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Volumn 187, Issue 1-3, 2010, Pages 135-141

Molecular basis of inhibition of substrate hydrolysis by a ligand bound to the peripheral site of acetylcholinesterase

Author keywords

Acetylcholinesterase; Carbamoylation; Enzyme mechanism; Peripheral site; Substrate analogs; Thioflavin T

Indexed keywords

3 (ACETAMIDO) N,N,N TRIMETHYLANILINIUM; ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; ANILINIUM DERIVATIVE; CARBACHOL; LIGAND; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 77955553053     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.05.009     Document Type: Article
Times cited : (18)

References (29)
  • 1
    • 0016593463 scopus 로고
    • Acetylcholinesterase
    • John Wiley & Sons, New York, A. Meister (Ed.)
    • Rosenberry T.L. Acetylcholinesterase. Advances in Enzymology 1975, 103-218. John Wiley & Sons, New York. A. Meister (Ed.).
    • (1975) Advances in Enzymology , pp. 103-218
    • Rosenberry, T.L.1
  • 2
    • 0001885399 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: from the Calabar bean to Alzheimer therapy
    • Martin Dunitz, London, E. Giacobini (Ed.)
    • Giacobini E. Cholinesterase inhibitors: from the Calabar bean to Alzheimer therapy. Cholinesterases and Cholinesterase Inhibitors 2000, 181-226. Martin Dunitz, London. E. Giacobini (Ed.).
    • (2000) Cholinesterases and Cholinesterase Inhibitors , pp. 181-226
    • Giacobini, E.1
  • 3
    • 0028957265 scopus 로고
    • Anticholinesterases: medical applications of neurochemical principles
    • Millard C.B., Broomfield C.A. 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
    • 0013945471 scopus 로고
    • Responses of acetylcholinesterase from Torpedo marmorata to salts and curarizing drugs
    • Changeux J.-P. Responses of acetylcholinesterase from Torpedo marmorata to salts and curarizing drugs. Mol. Pharmacol. 1966, 2:369-392.
    • (1966) Mol. Pharmacol. , vol.2 , pp. 369-392
    • Changeux, J.-P.1
  • 5
    • 0016823110 scopus 로고
    • Interaction of fluorescence probes with acetylcholinesterase. The site and specificity of propidium binding
    • Taylor P., Lappi S. Interaction of fluorescence probes with acetylcholinesterase. The site and specificity of propidium binding. Biochemistry 1975, 14:1989-1997.
    • (1975) Biochemistry , vol.14 , pp. 1989-1997
    • Taylor, P.1    Lappi, S.2
  • 6
    • 0035968202 scopus 로고    scopus 로고
    • Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites
    • De Ferrari G.V., Mallender W.D., Inestrosa N.C., Rosenberry T.L. Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites. J. Biol. Chem. 2001, 276:23282-23287.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23282-23287
    • De Ferrari, G.V.1    Mallender, W.D.2    Inestrosa, N.C.3    Rosenberry, T.L.4
  • 7
    • 57449090909 scopus 로고    scopus 로고
    • Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter
    • Rosenberry T.L., Sonoda L.K., Dekat S.E., Cusack B., Johnson J.L. Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter. Biochemistry 2008, 47:13056-13063.
    • (2008) Biochemistry , vol.47 , pp. 13056-13063
    • Rosenberry, T.L.1    Sonoda, L.K.2    Dekat, S.E.3    Cusack, B.4    Johnson, J.L.5
  • 8
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
    • 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. Science 1991, 253:872-879.
    • (1991) Science , 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
  • 9
    • 15844422678 scopus 로고    scopus 로고
    • The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase
    • Harel M., Quinn D.M., Nair H.K., Silman I., Sussman J.L. The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. J. Am. Chem. Soc. 1996, 118:2340-2346.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2340-2346
    • Harel, M.1    Quinn, D.M.2    Nair, H.K.3    Silman, I.4    Sussman, J.L.5
  • 10
    • 45749094206 scopus 로고    scopus 로고
    • The crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site
    • Harel M., Sonoda L.K., Silman I., Sussman J.L., Rosenberry T.L. The crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site. J. Am. Chem. Soc. 2008, 130:7856-7861.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7856-7861
    • Harel, M.1    Sonoda, L.K.2    Silman, I.3    Sussman, J.L.4    Rosenberry, T.L.5
  • 11
    • 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
  • 12
    • 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.G., 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.G.3    Silman, I.4    Sussman, J.L.5
  • 13
    • 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
  • 14
    • 0032402388 scopus 로고    scopus 로고
    • Rapid binding of a cationic active site inhibitor to wild type and mutant mouse acetylcholinesterase: Brownian dynamics simulation including diffusion in the active site gorge
    • Tara S., Elcock A.H., Kirchhoff P.D., Briggs J.M., Radic Z., Taylor P., McCammon J.A. Rapid binding of a cationic active site inhibitor to wild type and mutant mouse acetylcholinesterase: Brownian dynamics simulation including diffusion in the active site gorge. Biopolymers 1998, 46:465-474.
    • (1998) Biopolymers , vol.46 , pp. 465-474
    • Tara, S.1    Elcock, A.H.2    Kirchhoff, P.D.3    Briggs, J.M.4    Radic, Z.5    Taylor, P.6    McCammon, J.A.7
  • 15
    • 0033524414 scopus 로고    scopus 로고
    • Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect
    • Szegletes T., Mallender W.D., Thomas P.J., Rosenberry T.L. Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 1999, 38:122-133.
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallender, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4
  • 16
    • 0034604236 scopus 로고    scopus 로고
    • Acetylthiocholine binds to Asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway
    • Mallender W.D., Szegletes T., Rosenberry T.L. Acetylthiocholine binds to Asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway. Biochemistry 2000, 39:7753-7763.
    • (2000) Biochemistry , vol.39 , pp. 7753-7763
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 17
    • 0038219567 scopus 로고    scopus 로고
    • Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate
    • Johnson J.L., Cusack B., Davies M.P., Fauq A., Rosenberry T.L. Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate. Biochemistry 2003, 42:5438-5452.
    • (2003) Biochemistry , vol.42 , pp. 5438-5452
    • Johnson, J.L.1    Cusack, B.2    Davies, M.P.3    Fauq, A.4    Rosenberry, T.L.5
  • 18
    • 9644273861 scopus 로고    scopus 로고
    • Rational polynomial equation as an unbiased approach for the kinetic studies of Drosophila melanogaster acetylcholinesterase reaction mechanism
    • Stojan J., Golicnik M., Fournier D. Rational polynomial equation as an unbiased approach for the kinetic studies of Drosophila melanogaster acetylcholinesterase reaction mechanism. Biochim. Biophys. Acta 2004, 1703:53-61.
    • (2004) Biochim. Biophys. Acta , vol.1703 , pp. 53-61
    • Stojan, J.1    Golicnik, M.2    Fournier, D.3
  • 19
    • 74949105263 scopus 로고    scopus 로고
    • Strategies to resolve the catalytic mechanism of acetylcholinesterase
    • Rosenberry T.L. Strategies to resolve the catalytic mechanism of acetylcholinesterase. J. Mol. Neurosci. 2010, 40:32-39.
    • (2010) J. Mol. Neurosci. , vol.40 , pp. 32-39
    • Rosenberry, T.L.1
  • 20
    • 33845282579 scopus 로고
    • Enzyme structure, reaction dynamics, and virtual transition states
    • Quinn D.M., 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
  • 21
    • 0033605661 scopus 로고    scopus 로고
    • Organophosphorylation of acetylcholinesterase in the presence of peripheral site ligands: distinct effects of propidium and fasciculin
    • Mallender W.D., Szegletes T., Rosenberry T.L. Organophosphorylation of acetylcholinesterase in the presence of peripheral site ligands: distinct effects of propidium and fasciculin. J. Biol. Chem. 1999, 274:8491-8499.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8491-8499
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 22
    • 0029092671 scopus 로고
    • Fasciculin 2 binds to a peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation
    • Eastman J., Wilson E.J., Cervenansky C., Rosenberry T.L. Fasciculin 2 binds to a peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation. J. Biol. Chem. 1995, 270:19694-19701.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19694-19701
    • Eastman, J.1    Wilson, E.J.2    Cervenansky, C.3    Rosenberry, T.L.4
  • 23
    • 0000140355 scopus 로고    scopus 로고
    • Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands
    • Szegletes T., Mallender W.D., Rosenberry T.L. Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands. Biochemistry 1998, 37:4206-4216.
    • (1998) Biochemistry , vol.37 , pp. 4206-4216
    • Szegletes, T.1    Mallender, W.D.2    Rosenberry, T.L.3
  • 24
    • 50649109814 scopus 로고    scopus 로고
    • Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis
    • Rosenberry T.L., Sonoda L.K., Dekat S.E., Cusack B., Johnson J.L. Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis. Chem. Biol. Interact. 2008, 175:235-241.
    • (2008) Chem. Biol. Interact. , vol.175 , pp. 235-241
    • Rosenberry, T.L.1    Sonoda, L.K.2    Dekat, S.E.3    Cusack, B.4    Johnson, J.L.5
  • 27
    • 0027092277 scopus 로고
    • Ambenonium is a rapidly reversible noncovalent inhibitor of acetylcholinesterase with one of the highest known affinities
    • Hodge A.S., Humphrey D.R., Rosenberry T.L. Ambenonium is a rapidly reversible noncovalent inhibitor of acetylcholinesterase with one of the highest known affinities. Mol. Pharmacol. 1992, 41:937-942.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 937-942
    • Hodge, A.S.1    Humphrey, D.R.2    Rosenberry, T.L.3
  • 28
    • 0033966913 scopus 로고    scopus 로고
    • Huprine X is a novel high affinity inhibitor of acetylcholinesterase that is of interest for the treatment of Alzheimer's disease
    • Camps P., Cusack B., Mallender W.D., El Achab R., Morral J., Muñoz-Torrero D., Rosenberry T.L. Huprine X is a novel high affinity inhibitor of acetylcholinesterase that is of interest for the treatment of Alzheimer's disease. Mol. Pharmacol. 2000, 57:409-417.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 409-417
    • Camps, P.1    Cusack, B.2    Mallender, W.D.3    El Achab, R.4    Morral, J.5    Muñoz-Torrero, D.6    Rosenberry, T.L.7
  • 29
    • 0018839204 scopus 로고
    • Modulation of acetylcholinesterase activity by peripheral site ligands
    • Tomlinson G., Mutus B., McLennan I. Modulation of acetylcholinesterase activity by peripheral site ligands. Mol. Pharmacol. 1980, 18:33-39.
    • (1980) Mol. Pharmacol. , vol.18 , pp. 33-39
    • Tomlinson, G.1    Mutus, B.2    McLennan, I.3


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