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標題: Activation mechanisms of butyrylcholinesterase by 2,4,6-trinitrotoluene, 3,3-dimethylbutyl-N-n-butylcarbamate, and 2-trimethylsilyl-ethyl-N-n-butylcarbamate
作者: Chiou, S.Y.
Wu, Y.G.
Lin, G.
關鍵字: butyrylcholinesterase;enzyme kinetics;activation;TNT;carbamate;acetylcholinesterase;cholinesterases;inhibition;substrate;binding;hydrolysis;residues;state
Project: Applied Biochemistry and Biotechnology
期刊/報告no:: Applied Biochemistry and Biotechnology, Volume 150, Issue 3, Page(s) 337-344.
The goal of this work was to propose a possible mechanism for the butyrylcholinesterase activation by 2,4,6-trinitrotoluene (TNT), 3,3-dimethylbutyl-N-n-butylcarbamate (1), and 2-trimethylsilyl-ethyl-N-n-butylcarbamate (2). Kinetically, TNT, and compounds 1 and 2 were characterized as the nonessential activators of butyrylcholinesterase. TNT, and compounds 1 and 2 were hydrophobic compounds and were proposed to bind to the hydrophobic activator binding site, which was located outside the active site gorge of the enzyme. The conformational change from a normal active site gorge to a more accessible active site gorge of the enzyme was proposed after binding of TNT, and compounds 1 and 2 to the activator binding site of the enzyme. Therefore, TNT, and compounds 1 and 2 may act as the excess of butyrylcholine in the substrate activator for the butyrylcholinesterase catalyzed reactions.
ISSN: 0273-2289
DOI: 10.1007/s12010-008-8295-z
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