메뉴 건너뛰기




Volumn 187, Issue 1-3, 2010, Pages 44-48

Aging mechanism of butyrylcholinesterase inhibited by an N-methyl analogue of tabun: Implications of the trigonal-bipyramidal transition state rearrangement for the phosphylation or reactivation of cholinesterases

Author keywords

Acetylcholinesterase; Aging; Butyrylcholinesterase; Nerve agents; Reactivation; Transition state

Indexed keywords

CHOLINESTERASE; N METHYLETHYLPHOSPHORAMIDOFLUORIDATE; OXIME; TABUN; UNCLASSIFIED DRUG;

EID: 77955551992     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.03.053     Document Type: Article
Times cited : (20)

References (26)
  • 2
    • 0034009408 scopus 로고    scopus 로고
    • Pesticides and susceptible populations: people with butyrylcholinesterase genetic variants may be at risk
    • Lockridge O., Masson P. Pesticides and susceptible populations: people with butyrylcholinesterase genetic variants may be at risk. Neurotoxicology 2000, 21(1-2):113-126.
    • (2000) Neurotoxicology , vol.21 , Issue.1-2 , pp. 113-126
    • Lockridge, O.1    Masson, P.2
  • 3
    • 63449083967 scopus 로고    scopus 로고
    • Suitability of human butyrylcholinesterase as therapeutic marker and pseudo catalytic scavenger in organophosphate poisoning: a kinetic analysis
    • Aurbek N., Thiermann H., Eyer F., Eyer P., Worek F. Suitability of human butyrylcholinesterase as therapeutic marker and pseudo catalytic scavenger in organophosphate poisoning: a kinetic analysis. Toxicology 2009, 259(3):133-139.
    • (2009) Toxicology , vol.259 , Issue.3 , pp. 133-139
    • Aurbek, N.1    Thiermann, H.2    Eyer, F.3    Eyer, P.4    Worek, F.5
  • 4
    • 0021708080 scopus 로고
    • Stereochemical aspects of cholinesterase catalysis
    • Järv J. Stereochemical aspects of cholinesterase catalysis. Bioorg. Chem. 1984, 12(4):259-278.
    • (1984) Bioorg. Chem. , vol.12 , Issue.4 , pp. 259-278
    • Järv, J.1
  • 5
    • 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(11):2237-2248.
    • (2004) Biochem. Pharmacol. , vol.68 , Issue.11 , pp. 2237-2248
    • Worek, F.1    Thiermann, H.2    Szinicz, L.3    Eyer, P.4
  • 6
    • 0000527858 scopus 로고
    • The chemical basis of the " ageing process" of DFP-inhibited pseudocholinesterase
    • Berends F, Posthumus C.H., Sluys I.v.d., Deierkauf F.A. The chemical basis of the " ageing process" of DFP-inhibited pseudocholinesterase. Biochim. Biophys. Acta 1959, 34:567-568.
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 567-568
    • Berends, F.1    Posthumus, C.H.2    Sluys, I.3    Deierkauf, F.A.4
  • 9
    • 0029116116 scopus 로고
    • Origins and diversity of the aging reaction in phosphonate adducts of serine hydrolase enzymes: what characteristics of the active site do they probe?
    • Bencsura A., Enyedy I., Kovach I.M. Origins and diversity of the aging reaction in phosphonate adducts of serine hydrolase enzymes: what characteristics of the active site do they probe?. Biochemistry 1995, 34(28):8989-8999.
    • (1995) Biochemistry , vol.34 , Issue.28 , pp. 8989-8999
    • Bencsura, A.1    Enyedy, I.2    Kovach, I.M.3
  • 10
    • 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(Pt 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
  • 11
    • 0027728990 scopus 로고
    • Direct observation and elucidation of the structures of aged and nonaged phosphorylated cholinesterases by 31P NMR spectroscopy
    • Segall Y., Waysbort D., Barak D., Ariel N., Doctor B.P., Grunwald J., Ashani Y. Direct observation and elucidation of the structures of aged and nonaged phosphorylated cholinesterases by 31P NMR spectroscopy. Biochemistry 1993, 32(49):13441-13450.
    • (1993) Biochemistry , vol.32 , Issue.49 , pp. 13441-13450
    • Segall, Y.1    Waysbort, D.2    Barak, D.3    Ariel, N.4    Doctor, B.P.5    Grunwald, J.6    Ashani, Y.7
  • 12
    • 0034488760 scopus 로고    scopus 로고
    • Inhibition of acetylcholinesterase by (1S, 3S)-isomalathion proceeds with loss of thiomethyl: kinetic and mass spectral evidence for an unexpected primary leaving group
