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Volumn 77, Issue 2, 2009, Pages 370-377

The structure of G117H mutant of butyrylcholinesterase: Nerve agents scavenger

Author keywords

Butyrylcholinesterase; Empirical valence bond; Hydrolysis; Organophosphate esters; Serine esterases; Simulations

Indexed keywords

ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; CHOLINESTERASE; ESTER DERIVATIVE; ORGANOPHOSPHATE ESTER; RIBONUCLEASE A; UNCLASSIFIED DRUG;

EID: 84962336503     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22442     Document Type: Article
Times cited : (21)

References (57)
  • 1
    • 0000605095 scopus 로고
    • Anticholinesterase agents
    • Gilman AG, Nies AS, Rall TW, Taylor P, editors. New York: Macmillan
    • Taylor P. Anticholinesterase agents. In: Gilman AG, Nies AS, Rall TW, Taylor P, editors. The Pharmacological Basis of Therapeutics. New York: Macmillan; 1991. pp 131-150.
    • (1991) The Pharmacological Basis of Therapeutics , pp. 131-150
    • Taylor, P.1
  • 2
    • 0028957265 scopus 로고
    • Anticholinesterases: Medical applications of neurochemical principles
    • Millard CB, Broomfield CA. Anticholinesterases: medical applications of neurochemical principles. J Neurochem 1995;64:1909-1918.
    • (1995) J Neurochem , vol.64 , pp. 1909-1918
    • Millard, C.B.1    Broomfield, C.A.2
  • 4
    • 0030833798 scopus 로고    scopus 로고
    • Unique push-pull mechanism of dealkylation in soman-inhibited cholinesterases
    • DOI 10.1021/bi962764q
    • Viragh C, Akhmetshin R, Kovach IM, Broomfield C. Unique pushpull mechanism of dealkylation in soman-inhibited cholinesterases. Biochemistry 1997;36:8243-8252. (Pubitemid 27297533)
    • (1997) Biochemistry , vol.36 , Issue.27 , pp. 8243-8252
    • Viragh, C.1    Akhmetshin, R.2    Kovach, I.M.3    Broomfield, C.4
  • 5
    • 0032488593 scopus 로고    scopus 로고
    • Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: Synergy results in a somanase
    • DOI 10.1021/bi972057c
    • Millard CB, Lockridge O, Broomfield CA. Design and expression of organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase. Biochemistry 1995;34:15925-15933. (Pubitemid 28049126)
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 237-247
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 6
    • 33845282579 scopus 로고
    • Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states
    • Quinn DM. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem Rev 1987;87:955-979.
    • (1987) Chem Rev , vol.87 , pp. 955-979
    • Quinn, D.M.1
  • 8
    • 0027515387 scopus 로고
    • Structure and functions of acetylcholinesterase and butyrylcholinesterase
    • Massoulie J, Sussman J, Bon S, Silman I. Structure and functions of acetylcholinesterase and butyrylcholinesterase. Prog Brain Res 1993;98:139-146.
    • (1993) Prog Brain Res , vol.98 , pp. 139-146
    • Massoulie, J.1    Sussman, J.2    Bon, S.3    Silman, I.4
  • 9
    • 0028174977 scopus 로고
    • The cholinesterases - From genes to proteins
    • Taylor P, Radic Z. The cholinesterases - from genes to proteins. Annu Rev Pharmacol Toxicol 1994;34:281-320.
    • (1994) Annu Rev Pharmacol Toxicol , vol.34 , pp. 281-320
    • Taylor, P.1    Radic, Z.2
  • 14
    • 0027459560 scopus 로고
    • Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity
    • DOI 10.1021/bi00052a003
    • Vellom DC, Radic Z, Li Y, Pickering NA, Camp S, Taylor P. Aminoacid residues controlling acetylcholinesterase and butylcholinesterase specificity. Biochemistry 1993;32:12-17. (Pubitemid 23033314)
    • (1993) Biochemistry , vol.32 , Issue.1 , pp. 12-17
    • Vellom, D.C.1    Radic, Z.2    Li, Y.3    Pickering, N.A.4    Camp, S.5    Taylor, P.6
  • 15
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- And butyrylcholinesterase inhibitors
    • DOI 10.1021/bi00096a018
    • Radic Z, Pickering NA, Vellom DC, Camp S, Taylor P. Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry 1993;32:12074-12084. (Pubitemid 23353646)
    • (1993) Biochemistry , vol.32 , Issue.45 , pp. 12074-12084
    • Radic, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 16
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic-Structure of Acetylcholinesterase from Torpedo-Californica - a Prototypic Acetylcholine-Binding Protein. Science 1991;253:872-879. (Pubitemid 21917225)
