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Volumn 19, Issue 4, 2005, Pages 234-243

Probing the peripheral anionic site of acetylcholinesterase with quantitative structure activity relationships for inhibition by biphenyl-4-acyoxylate-4′-N-butylcarbamates

Author keywords

Acetylcholinesterase; Carbamate Inhibitors; Peripheral Anionic Site; QSAR

Indexed keywords

4,4' BIPHENYL DERIVATIVE; ACETYLCHOLINESTERASE; BIPHENYL 4 ACYOXYLATE 4' N BUTYLCARBAMATE DERIVATIVE; BIPHENYL DERIVATIVE; CARBAMIC ACID DERIVATIVE; N BUTYLCARBAMATE DERIVATIVE; PHENOL DERIVATIVE; SERINE; UNCLASSIFIED DRUG;

EID: 24944461918     PISSN: 10956670     EISSN: None     Source Type: Journal    
DOI: 10.1002/jbt.20087     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0031880242 scopus 로고    scopus 로고
    • Development of acetylcholinesterase inhibitors in the therapy of Alzheimer's disease
    • Taylor P. Development of acetylcholinesterase inhibitors in the therapy of Alzheimer's disease. Neurology 1998;51(1, Suppl 1):S30-S35, S65-S67.
    • (1998) Neurology , vol.51 , Issue.1 SUPPL. 1
    • Taylor, P.1
  • 3
    • 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
  • 4
    • 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;53:872-879.
    • (1991) Science , vol.53 , 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
  • 6
    • 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 DM, Nair HK, Silman I, Sussman JL. 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
  • 7
    • 0033522370 scopus 로고    scopus 로고
    • "Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase
    • Bartolucci C, Perola E, Cellai L, Brufani M, Lamba D. "Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase. Biochemistry 1999;38:5714-5719.
    • (1999) Biochemistry , vol.38 , pp. 5714-5719
    • Bartolucci, C.1    Perola, E.2    Cellai, L.3    Brufani, M.4    Lamba, D.5
  • 8
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Radić Z, Pickering N, 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.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radić, Z.1    Pickering, N.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 9
    • 0028047375 scopus 로고
    • Conformers of acetylcholinesterase: A mechanism of allosteric control
    • Taylor P, Mayer RH, Himel CM. Conformers of acetylcholinesterase: A mechanism of allosteric control. Mol Pharmacol 1994;45:74-83.
    • (1994) Mol Pharmacol , vol.45 , pp. 74-83
    • Taylor, P.1    Mayer, R.H.2    Himel, C.M.3
  • 10
    • 0029817834 scopus 로고    scopus 로고
    • Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's disease
    • Pang Y-P, Quiram P, Jalacie T, Hong F, Brimijoin S. Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's disease. J Biol Chem 1996;271:23646-23649.
    • (1996) J Biol Chem , vol.271 , pp. 23646-23649
    • Pang, Y.-P.1    Quiram, P.2    Jalacie, T.3    Hong, F.4    Brimijoin, S.5
  • 11
    • 0000134682 scopus 로고    scopus 로고
    • Cholinestease inhibitors do more than inhibit cholinesterase
    • Becker R, Giacobini E, editors. Boston, MA: Birkhauser
    • Giacobini E. Cholinestease inhibitors do more than inhibit cholinesterase. In: Becker R, Giacobini E, editors. Alzheimer's disease: Molecular biology to therapy. Boston, MA: Birkhauser; 1997. pp 188-204.
    • (1997) Alzheimer's Disease: Molecular Biology to Therapy , pp. 188-204
    • Giacobini, E.1
  • 14
    • 0037133519 scopus 로고    scopus 로고
    • Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine
    • Bar-On P, Millard CB, Harel M, Dvir H, Enz A, Sussman JL, Silman I. Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine. Biochemistry 2002;41:3555-3564.
    • (2002) Biochemistry , vol.41 , pp. 3555-3564
