메뉴 건너뛰기




Volumn 53, Issue 10, 2010, Pages 4002-4008

Structural evidence that human acetylcholinesterase inhibited by tabun ages through O-dealkylation

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE INHIBITOR; FASCICULIN; TABUN;

EID: 77952718967     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm901853b     Document Type: Article
Times cited : (92)

References (52)
  • 1
    • 0021737985 scopus 로고
    • Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps
    • Karlsson, E.; Mbugua, P. M.; Rodriguez-Ithurralde, D. Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps J. Physiol. (Paris) 1984, 79, 232-240
    • (1984) J. Physiol. (Paris) , vol.79 , pp. 232-240
    • Karlsson, E.1    Mbugua, P.M.2    Rodriguez-Ithurralde, D.3
  • 2
    • 0642309501 scopus 로고    scopus 로고
    • Acetylcholinesterase: A multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimers disease
    • Greenblatt, H. M.; Dvir, H.; Silman, I.; Sussman, J. L. Acetylcholinesterase: A multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimers disease J. Mol. Neurosci. 2003, 20, 369-383
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 369-383
    • Greenblatt, H.M.1    Dvir, H.2    Silman, I.3    Sussman, J.L.4
  • 3
    • 0032439404 scopus 로고    scopus 로고
    • Experimental and clinical toxicology of anticholinesterase agents
    • Moretto, A. Experimental and clinical toxicology of anticholinesterase agents Toxicol. Lett. 1998, 102-103, 509-513
    • (1998) Toxicol. Lett. , vol.102-103 , pp. 509-513
    • Moretto, A.1
  • 6
    • 34547447574 scopus 로고    scopus 로고
    • Acute pesticide poisoning-A global public health problem
    • Konradsen, F. Acute pesticide poisoning-A global public health problem Danish Med. Bull. 2007, 54, 58-59
    • (2007) Danish Med. Bull. , vol.54 , pp. 58-59
    • Konradsen, F.1
  • 7
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding
    • Sussman, J. L.; Harel, M.; Frolow, F.; Oefner, C.; Goldman, A.; Toker, L.; Silman, I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding Protein Sci. 1991, 253, 872-879
    • (1991) Protein Sci. , vol.253 , 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
  • 8
    • 7444221716 scopus 로고    scopus 로고
    • Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes
    • Worek, F.; Thiermann, H.; Szinicz, L.; Eyer, P. Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes Biochem. Pharmacol. 2004, 68, 2237-2248
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 2237-2248
    • Worek, F.1    Thiermann, H.2    Szinicz, L.3    Eyer, P.4
  • 10
    • 0000976597 scopus 로고
    • On the mechanism of ageing of phosphonylated cholinesterases
    • Benschop, H. P.; Keijer, J. H. On the mechanism of ageing of phosphonylated cholinesterases Biochim. Biophys. Acta 1966, 128, 586-588
    • (1966) Biochim. Biophys. Acta , vol.128 , pp. 586-588
    • Benschop, H.P.1    Keijer, J.H.2
  • 11
    • 35448956936 scopus 로고    scopus 로고
    • Aging pathways for organophosphate-inhibited human butyrylcholinesterase, including novel pathways for isomalathion, resolved by mass spectrometry
    • Li, H.; Schopfer, L. M.; Nachon, F.; Froment, M. T.; Masson, P.; Lockridge, O. Aging pathways for organophosphate-inhibited human butyrylcholinesterase, including novel pathways for isomalathion, resolved by mass spectrometry Toxicol. Sci. 2007, 100, 136-145
    • (2007) Toxicol. Sci. , vol.100 , pp. 136-145
    • Li, H.1    Schopfer, L.M.2    Nachon, F.3    Froment, M.T.4    Masson, P.5    Lockridge, O.6
  • 14
    • 0033610449 scopus 로고    scopus 로고
    • Reaction products of acetylcholinesterase and vx reveal a mobile histidine in the catalytic triad
    • Millard, C. B.; Koellner, G.; Ordentlich, A.; Shafferman, A.; Silman, I.; Sussman, J. L. Reaction Products of Acetylcholinesterase and VX Reveal a Mobile Histidine in the Catalytic Triad J. Am. Chem. Soc. 1999, 121, 9983-9984