    • (1991) Science , vol.253 , Issue.5022 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 17
    • 0142039868 scopus 로고    scopus 로고
    • Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products
    • DOI 10.1074/jbc.M210241200
    • Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem 2003;278:41141-141117 (Pubitemid 37280939)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.C.4    Nachon, F.5
  • 19
    • 0031054145 scopus 로고    scopus 로고
    • A single amino acid substitution. Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase
    • Lockridge O, Blong RM, Masson P, Froment MT, Millard CB, Broomfield CA. A single amino acid substitution. Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase. Biochemistry 1997;36:786-795.
    • (1997) Biochemistry , vol.36 , pp. 786-795
    • Lockridge, O.1    Blong, R.M.2    Masson, P.3    Froment, M.T.4    Millard, C.B.5    Broomfield, C.A.6
  • 21
    • 0024052137 scopus 로고
    • Use of serum cholinesterase in severe phosphorus poisoning. Personal experience
    • Cascio C, Comite C, Ghiara M, Lanza G, Ponchione A. Use of serum cholinesterase in severe phosphorus poisoning. Personal experience. Min Anest 1988;54:337-338.
    • (1988) Min Anest , vol.54 , pp. 337-338
    • Cascio, C.1    Comite, C.2    Ghiara, M.3    Lanza, G.4    Ponchione, A.5
  • 22
    • 13444261934 scopus 로고    scopus 로고
    • Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: The crystal structure suggests two alternative mechanisms of aging
    • DOI 10.1021/bi048238d
    • Nachon F, Asojo OA, Borgstahl GE, Masson P, Lockridge O. Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging. Biochemistry 2005;44:1154-1162. (Pubitemid 40208995)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1154-1162
    • Nachon, F.1    Asojo, O.A.2    Borgstahl, G.E.O.3    Masson, P.4    Lockridge, O.5
  • 25
    • 4243810035 scopus 로고
    • Simulation of enzyme reactions using valence bond force fields and other hybrid quantum/classical approaches
    • Aqvist J, Warshel A. Simulation of enzyme-reactions using valence-bond force-fields and other hybrid quantum-classical approaches. Chem Rev 1993;93:2523-2544. (Pubitemid 23989466)
    • (1993) Chemical Reviews , vol.93 , Issue.7 , pp. 2523-2544
    • Aqvist, J.1    Warshel, A.2
  • 26
    • 84962477148 scopus 로고    scopus 로고
    • Structure/function correlations of proteins using MM. QM/MM and related approaches; methods concepts pitfalls and current progress
    • Shurki A, Warshel A. Structure/function correlations of proteins using MM. QM/MM and related approaches; methods concepts pitfalls and current progress. Adv Protein Chem 2003;66:249-313.
    • (2003) Adv Protein Chem , vol.66 , pp. 249-313
    • Shurki, A.1    Warshel, A.2
  • 27
    • 33544471258 scopus 로고    scopus 로고
    • Empirical valence bond and related approaches
    • Schleyer PvR, Jorgensen WL, Schaefer HF III, Schreiner PR, Thiel W, Glen R, editors. New York: Wiley; DOI: 10.1002/0470845015.cu0002
    • Warshel A, Florián J. Empirical valence bond and related approaches. In: Schleyer PvR, Jorgensen WL, Schaefer HF III, Schreiner PR, Thiel W, Glen R, editors. The encyclopedia of computational chemistry. New York: Wiley; 2004. DOI: 10.1002/0470845015.cu0002.
    • (2004) The Encyclopedia of Computational Chemistry
    • Warshel, A.1    Florián, J.2
  • 28
    • 36849122972 scopus 로고
    • High-temperature equation of state by a perturbation method. I. Nonpolar gases
    • Zwanzig RW. High-temperature equation of state by a perturbation method. I. Nonpolar gases. J Chem Phys 1954;22:1420.
    • (1954) J Chem Phys , Issue.22 , pp. 1420
    • Zwanzig, R.W.1
  • 29
    • 0000152754 scopus 로고
    • A guide to Monte Carlo for statistical mechanics: 2. Byways statistical mechanics. Part A: Equilibrium techniques
    • Berne BJ, editor. New York: Plenum Press, chapter 5
    • Valleau JP, Torrie GM. A guide to Monte Carlo for statistical mechanics: 2. Byways statistical mechanics. Part A: Equilibrium techniques. In: Berne BJ, editor. In the series Modern Theoretical Chemistry. New York: Plenum Press, chapter 5; 1977. pp 169-194.
    • (1977) In the Series Modern Theoretical Chemistry , pp. 169-194
    • Valleau, J.P.1    Torrie, G.M.2
  • 30
    • 33845282688 scopus 로고
    • Microscopic examination of free energy relationships for electron transfer in polar solvents
