Activation Mechanisms of Butyrylcholinesterase by 2,4,6-Trinitrotoluene, 3,3-Dimethylbutyl-N-N-butylcarbamate, and 2-Trimethylsilyl-ethyl-N-N-butylcarbamate

Authors: Chiou, Shyh-Ying¹; Wu, Yon-Gi²; Lin, Gialih³

Source: Applied Biochemistry and Biotechnology, Volume 150, Number 3, September 2008 , pp. 337-344(8)

Buy & download fulltext article:

Price: $42.00 plus tax (Refund Policy)

Abstract:

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.

Keywords: Butyrylcholinesterase; Enzyme kinetics; Activation; TNT; Carbamate

Document Type: Research article

DOI: http://dx.doi.org/10.1007/s12010-008-8295-z

Affiliations: 1: Division of Neurosurgery, Chung-Shan Medical University and Hospital, Taichung, 402, Taiwan, 2: Department of Chemistry, National Chung-Hsing University, Taichung, 402, Taiwan, 3: Department of Chemistry, National Chung-Hsing University, Taichung, 402, Taiwan, Email: gilin@dragon.nchu.edu.tw

Publication date: 2008-09-01