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9983-9984
    • Millard, C.B.1    Koellner, G.2    Ordentlich, A.3    Shafferman, A.4    Silman, I.5    Sussman, J.L.6
  • 15
    • 34247550159 scopus 로고    scopus 로고
    • Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state
    • Hornberg, A.; Tunemalm, A. K.; Ekstrom, F. Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state Biochemistry 2007, 46, 4815-4825
    • (2007) Biochemistry , vol.46 , pp. 4815-4825
    • Hornberg, A.1    Tunemalm, A.K.2    Ekstrom, F.3
  • 17
    • 69549106972 scopus 로고    scopus 로고
    • Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime (dagger)
    • Sanson, B.; Nachon, F.; Colletier, J. P.; Froment, M. T.; Toker, L.; Greenblatt, H. M.; Sussman, J. L.; Ashani, Y.; Masson, P.; Silman, I.; Weik, M. Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime (dagger) J. Med. Chem. 2009, 52, 7593-7603
    • (2009) J. Med. Chem. , vol.52 , pp. 7593-7603
    • Sanson, B.1    Nachon, F.2    Colletier, J.P.3    Froment, M.T.4    Toker, L.5    Greenblatt, H.M.6    Sussman, J.L.7    Ashani, Y.8    Masson, P.9    Silman, I.10    Weik, M.11
  • 18
    • 67650099505 scopus 로고    scopus 로고
    • Structure of HI-6 sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: Reactivator mechanism and design
    • Ekstrom, F.; Hornberg, A.; Artursson, E.; Hammarstrom, L. G.; Schneider, G.; Pang, Y. P. Structure of HI-6 sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: Reactivator mechanism and design PLoS One 2009, 4, e5957
    • (2009) PLoS One , vol.4 , pp. 5957
    • Ekstrom, F.1    Hornberg, A.2    Artursson, E.3    Hammarstrom, L.G.4    Schneider, G.5    Pang, Y.P.6
  • 19
    • 34547866680 scopus 로고    scopus 로고
    • Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes
    • Ekstrom, F. J.; Astot, C.; Pang, Y. P. Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes Clin. Pharmacol. Ther. 2007, 82, 282-293
    • (2007) Clin. Pharmacol. Ther. , vol.82 , pp. 282-293
    • Ekstrom, F.J.1    Astot, C.2    Pang, Y.P.3
  • 20
    • 34247165881 scopus 로고    scopus 로고
    • Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by different phosphoramidates
    • Worek, F.; Aurbek, N.; Koller, M.; Becker, C.; Eyer, P.; Thiermann, H. Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by different phosphoramidates Biochem. Pharmacol. 2007, 73, 1807-1817
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 1807-1817
    • Worek, F.1    Aurbek, N.2    Koller, M.3    Becker, C.4    Eyer, P.5    Thiermann, H.6
  • 21
    • 0034933842 scopus 로고    scopus 로고
    • Resolving pathways of interaction of covalent inhibitors with the active site of acetylcholinesterases: MALDI-TOF/MS analysis of various nerve agent phosphyl adducts
    • Elhanany, E.; Ordentlich, A.; Dgany, O.; Kaplan, D.; Segall, Y.; Barak, R.; Velan, B.; Shafferman, A. Resolving pathways of interaction of covalent inhibitors with the active site of acetylcholinesterases: MALDI-TOF/MS analysis of various nerve agent phosphyl adducts Chem. Res. Toxicol. 2001, 14, 912-918
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 912-918
    • Elhanany, E.1    Ordentlich, A.2    Dgany, O.3    Kaplan, D.4    Segall, Y.5    Barak, R.6    Velan, B.7    Shafferman, A.8
  • 22
    • 30144445702 scopus 로고    scopus 로고
    • Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase
    • Ekstrom, F.; Akfur, C.; Tunemalm, A. K.; Lundberg, S. Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase Biochemistry 2006, 45, 74-81
    • (2006) Biochemistry , vol.45 , pp. 74-81
    • Ekstrom, F.1    Akfur, C.2    Tunemalm, A.K.3    Lundberg, S.4
  • 23
    • 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
    • Nachon, F.; Asojo, O. A.; Borgstahl, G. E.; 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
    • (2005) Biochemistry , vol.44 , pp. 1154-1162
    • Nachon, F.1    Asojo, O.A.2    Borgstahl, G.E.3    Masson, P.4    Lockridge, O.5
  • 26
