메뉴 건너뛰기




Volumn 275, Issue 10, 2008, Pages 2659-2664

Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel

Author keywords

Acetycholinesterase; Back door; Inhibition; Substrate; Traffic

Indexed keywords

ACETYLCHOLINESTERASE; ALANINE; GLUTAMINE; TRYPTOPHAN;

EID: 42649083300     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06413.x     Document Type: Article
Times cited : (21)

References (29)
  • 1
    • 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 (1991) Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 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
  • 2
    • 1942520265 scopus 로고    scopus 로고
    • Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate
    • Stojan J, Brochier L, Alies C, Colletier JP Fournier D (2004) Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate. Eur J Biochem 271, 1364 1371.
    • (2004) Eur J Biochem , vol.271 , pp. 1364-1371
    • Stojan, J.1    Brochier, L.2    Alies, C.3    Colletier, J.P.4    Fournier, D.5
  • 3
    • 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 WD, Szegletes T Rosenberry TL (2000) Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway. Biochemistry 39, 7753 7763.
    • (2000) Biochemistry , vol.39 , pp. 7753-7763
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 6
    • 0028171404 scopus 로고
    • The 'back door' hypothesis for product clearance in acetylcholinesterase challenged by site-directed mutagenesis
    • Kronman C, Ordentlich A, Barak D, Velan B Shafferman A (1994) The 'back door' hypothesis for product clearance in acetylcholinesterase challenged by site-directed mutagenesis. J Biol Chem 269, 27819 27822.
    • (1994) J Biol Chem , vol.269 , pp. 27819-27822
    • Kronman, C.1    Ordentlich, A.2    Barak, D.3    Velan, B.4    Shafferman, A.5
  • 8
    • 0037140969 scopus 로고    scopus 로고
    • Multi-step analysis as a tool for kinetic parameter estimation and mechanism discrimination in the reaction between tight-binding fasciculin 2 and electric eel acetylcholinesterase
    • Golicnik M Stojan J (2002) Multi-step analysis as a tool for kinetic parameter estimation and mechanism discrimination in the reaction between tight-binding fasciculin 2 and electric eel acetylcholinesterase. Biochim Biophys Acta 1597, 164 172.
    • (2002) Biochim Biophys Acta , vol.1597 , pp. 164-172
    • Golicnik, M.1    Stojan, J.2
  • 9
    • 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 WD, Thomas PJ Rosenberry TL (1999) Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 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
  • 11
    • 42649103898 scopus 로고    scopus 로고
    • A second look at the crystal structures of Drosophila melanogaster acetylcholinesterase: Evidence for backdoor opening and stabilization of an enzyme/carboxylate complex
    • 6-10 May, Suzhou
    • Nachon F, Nicolet Y, Harel M, Rosenberry TL, Masson P, Silman I Sussman JL (2007) A second look at the crystal structures of Drosophila melanogaster acetylcholinesterase: evidence for backdoor opening and stabilization of an enzyme/carboxylate complex. Abstracts, IXth International Meeting on Cholinesterases, 6-10 May, Suzhou, p. 113.
    • (2007) Abstracts, IXth International Meeting on Cholinesterases , pp. 113
    • Nachon, F.1    Nicolet, Y.2    Harel, M.3    Rosenberry, T.L.4    Masson, P.5    Silman, I.6    Sussman, J.L.7
  • 12
    • 33749402097 scopus 로고    scopus 로고
    • Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding
    • Bourne Y, Radic Z, Sulzenbacher G, Kim E, Taylor P Marchot P (2006) Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding. J Biol Chem 281, 29256 29267.
    • (2006) J Biol Chem , vol.281 , pp. 29256-29267
    • Bourne, Y.1    Radic, Z.2    Sulzenbacher, G.3    Kim, E.4    Taylor, P.5    Marchot, P.6
  • 13
    • 0035814793 scopus 로고    scopus 로고
    • Interaction of Drosophila acetylcholinesterases with D-tubocurarine: An explanation of the activation by an inhibitor
    • Golicnik M, Fournier D Stojan J (2001) Interaction of Drosophila acetylcholinesterases with D-tubocurarine: an explanation of the activation by an inhibitor. Biochemistry 40, 1214 1219.
    • (2001) Biochemistry , vol.40 , pp. 1214-1219
    • Golicnik, M.1    Fournier, D.2    Stojan, J.3
  • 14
    • 0032998177 scopus 로고    scopus 로고
    • Inhibition of Drosophila acetylcholinesterase by 7- (methylethoxyphosphinyloxy)1-methyl-quinolinium iodide
    • Stojan J, Marcel V Fournier D (1999) Inhibition of Drosophila acetylcholinesterase by 7-(methylethoxyphosphinyloxy)1-methyl-quinolinium iodide. Chem Biol Interact 119-120, 147 157.
    • (1999) Chem Biol Interact , vol.119-120 , pp. 147-157
    • Stojan, J.1    Marcel, V.2    Fournier, D.3
  • 15