    • Bar-On, P.1    Millard, C.B.2    Harel, M.3    Dvir, H.4    Enz, A.5    Sussman, J.L.6    Silman, I.7
  • 15
    • 0033379073 scopus 로고    scopus 로고
    • Molecular recognition by acetylcholinesterase at the peripheral anionic site: Structure-activity relationships for inhibitions by aryl carbamates
    • Lin G, Lai C-Y, Liao W-C. Molecular recognition by acetylcholinesterase at the peripheral anionic site: Structure-activity relationships for inhibitions by aryl carbamates. Bioorg Med Chem 1999;7:2683-2689.
    • (1999) Bioorg Med Chem , vol.7 , pp. 2683-2689
    • Lin, G.1    Lai, C.-Y.2    Liao, W.-C.3
  • 16
    • 0002033953 scopus 로고
    • Neuberger A, Tatun EL, editors. Amsterdam: North-Holland
    • Aldridge WN, Reiner E. In: Neuberger A, Tatun EL, editors. Enzyme inhibitors as substrates. Amsterdam: North-Holland; 1972, pp. 123-145.
    • (1972) Enzyme Inhibitors as Substrates , pp. 123-145
    • Aldridge, W.N.1    Reiner, E.2
  • 17
    • 0015789712 scopus 로고
    • Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate
    • Hart GJ, O'Brien RD. Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate. Biochemistry 1973;12:2940-2945.
    • (1973) Biochemistry , vol.12 , pp. 2940-2945
    • Hart, G.J.1    O'Brien, R.D.2
  • 18
    • 0023151506 scopus 로고
    • p-Nitrophenyl and cholesteryl-N-alkyl carbamates as inhibitors of cholesterol esterase
    • Hosie L, Sutton LD, Quinn DM. p-Nitrophenyl and cholesteryl-N-alkyl carbamates as inhibitors of cholesterol esterase. J Biol Chem 1987;262:260-264.
    • (1987) J Biol Chem , vol.262 , pp. 260-264
    • Hosie, L.1    Sutton, L.D.2    Quinn, D.M.3
  • 19
    • 0010706689 scopus 로고    scopus 로고
    • Structure-reactivity relationships as probes for the inhibition mechanism of cholesterol esterase by aryl carbamates, I: Steady-state kinetics
    • Lin G, Lai C-Y, Liao W-C, Kuo B-H, Lu C-P. Structure-reactivity relationships as probes for the inhibition mechanism of cholesterol esterase by aryl carbamates, I: Steady-state kinetics. J Chin Chem Soc 2000;47:489-500.
    • (2000) J Chin Chem Soc , vol.47 , pp. 489-500
    • Lin, G.1    Lai, C.-Y.2    Liao, W.-C.3    Kuo, B.-H.4    Lu, C.-P.5
  • 20
  • 21
    • 5444268469 scopus 로고    scopus 로고
    • Structure-reactivity relationships as probes for the inhibition mechanism of acetylcholinesterase by aryl carbamates, I: Steady-state kinetics
    • Lin G, Lai C-Y, Liao W-C, Liao B-H, Lu C-P. Structure-reactivity relationships as probes for the inhibition mechanism of acetylcholinesterase by aryl carbamates, I: Steady-state kinetics. J Chin Chem Soc 2003;50:1259-1265.
    • (2003) J Chin Chem Soc , vol.50 , pp. 1259-1265
    • Lin, G.1    Lai, C.-Y.2    Liao, W.-C.3    Liao, B.-H.4    Lu, C.-P.5
  • 22
    • 0033803011 scopus 로고    scopus 로고
    • Quantitative structure-activity relationships for the pre-steady-state inhibition of cholesterol esterase by 4-nitrophenyl-N-substituted carbamates
    • Lin G, Liao W-C, Chiou S-Y. Quantitative structure-activity relationships for the pre-steady-state inhibition of cholesterol esterase by 4-nitrophenyl-N-substituted carbamates. Bioorg Med Chem 2000;8:2601-2607.
    • (2000) Bioorg Med Chem , vol.8 , pp. 2601-2607
    • Lin, G.1    Liao, W.-C.2    Chiou, S.-Y.3
  • 26
    • 0029111479 scopus 로고
    • Hammett analysis of the inhibition of pancreatic cholesterol esterase by substituted phenyl-N-butylcarbamate
    • Lin G, Lai C-Y. Hammett analysis of the inhibition of pancreatic cholesterol esterase by substituted phenyl-N-butylcarbamate. Tetrahedron Lett 1995;36:6117-6120.
    • (1995) Tetrahedron Lett , vol.36 , pp. 6117-6120
    • Lin, G.1    Lai, C.-Y.2
  • 27
    • 0030478552 scopus 로고    scopus 로고