    • Hwang J-K, Warshel A. Microscopic examination of free energy relationships for electron transfer in polar solvents. J Am Chem Soc 1987;109:715-720.
    • (1987) J Am Chem Soc , vol.109 , pp. 715-720
    • Hwang, J.-K.1    Warshel, A.2
  • 31
    • 0041600218 scopus 로고
    • Simulation of free energy relationships and dynamics of SN2 reactions in aqueous solution
    • Hwang J-K, King G, Creighton S, Warshel A. Simulation of free energy relationships and dynamics of SN2 reactions in aqueous solution. J Am Chem Soc 1988;110:5297-5311.
    • (1988) J Am Chem Soc , vol.110 , pp. 5297-5311
    • Hwang, J.-K.1    King, G.2    Creighton, S.3    Warshel, A.4
  • 32
    • 0000354626 scopus 로고
    • Investigation of the free energy functions for electron transfer reactions
    • King G, Warshel A. Investigation of the free energy functions for electron transfer reactions. J Chem Phys 1990;93:8682-8692.
    • (1990) J Chem Phys , vol.93 , pp. 8682-8692
    • King, G.1    Warshel, A.2
  • 33
    • 0000728542 scopus 로고
    • Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the POLARIS and ENZYMIX programs
    • Lee FS, Chu ZT, Warshel A. Microscopic and semimicroscopic calculations of electrostatic energies in proteins by the POLARIS and ENZYMIX programs. J Comput Chem 1993;14:161-185.
    • (1993) J Comput Chem , vol.14 , pp. 161-185
    • Lee, F.S.1    Chu, Z.T.2    Warshel, A.3
  • 35
    • 36549094414 scopus 로고
    • A surface constrained all-atom solvent model for effective simulations of polar solutions
    • King G, Warshel A. A surface constrained all-atom solvent model for effective simulations of polar solutions. J Chem Phys 1989;91: 3647-3661.
    • (1989) J Chem Phys , vol.91 , pp. 3647-3661
    • King, G.1    Warshel, A.2
  • 36
    • 0000115003 scopus 로고
    • A Local Reaction Field Method for Fast Evaluation of Long-Range Electrostatic Interactions in Molecular Simulations
    • Lee FS, Warshel A. A Local Reaction Field Method for Fast Evaluation of Long-Range Electrostatic Interactions in Molecular Simulations. J Chem Phys 1992;97:3100-3107.
    • (1992) J Chem Phys , vol.97 , pp. 3100-3107
    • Lee, F.S.1    Warshel, A.2
  • 38
    • 84946893847 scopus 로고
    • Electrostatic interaction of a solute with a continuum - A direct utilization of abinitio molecular potentials for the prevision of solvent effects
    • Miertus S, Scrocco E, Tomasi J. Electrostatic interaction of a solute with a continuum - a direct utilization of abinitio molecular potentials for the prevision of solvent effects. Chem Phys 1981;55:117-129.
    • (1981) Chem Phys , vol.55 , pp. 117-129
    • Miertus, S.1    Scrocco, E.2    Tomasi, J.3
  • 39
    • 84962432699 scopus 로고
    • Approximate evaluations of the electrostatic free-energy and internal energy changes in solution processes
    • Miertus S, Tomasi J. Approximate evaluations of the electrostatic free-energy and internal energy changes in solution processes. Chem Phys 1982;65:239-245.
    • (1982) Chem Phys , vol.65 , pp. 239-245
    • Miertus, S.1    Tomasi, J.2
  • 40
    • 0021126688 scopus 로고
    • Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine
    • Froede HC, Wilson IB. Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine. J Biol Chem 1984;259:1010-1013.
    • (1984) J Biol Chem , vol.259 , pp. 1010-1013
    • Froede, H.C.1    Wilson, I.B.2
  • 41
    • 84962407693 scopus 로고    scopus 로고
    • Ab initio evaluation of the free energy surfaces for the general base/acid catalyzed thiolysis of formamide and the hydrolysis of methyl thiolformate: A reference solution reaction for studies of cysteine proteases
    • DOI 10.1021/jp010279l
    • Štrajble M, Florián J, Warshel A. Ab initio evaluation of the free energy surfaces for the general base/acid catalyzed thiolysis of formamide and the hydrolysis of methyl thiolformate: a reference solution reaction for studies of cysteine proteases. J Phys Chem B 2001;105:4471-4484. (Pubitemid 35381589)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.19 , pp. 4471-4484
    • Strajbl, M.1    Florian, J.2    Warshel, A.3
  • 42
    • 84962422582 scopus 로고    scopus 로고
    • Origin of the catalytic power of acetylcholinesterase: Computer simulation studies
    • DOI 10.1021/ja972326m
