Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68227
標題: Molecular recognition by acetylcholinesterase at the peripheral anionic site: Structure-activity relationships for inhibitions by aryl carbamates
作者: Lin, G.L.
Lai, C.Y.
Liao, W.C.
關鍵字: acetylcholinesterase inhibition;peripheral site;carbamates;pancreatic cholesterol esterase;hammett analysis;alzheimer-type;substrate;dementia;binding;butyrylcholinesterase;residues;potent;gorge
Project: Bioorganic & Medicinal Chemistry
期刊/報告no:: Bioorganic & Medicinal Chemistry, Volume 7, Issue 12, Page(s) 2683-2689.
摘要: 
Substituted phenyl-N-butyl carbamates (1-9) are potent irreversible inhibitors of Electrophorus electricus acetylcholinesterase. Carbamates 1-9 act as the peripheral anionic site-directed irreversible inhibitors of acetylcholinesterase by the stop-time assay in the presence of a competitive inhibitor, edrophonium. Linear relationships between the logarithms of the dissociation constant of the enzyme-inhibitor adduct (K-i), the inactivation constant of the enzyme-inhibitor adduct (k(2)), and the bimolecular inhibition constant (k(i)) for the inhibition of Electrophorus electricus acetylcholinesterase by carbamates 1-9 and the Hammett substituent constant (sigma), are observed, and the reaction constants (rho s) are -1.36, 0.35 and -1.01, respectively. Therefore, the above reaction may form a positive charged enzyme-inhibitor intermediate at the peripheral anionic site of the enzyme and may follow the irreversible inactivation by a conformational change of the enzyme. (C) 1999 Elsevier Science Ltd. All rights reserved.
URI: http://hdl.handle.net/11455/68227
ISSN: 0968-0896
DOI: 10.1016/s0968-0896(99)00213-8
Appears in Collections:期刊論文

Show full item record
 

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.