    • Molecular recognition by cholesterol esterase of active site ligands: Structure-reactivity effects for inhibition by aryl carbamates and subsequent carbamyl enzyme turnover
    • Feaster SR, Lee K, Baker N, Hui DY, Quinn DM. Molecular recognition by cholesterol esterase of active site ligands: Structure-reactivity effects for inhibition by aryl carbamates and subsequent carbamyl enzyme turnover. Biochemistry 1996;35:16723-16734.
    • (1996) Biochemistry , vol.35 , pp. 16723-16734
    • Feaster, S.R.1    Lee, K.2    Baker, N.3    Hui, D.Y.4    Quinn, D.M.5
  • 28
    • 0001282182 scopus 로고    scopus 로고
    • Hammett-Taft cross-interaction correlations for the inhibition mechanism of cholesterol esterase by substituted phenyl N-substituted carbamates
    • Lin G. Hammett-Taft cross-interaction correlations for the inhibition mechanism of cholesterol esterase by substituted phenyl N-substituted carbamates. J Phys Org Chem 2000;13:313-321.
    • (2000) J Phys Org Chem , vol.13 , pp. 313-321
    • Lin, G.1
  • 29
    • 0030029491 scopus 로고    scopus 로고
    • Linear free energy relationships of the inhibition of pancreatic cholesterol esterase by 4-nitrophenyl-N-alkylcarbamate
    • LinG, Lai C-Y. Linear free energy relationships of the inhibition of pancreatic cholesterol esterase by 4-nitrophenyl-N-alkylcarbamate. Tetrahedron Lett 1996;2:193-196.
    • (1996) Tetrahedron Lett , vol.2 , pp. 193-196
    • Lin, G.1    Lai, C.-Y.2
  • 30
    • 0017076526 scopus 로고
    • Structure-activity relationships in acetylcholinesterase reactions. Hydrolysis of non-ionic acetic esters
    • Järv J, Kesvatera T, Aavikasar A. Structure-activity relationships in acetylcholinesterase reactions. Hydrolysis of non-ionic acetic esters. Eur J Biochem 1976;67:315-322.
    • (1976) Eur J Biochem , vol.67 , pp. 315-322
    • Järv, J.1    Kesvatera, T.2    Aavikasar, A.3
  • 31
    • 0032774638 scopus 로고    scopus 로고
    • Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates
    • Masson P, Xie W, Foroment M-T, Levitsky V, Fortier P-L, Albaret C, Lockridge O. Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates. Biochim Biophys Acta 1999;1433:281-293.
    • (1999) Biochim Biophys Acta , vol.1433 , pp. 281-293
    • Masson, P.1    Xie, W.2    Foroment, M.-T.3    Levitsky, V.4    Fortier, P.-L.5    Albaret, C.6    Lockridge, O.7
  • 34
    • 0032946092 scopus 로고    scopus 로고
    • Structure-reactivity probes for active site shapes of cholesterol esterase by carbamate inhibitors
    • 35905
    • Lin G, Shieh C-T, Tsai Y-C, Hwang C-I, Lu C-P, Chen G-H. Structure-reactivity probes for active site shapes of cholesterol esterase by carbamate inhibitors. Biochem Biophys Acta 1999;35905:161-174.
    • (1999) Biochem Biophys Acta , pp. 161-174
    • Lin, G.1    Shieh, C.-T.2    Tsai, Y.-C.3    Hwang, C.-I.4    Lu, C.-P.5    Chen, G.-H.6
  • 35
    • 0033520108 scopus 로고    scopus 로고
    • Structure-reactivity relationships for the inhibition mechanism at the second alkyl-chain-binding site of cholesterol esterase and lipase
    • Lin G, Shieh C-T, Ho H-C, Chouhwang J-Y, Lin W-Y, Lu C-P. Structure-reactivity relationships for the inhibition mechanism at the second alkyl-chain-binding site of cholesterol esterase and lipase. Biochemistry 1999;38:9971-9981.
    • (1999) Biochemistry , vol.38 , pp. 9971-9981
    • Lin, G.1    Shieh, C.-T.2    Ho, H.-C.3    Chouhwang, J.-Y.4    Lin, W.-Y.5    Lu, C.-P.6
  • 36
    • 0035761595 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship for the inhibition of Pseudomonas species lipase by 4-nitrophenyl-N-substituted carbamate, I: The steady-state kinetics
    • Lin G, Chouhwang J-Y. Quantitative structure-activity relationship for the inhibition of Pseudomonas species lipase by 4-nitrophenyl-N-substituted carbamate, I: The steady-state kinetics. J Biochem Mol Biol Biophys 2001;5:301-308.