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
    • Bourne, Y.; Taylor, P.; Marchot, P. Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex Cell 1995, 83, 503-512
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 27
    • 0029646114 scopus 로고
    • Crystal structure of an acetylcholinesterase-fasciculin complex: Interaction of a three-fingered toxin from snake venom with its target
    • Harel, M.; Kleywegt, G. J.; Ravelli, R. B.; Silman, I.; Sussman, J. L. Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target Structure 1995, 3, 1355-1366
    • (1995) Structure , vol.3 , pp. 1355-1366
    • Harel, M.1    Kleywegt, G.J.2    Ravelli, R.B.3    Silman, I.4    Sussman, J.L.5
  • 28
    • 0021338810 scopus 로고
    • Structure of human erythrocyte acetylcholinesterase. Characterization of intersubunit disulfide bonding and detergent interaction
    • Rosenberry, T. L.; Scoggin, D. M. Structure of human erythrocyte acetylcholinesterase. Characterization of intersubunit disulfide bonding and detergent interaction J. Biol. Chem. 1984, 259, 5643-5652
    • (1984) J. Biol. Chem. , vol.259 , pp. 5643-5652
    • Rosenberry, T.L.1    Scoggin, D.M.2
  • 29
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo, M. C.; Aulabaugh, A.; Jin, G.; Cowling, R.; Bard, J.; Malamas, M.; Ellestad, G. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery Anal. Biochem. 2004, 332, 153-159
    • (2004) Anal. Biochem. , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 36
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J.; Merritt, E. A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006, 62, 439-450
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 38
    • 0006332887 scopus 로고
    • Enantiospecific complexation gas chromatography of nerve agents. Isolation and properties of the enantiomers of ethyl N,N- dimethylphosphoramidocyanidate (tabun)
    • Degenhardt, C. E.; Van Den Berg, G. R.; De Jong, L. P. A.; Benschop, H. P.; Van Genderen, J.; Van De Meent, D. Enantiospecific complexation gas chromatography of nerve agents. Isolation and properties of the enantiomers of ethyl N,N-dimethylphosphoramidocyanidate (tabun) J. Am. Chem. Soc. 1986, 108, 8290-8291
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 8290-8291
    • Degenhardt, C.E.1    Van Den Berg, G.R.2    De Jong, L.P.A.3    Benschop, H.P.4    Van Genderen, J.5    Van De Meent, D.6
  • 39
    • 0021708080 scopus 로고
    • Stereochemical aspects of cholinesterase catalysis
    • Järv, J. Stereochemical aspects of cholinesterase catalysis Bioorg. Chem. 1984, 12, 259-278
    • (1984) Bioorg. Chem. , vol.12 , pp. 259-278
    • Järv, J.1
  • 40
    • 67650799940 scopus 로고    scopus 로고
    • Fixation of the two tabun isomers in acetylcholinesterase: A QM/MM study
    • Kwasnieski, O.; Verdier, L.; Malacria, M.; Derat, E. Fixation of the two tabun isomers in acetylcholinesterase: A QM/MM study J. Phys. Chem. B 2009, 113, 10001-10007
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10001-10007
    • Kwasnieski, O.1    Verdier, L.2    Malacria, M.3    Derat, E.4
  • 41
    • 28744432143 scopus 로고    scopus 로고
    • The stereochemistry of the inhibition of acetylcholinesterase with acetylcholine-mimetic 7-aza-2,4-dioxaphosphadecalins
    • Furegati, S.; Zerbe, O.; Ruedi, P. The stereochemistry of the inhibition of acetylcholinesterase with acetylcholine-mimetic 7-aza-2,4- dioxaphosphadecalins Chem.-Biol. Interact. 2005, 157-158, 418-420
    • (2005) Chem.-Biol. Interact. , vol.157-158 , pp. 418-420
    • Furegati, S.1    Zerbe, O.2    Ruedi, P.3
  • 42
    • 0037413712 scopus 로고    scopus 로고
    • Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
    • 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
    • (2003) EMBO J. , vol.22 , pp. 1-12
    • Bourne, Y.1    Taylor, P.2    Radic, Z.3    Marchot, P.4
  • 45
    • 1542533734 scopus 로고    scopus 로고
    • Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase?
