiol group of glutathione in the enzyme-glutathione complex
    • Kong KH, Takasu K, Inoue H, Takahashi K. Tyrosine-7 in human class Pi glutathione S-transferase is important for lowering the pKa of the thiol group of glutathione in the enzyme-glutathione complex. Biochem Biophys Res Commun 1992;184:194-197.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 194-197
    • Kong, K.H.1    Takasu, K.2    Inoue, H.3    Takahashi, K.4
  • 18
    • 0027250509 scopus 로고
    • The catalytic mechanism of glutathione S-transferase (GST). Spectroscopic determination of the pKa of Tyr-9 in rat alpha 1-1 GST
    • Atkins WM, Wang RW, Bird AW, Newton DJ, Lu AY. The catalytic mechanism of glutathione S-transferase (GST). Spectroscopic determination of the pKa of Tyr-9 in rat alpha 1-1 GST. J Biol Chem 1993;268:19188-19191.
    • (1993) J Biol Chem , vol.268 , pp. 19188-19191
    • Atkins, W.M.1    Wang, R.W.2    Bird, A.W.3    Newton, D.J.4    Lu, A.Y.5
  • 20
    • 0027170216 scopus 로고
    • Electrostatic evidence for the activation of the glutathione thiol by Tyr7 in pi-class glutathione transferases
    • Karshikoff A, Reinemer P, Huber R, Ladenstein R. Electrostatic evidence for the activation of the glutathione thiol by Tyr7 in pi-class glutathione transferases. Eur J Biochem 1993;215:663-670.
    • (1993) Eur J Biochem , vol.215 , pp. 663-670
    • Karshikoff, A.1    Reinemer, P.2    Huber, R.3    Ladenstein, R.4
  • 21
    • 0029960278 scopus 로고    scopus 로고
    • Proton configuration in the ground state and transition state of a glutathione transferase-catalyzed reaction inferred from the properties of tetradeca(3-fluorotyrosyl)-glutathione transferase
    • Parsons JF, Armstrong RN. Proton configuration in the ground state and transition state of a glutathione transferase-catalyzed reaction inferred from the properties of tetradeca(3-fluorotyrosyl)-glutathione transferase. J Am Chem Soc 1996;118:2295-2296.
    • (1996) J Am Chem Soc , vol.118 , pp. 2295-2296
    • Parsons, J.F.1    Armstrong, R.N.2
  • 22
    • 0030937423 scopus 로고    scopus 로고
    • Role of active site tyrosine in glutathione S-transferase: Insights from a theoretical study on model systems
    • Zheng YJ, Ornstein RL. Role of active site tyrosine in glutathione S-transferase: insights from a theoretical study on model systems. J Am Chem Soc 1997;119:1523-1528.
    • (1997) J Am Chem Soc , vol.119 , pp. 1523-1528
    • Zheng, Y.J.1    Ornstein, R.L.2
  • 23
    • 0024588467 scopus 로고
    • Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase
    • Graminski GF, Kubo Y, Armstrong RN. Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase Biochemistry 1989;28:3562-3568.
    • (1989) Biochemistry , vol.28 , pp. 3562-3568
    • Graminski, G.F.1    Kubo, Y.2    Armstrong, R.N.3
  • 24
    • 0029995385 scopus 로고    scopus 로고
    • First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase
    • Xiao G, Liu S, Ji X, et al. First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase. Biochemistry 1996;35:4753-4765.
    • (1996) Biochemistry , vol.35 , pp. 4753-4765
    • Xiao, G.1    Liu, S.2    Ji, X.3
  • 25
    • 0029787227 scopus 로고    scopus 로고
    • Rational modulation of the catalytic activity of A1-1 glutathione S-transferase: Evidence for incorporation of an on-face (π***HO-Ar) hydrogen bond at tyrosine-9
    • Dietze EC, Ibarra C, Dabrowski MJ, Bird A, Atkins WM. Rational modulation of the catalytic activity of A1-1 glutathione S-transferase: evidence for incorporation of an on-face (π***HO-Ar) hydrogen bond at tyrosine-9. Biochemistry 1996;35:11938-11944.
    • (1996) Biochemistry , vol.35 , pp. 11938-11944
    • Dietze, E.C.1    Ibarra, C.2    Dabrowski, M.J.3    Bird, A.4    Atkins, W.M.5
  • 26
    • 0033604849 scopus 로고    scopus 로고
    • Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a
    • Patskovsky YV, Patskovska LN, Listowsky I. Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a. Biochemistry 1999;38:1193-1202.
    • (1999) Biochemistry , vol.38 , pp. 1193-1202
    • Patskovsky, Y.V.1    Patskovska, L.N.2    Listowsky, I.3
  • 27
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 1995;3:239-243.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 28
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board PG, Baker RT, Chelvanayagam G, Jermiin LS. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem J 1997;15:929-935.
    • (1997) Biochem J , vol.15 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 31
    • 0033520119 scopus 로고
    • Fast product formation and slow product release are important features in a hysteretic reaction mechanism of glutathione transferase T2-2
    • Jemth P, Mannervik B. Fast product formation and slow product release are important features in a hysteretic reaction mechanism of glutathione transferase T2-2. Biochemistry 1991;38:9982-9991.
    • (1991) Biochemistry , vol.38 , pp. 9982-9991
    • Jemth, P.1    Mannervik, B.2
  • 32
    • 0029926948 scopus 로고    scopus 로고
    • The energetics of hydrogen bonds in model systems: Implications for enzymatic catalysis
    • Shan SO, Loh S, Herschlag D. The energetics of hydrogen bonds in model systems: implications for enzymatic catalysis. Science 1996;272:97-101.
    • (1996) Science , vol.272 , pp. 97-101
    • Shan, S.O.1    Loh, S.2    Herschlag, D.3
  • 33
    • 0028030684 scopus 로고
    • Low barrier hydrogen bonds and enzymatic catalysis
    • Cleland WW, Kreevoy MM. Low barrier hydrogen bonds and enzymatic catalysis. Science 1994;264:1887-1890.
    • (1994) Science , vol.264 , pp. 1887-1890
    • Cleland, W.W.1    Kreevoy, M.M.2
  • 34
    • 0032526942 scopus 로고    scopus 로고
    • A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications
    • Rossjohn J, Polekhina G, Geil SC, et al. A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Stucture 1998;6:721-734.
    • (1998) Stucture , vol.6 , pp. 721-734
    • Rossjohn, J.1    Polekhina, G.2    Geil, S.C.3
  • 35
    • 0029101750 scopus 로고
    • Evidence for an essential serine residue in the active site of the Theta class glutathione transferases
    • Board PG, Coggan M, Wilce MCJ, Parker MW. Evidence for an essential serine residue in the active site of the Theta class glutathione transferases. Biochem J 1995;311:247-250.
    • (1995) Biochem J , vol.311 , pp. 247-250
    • Board, P.G.1    Coggan, M.2    Wilce, M.C.J.3    Parker, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.