    • Doorn J.A., Gage D.A., Schall M., Talley T.T., Thompson C.M., Richardson R.J. Inhibition of acetylcholinesterase by (1S, 3S)-isomalathion proceeds with loss of thiomethyl: kinetic and mass spectral evidence for an unexpected primary leaving group. Chem. Res. Toxicol. 2000, 13(12):1313-1320.
    • (2000) Chem. Res. Toxicol. , vol.13 , Issue.12 , pp. 1313-1320
    • Doorn, J.A.1    Gage, D.A.2    Schall, M.3    Talley, T.T.4    Thompson, C.M.5    Richardson, R.J.6
  • 13
    • 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(4):1154-1162.
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1154-1162
    • Nachon, F.1    Asojo, O.A.2    Borgstahl, G.E.3    Masson, P.4    Lockridge, O.5
  • 14
    • 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(1):136-145.
    • (2007) Toxicol. Sci. , vol.100 , Issue.1 , pp. 136-145
    • Li, H.1    Schopfer, L.M.2    Nachon, F.3    Froment, M.T.4    Masson, P.5    Lockridge, O.6
  • 15
    • 34047272804 scopus 로고    scopus 로고
    • Mechanism of aging of mipafox-inhibited butyrylcholinesterase
    • Kropp T.J, Richardson R.J. Mechanism of aging of mipafox-inhibited butyrylcholinesterase. Chem. Res. Toxicol. 2007, 20(3):504-510.
    • (2007) Chem. Res. Toxicol. , vol.20 , Issue.3 , pp. 504-510
    • Kropp, T.J.1    Richardson, R.J.2
  • 16
    • 33644528740 scopus 로고    scopus 로고
    • Aging of mipafox-inhibited human acetylcholinesterase proceeds by displacement of both isopropylamine groups to yield a phosphate adduct
    • Kropp T.J., Richardson R.J. Aging of mipafox-inhibited human acetylcholinesterase proceeds by displacement of both isopropylamine groups to yield a phosphate adduct. Chem. Res. Toxicol. 2006, 19(2):334-339.
    • (2006) Chem. Res. Toxicol. , vol.19 , Issue.2 , pp. 334-339
    • Kropp, T.J.1    Richardson, R.J.2
  • 17
    • 1642283190 scopus 로고    scopus 로고
    • The mipafox-inhibited catalytic domain of human neuropathy target esterase ages by reversible proton loss
    • Kropp T.J., Glynn P., Richardson R.J. The mipafox-inhibited catalytic domain of human neuropathy target esterase ages by reversible proton loss. Biochemistry 2004, 43(12):3716-3722.
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3716-3722
    • Kropp, T.J.1    Glynn, P.2    Richardson, R.J.3
  • 19
    • 15944383182 scopus 로고
    • Correlation of rates of intramolecular tunneling processes, with application to some group V compounds
    • Berry R.S. Correlation of rates of intramolecular tunneling processes, with application to some group V compounds. J. Chem. Phys. 1960, 32(3).
    • (1960) J. Chem. Phys. , vol.32 , Issue.3
    • Berry, R.S.1
  • 20
    • 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(29):10001-10007.
    • (2009) J. Phys. Chem. B , vol.113 , Issue.29 , pp. 10001-10007
    • Kwasnieski, O.1    Verdier, L.2    Malacria, M.3    Derat, E.4
  • 21
    • 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(42):9983-9984.
    • (1999) J. Am. Chem. Soc. , vol.121 , Issue.42 , pp. 9983-9984
    • Millard, C.B.1    Koellner, G.2    Ordentlich, A.3    Shafferman, A.4    Silman, I.5    Sussman, J.L.6
  • 23
    • 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
    • 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. J. Med. Chem. 2009, 52(23):7593-7603.
    • (2009) J. Med. Chem. , vol.52 , Issue.23 , 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
  • 24
    • 67650099505 scopus 로고    scopus 로고
    • Structure of HI-6sarin-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-6sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: reactivator mechanism and design. PLoS One 2009, 4(6):e5957.
    • (2009) PLoS One , vol.4 , Issue.6
    • Ekstrom, F.1    Hornberg, A.2    Artursson, E.3    Hammarstrom, L.G.4    Schneider, G.5    Pang, Y.P.6
  • 25
    • 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(3):282-293.
    • (2007) Clin. Pharmacol. Ther. , vol.82 , Issue.3 , pp. 282-293
    • Ekstrom, F.J.1    Astot, C.2    Pang, Y.P.3
  • 26
    • 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(3):507-515.
    • (2010) Biochem. Pharmacol. , vol.79 , Issue.3 , pp. 507-515
    • Hornberg, A.1    Artursson, E.2    Warme, R.3    Pang, Y.P.4    Ekstrom, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.