    • 0033002408 scopus 로고    scopus 로고
    • Effect of tetramethylammonium, choline and edrophonium on insect acetylcholinesterase: Test of a kinetic model
    • Stojan J, Marcel V Fournier D (1999) Effect of tetramethylammonium, choline and edrophonium on insect acetylcholinesterase: test of a kinetic model. Chem Biol Interact 119-120, 137 146.
    • (1999) Chem Biol Interact , vol.119-120 , pp. 137-146
    • Stojan, J.1    Marcel, V.2    Fournier, D.3
  • 17
    • 0034697035 scopus 로고    scopus 로고
    • Exploration of the Drosophila acetylcholinesterase substrate activation site using a reversible inhibitor (Triton X-100) and mutated enzymes
    • Marcel V, Estrada-Mondaca S, Magne F, Stojan J, Klaebe A Fournier D (2000) Exploration of the Drosophila acetylcholinesterase substrate activation site using a reversible inhibitor (Triton X-100) and mutated enzymes. J Biol Chem 275, 11603 11609.
    • (2000) J Biol Chem , vol.275 , pp. 11603-11609
    • Marcel, V.1    Estrada-Mondaca, S.2    Magne, F.3    Stojan, J.4    Klaebe, A.5    Fournier, D.6
  • 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 (2004) Rational polynomial equation as an unbiased approach for the kinetic studies of Drosophila melanogaster acetylcholinesterase reaction mechanism. Biochim Biophys Acta 1703, 53 61.
    • (2004) Biochim Biophys Acta , vol.1703 , pp. 53-61
    • Stojan, J.1    Golicnik, M.2    Fournier, D.3
  • 19
    • 0032518976 scopus 로고    scopus 로고
    • Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration
    • Marcel V, Palacios LG, Pertuy C, Masson P Fournier D (1998) Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration. Biochem J 329, 329 334.
    • (1998) Biochem J , vol.329 , pp. 329-334
    • Marcel, V.1    Palacios, L.G.2    Pertuy, C.3    Masson, P.4    Fournier, D.5
  • 21
    • 0027217179 scopus 로고
    • Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket
    • Ordentlich A, Barak D, Kronman C, Flashner Y, Leitner M, Segall Y, Ariel N, Cohen S, Velan B Shafferman A (1993) Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket. J Biol Chem 268, 17083 17095.
    • (1993) J Biol Chem , vol.268 , pp. 17083-17095
    • Ordentlich, A.1    Barak, D.2    Kronman, C.3    Flashner, Y.4    Leitner, M.5    Segall, Y.6    Ariel, N.7    Cohen, S.8    Velan, B.9    Shafferman, A.10
  • 22
    • 0036182499 scopus 로고    scopus 로고
    • Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion
    • Stojan J, Golicnik M, Froment MT, Estour F Masson P (2002) Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion. Eur J Biochem 269, 1154 1161.
    • (2002) Eur J Biochem , vol.269 , pp. 1154-1161
    • Stojan, J.1    Golicnik, M.2    Froment, M.T.3    Estour, F.4    Masson, P.5
  • 23
    • 0028955778 scopus 로고
    • Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase
    • Ordentlich A, Barak D, Kronman C, Ariel N, Segall Y, Velan B Shafferman A (1995) Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase. J Biol Chem 270, 2082 2091.
    • (1995) J Biol Chem , vol.270 , pp. 2082-2091
    • Ordentlich, A.1    Barak, D.2    Kronman, C.3    Ariel, N.4    Segall, Y.5    Velan, B.6    Shafferman, A.7
  • 24
    • 0029133139 scopus 로고
    • Allosteric control of acetylcholinesterase catalysis by fasciculin
    • Radic Z, Quinn DM, Vellom DC, Camp S Taylor P (1995) Allosteric control of acetylcholinesterase catalysis by fasciculin. J Biol Chem 270, 20391 20399.
    • (1995) J Biol Chem , vol.270 , pp. 20391-20399
    • Radic, Z.1    Quinn, D.M.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 25
    • 0029092671 scopus 로고
    • Fasciculin 2 binds to the peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation
    • Eastman J, Wilson EJ, Cervenansky C Rosenberry TL (1995) Fasciculin 2 binds to the peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation. J Biol Chem 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
  • 27
    • 0032030173 scopus 로고    scopus 로고
    • Stabilization of recombinant Drosophila acetylcholinesterase
    • Estrada-Mondaca S Fournier D (1998) Stabilization of recombinant Drosophila acetylcholinesterase. Protein Expr Purif 12, 166 172.
    • (1998) Protein Expr Purif , vol.12 , pp. 166-172
    • Estrada-Mondaca, S.1    Fournier, D.2
  • 28
    • 0034307502 scopus 로고    scopus 로고
    • A method to estimate acetylcholinesterase-active sites and turnover in insects
    • Charpentier A, Menozzi P, Marcel V, Villatte F Fournier D (2000) A method to estimate acetylcholinesterase-active sites and turnover in insects. Anal Biochem 285, 76 81.
    • (2000) Anal Biochem , vol.285 , pp. 76-81
    • Charpentier, A.1    Menozzi, P.2    Marcel, V.3    Villatte, F.4    Fournier, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.