    • Fuxreiter M, Warshel A. Origin of the catalytic power of acetylcholinesterase: computer simulation studies. J Am Chem Soc 1998;120:183-194. (Pubitemid 28046444)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.1 , pp. 183-194
    • Fuxreiter, M.1    Warshel, A.2
  • 43
    • 0037019547 scopus 로고    scopus 로고
    • Role of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: An ab initio QM/MM study
    • DOI 10.1021/ja020243m
    • Zhang YK, Kua J, McCammon JA. Role of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: an ab initio QM/ MM study. J Am Chem Soc 2002;124:10572-10577. (Pubitemid 34977409)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.35 , pp. 10572-10577
    • Zhang, Y.1    Kua, J.2    McCammon, J.A.3
  • 44
    • 0032488593 scopus 로고    scopus 로고
    • Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: Synergy results in a somanase
    • DOI 10.1021/bi972057c
    • Millard CB, Lockridge O, Broomfield CA. Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: synergy results in a somanase. Biochemistry 1998;37:237-247. (Pubitemid 28049126)
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 237-247
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 45
    • 84961983498 scopus 로고    scopus 로고
    • Theoretical studies on the deacylation step of serine protease catalysis in the gas phase, in solution, and in elastase
    • DOI 10.1021/ja047010a
    • Topf M, Richards WG. Theoretical studies on the deacylation step of serine protease catalysis in the gas phase, in solution, and in elastase. J Am Chem Soc 2004;126:14631-14641. (Pubitemid 39463643)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.44 , pp. 14631-14641
    • Topf, M.1    Richards, W.G.2
  • 47
  • 50
    • 0344011673 scopus 로고    scopus 로고
    • Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept (R)) to cholinesterases
    • DOI 10.1046/j.1432-1033.2003.03837.x
    • Saxena A, Fedorko JM, Vinayaka CR, Medhekar R, Radic Z, Taylor P, Lockridge O, Doctor BP. Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept (R)) to cholinesterases. Eur J Biochem 2003;270:4447-4458. (Pubitemid 37452521)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.22 , pp. 4447-4458
    • Saxena, A.1    Fedorko, J.M.2    Vinayaka, C.R.3    Medhekar, R.4    Radic, Z.5    Taylor, P.6    Lockridge, O.7    Doctor, B.P.8
  • 51
    • 0037413712 scopus 로고    scopus 로고
    • Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
    • DOI 10.1093/emboj/cdg005
    • Bourne Y, Taylor P, Radic Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 2003;22:1-12. (Pubitemid 36091264)
    • (2003) EMBO Journal , vol.22 , Issue.1 , pp. 1-12
    • Bourne, Y.1    Taylor, P.2    Radic, Z.3    Marchot, P.4
  • 55
    • 0035964089 scopus 로고    scopus 로고
    • Cleavage of 3 ',5 '-pyrophosphate-linked dinucleotides by ribonuclease a and angiogenin
    • DOI 10.1021/bi010888j
    • Jardine AM, Leonidas DD, Jenkins JL, Park C, Raines RT, Acharya KR, Shapiro R. Cleavage of 3 ',5 '-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin. Biochemistry 2001;40: 10262-10272. (Pubitemid 32800133)
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10262-10272
    • Jardine, A.M.1    Leonidas, D.D.2    Jenkins, J.L.3    Park, C.4    Raines, R.T.5    Acharya, K.R.6    Shapiro, R.7
  • 56
    • 11544373758 scopus 로고    scopus 로고
    • The hydrolysis of RNA: From theoretical calculations to the hammerhead ribozyme-mediated cleavage of RNA
    • Zhou DM, Taira K. The hydrolysis of RNA: From theoretical calculations to the hammerhead ribozyme-mediated cleavage of RNA. Chem Rev 1998;98:991-1026. (Pubitemid 128632234)
    • (1998) Chemical Reviews , vol.98 , Issue.3 , pp. 991-1026
    • Zhou, D.-M.1    Taira, K.2
  • 57
    • 0035808714 scopus 로고    scopus 로고
    • Theoretical studies on the hydrolysis of phosphate diesters in the gas phase, solution, and RNase a
    • DOI 10.1002/qua.1601, Electronic Structure: Predictions and Applications (Part 1)
    • Lopez X, York DM, Dejaegere A, Karplus M. Theoretical studies on the hydrolysis of phosphate diesters in the gas phase, solution, and RNase A. Int J Quantum Chem 2002;86:10-26. (Pubitemid 33148731)
    • (2002) International Journal of Quantum Chemistry , vol.86 , Issue.1 , pp. 10-26
    • Lopez, X.1    York, D.M.2    Dejaegere, A.3    Karplus, M.4


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