    • Kaplan, D.; Barak, D.; Ordentlich, A.; Kronman, C.; Velan, B.; Shafferman, A. Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase? Biochemistry 2004, 43, 3129-3136
    • (2004) Biochemistry , vol.43 , pp. 3129-3136
    • Kaplan, D.1    Barak, D.2    Ordentlich, A.3    Kronman, C.4    Velan, B.5    Shafferman, A.6
  • 46
    • 70449637196 scopus 로고    scopus 로고
    • Crystal structures of oxime-bound fenamiphos-acetylcholinesterases: Reactivation involving flipping of the His447 ring to form a reactive Glu334-His447-oxime triad
    • Hornberg, A.; Artursson, E.; Warme, R.; Pang, Y. P.; Ekstrom, F. Crystal structures of oxime-bound fenamiphos-acetylcholinesterases: reactivation involving flipping of the His447 ring to form a reactive Glu334-His447-oxime triad Biochem. Pharmacol. 2010, 79, 507-515
    • (2010) Biochem. Pharmacol. , vol.79 , pp. 507-515
    • Hornberg, A.1    Artursson, E.2    Warme, R.3    Pang, Y.P.4    Ekstrom, F.5
  • 48
    • 0029742777 scopus 로고    scopus 로고
    • Aging of phosphylated human acetylcholinesterase: Catalytic processes mediated by aromatic and polar residues of the active centre
    • Shafferman, A.; Ordentlich, A.; Barak, D.; Stein, D.; Ariel, N.; Velan, B. Aging of phosphylated human acetylcholinesterase: catalytic processes mediated by aromatic and polar residues of the active centre Biochem. J. 1996, 318 (Part 3) 833-840
    • (1996) Biochem. J. , vol.318 , Issue.PART 3 , pp. 833-840
    • Shafferman, A.1    Ordentlich, A.2    Barak, D.3    Stein, D.4    Ariel, N.5    Velan, B.6
  • 50
    • 77952710487 scopus 로고    scopus 로고
    • International Meeting on Cholinesterases, Sibenik, Croatia, oral communication
    • Shafferman, A. Next generation of OP-bioscavengers. International Meeting on Cholinesterases, Sibenik, Croatia 2009, oral communication.
    • (2009) Next Generation of OP-bioscavengers
    • Shafferman, A.1
  • 51
    • 2442769298 scopus 로고    scopus 로고
    • Hydration change during the aging of phosphorylated human butyrylcholinesterase: Importance of residues aspartate-70 and glutamate-197 in the water network as probed by hydrostatic and osmotic pressures
    • Masson, P.; Clery, C.; Guerra, P.; Redslob, A.; Albaret, C.; Fortier, P. L. Hydration change during the aging of phosphorylated human butyrylcholinesterase: importance of residues aspartate-70 and glutamate-197 in the water network as probed by hydrostatic and osmotic pressures Biochem. J. 1999, 343 (Part 2) 361-369
    • (1999) Biochem. J. , vol.343 , Issue.PART 2 , pp. 361-369
    • Masson, P.1    Clery, C.2    Guerra, P.3    Redslob, A.4    Albaret, C.5    Fortier, P.L.6
  • 52
    • 32244447946 scopus 로고    scopus 로고
    • Capillary electrophoresis versus differential scanning calorimetry for the analysis of free enzyme versus enzyme-ligand complexes: In the search of the ligand-free status of cholinesterases
    • Rochu, D.; Clery-Barraud, C.; Renault, F.; Chevalier, A.; Bon, C.; Masson, P. Capillary electrophoresis versus differential scanning calorimetry for the analysis of free enzyme versus enzyme-ligand complexes: in the search of the ligand-free status of cholinesterases Electrophoresis 2006, 27, 442-451
    • (2006) Electrophoresis , vol.27 , pp. 442-451
    • Rochu, D.1    Clery-Barraud, C.2    Renault, F.3    Chevalier, A.4    Bon, C.5    Masson, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.