    • (2001) J Biochem Mol Biol Biophys , vol.5 , pp. 301-308
    • Lin, G.1    Chouhwang, J.-Y.2
  • 37
    • 0242662315 scopus 로고    scopus 로고
    • Cage amines as the stopper inhibitors of cholinesterase
    • Lin G, Tsai H-J, Tsai, T-H. Cage amines as the stopper inhibitors of cholinesterase. Bioorg Med Chem Lett 2003; 13:2887-2890.
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 2887-2890
    • Lin, G.1    Tsai, H.-J.2    Tsai, T.-H.3
  • 38
    • 3042655101 scopus 로고    scopus 로고
    • Structure-reactivity relationships as probes for the inhibition mechanism of cholesterol esterase by aryl carbamates, I: Hammett-Taft cross-interaction correlations
    • Lin G. Structure-reactivity relationships as probes for the inhibition mechanism of cholesterol esterase by aryl carbamates, I: Hammett-Taft cross-interaction correlations. J Chin Chem Soc 2004;51:423-429.
    • (2004) J Chin Chem Soc , vol.51 , pp. 423-429
    • Lin, G.1
  • 39
    • 11044233666 scopus 로고    scopus 로고
    • Ortho effects in quantitative structure activity relationships for acetylcholinesterase inhibition by aryl carbamates
    • Lin G, Liu Y-C, Lin Y-F, Wu Y-G. Ortho effects in quantitative structure activity relationships for acetylcholinesterase inhibition by aryl carbamates. J Enzym Inhib Med Chem 2004;19:395-401.
    • (2004) J Enzym Inhib Med Chem , vol.19 , pp. 395-401
    • Lin, G.1    Liu, Y.-C.2    Lin, Y.-F.3    Wu, Y.-G.4
  • 40
    • 12844267417 scopus 로고    scopus 로고
    • Quantitative structure-activity relationships for the pre-steady state acetylcholinesterase inhibition by carbamates
    • Lin G, Liao W-C, Chan C-H, Wu Y-H, Tsai H-J, Hsieh C-W. Quantitative structure-activity relationships for the pre-steady state acetylcholinesterase inhibition by carbamates. J Biochem Mol Toxicol 2004;18:353-360.
    • (2004) J Biochem Mol Toxicol , vol.18 , pp. 353-360
    • Lin, G.1    Liao, W.-C.2    Chan, C.-H.3    Wu, Y.-H.4    Tsai, H.-J.5    Hsieh, C.-W.6
  • 41
    • 16244414645 scopus 로고    scopus 로고
    • A rate determining step change in the pre-steady state of acetylcholinesterase inhibitions by 1,n-alkane-di-N-butyl-carbamates
    • Lin G, Tseng H-C, Chio A-C, Tseng T-M, Tsai B-Y. A rate determining step change in the pre-steady state of acetylcholinesterase inhibitions by 1,n-alkane-di-N-butyl-carbamates. Bioorg Med Chem Lett 2005;15:951-955.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 951-955
    • Lin, G.1    Tseng, H.-C.2    Chio, A.-C.3    Tseng, T.-M.4    Tsai, B.-Y.5
  • 42
    • 0036251240 scopus 로고    scopus 로고
    • Inhibition of acetylcholinesterase by physostigmine analogs: Conformational mobility of cysteine loop due to the steric effect of the alkyl chain
    • Gavuzzo E, Pomponi M. Inhibition of acetylcholinesterase by physostigmine analogs: Conformational mobility of cysteine loop due to the steric effect of the alkyl chain. J Biochem Mol Toxicol 2002;16:64-69.
    • (2002) J Biochem Mol Toxicol , vol.16 , pp. 64-69
    • Gavuzzo, E.1    Pomponi, M.2
  • 43
    • 0037413568 scopus 로고    scopus 로고
    • Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors
    • Savini L, Gaeta A, Fattorusso C, Catalanotti B, Campiani G, Chiasserini L, Pellerano C, Novellino E, McKissic D, Saxena A. Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors. J Med Chem 2003;46:1-4.
    • (2003) J Med Chem , vol.46 , pp. 1-4
    • Savini, L.1    Gaeta, A.2    Fattorusso, C.3    Catalanotti, B.4    Campiani, G.5    Chiasserini, L.6    Pellerano, C.7    Novellino, E.8    McKissic, D.9    Saxena, A.10


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