Premium
Substrate activation of butyrylcholinesterase and substrate inhibition of acetylcholinesterase by 3,3‐dimethylbutyl‐ N ‐ n ‐butylcarbamate and 2‐trimethylsilyl‐ethyl‐ N ‐ n ‐butylcarbamate
Author(s) -
Chiou ShyhYing,
Wu YonGi,
Lin YanFu,
Lin LongYau,
Lin Gialih
Publication year - 2007
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.20158
Subject(s) - butyrylcholinesterase , acetylcholinesterase , chemistry , substrate (aquarium) , trimethylsilyl , cholinesterase , stereochemistry , enzyme , organic chemistry , aché , pharmacology , medicine , oceanography , geology
Carbamates are used to treat Alzheimer's disease. These compounds inhibit acetylcholinesterase and butyrylcholinesterase. The goal of this work is to use the substrate analogs of butyrylcholinesterase, 3,3‐dimethylbutyl‐ N ‐ n ‐butylcarbamate (1) and 2‐trimethylsilyl‐ethyl‐ N ‐ n ‐butylcarbamate (2) to probe the substrate activation mechanism of butyrylcholinesterase. Compounds 1 and 2 are characterized as the pseudo substrate inhibitors of acetylcholinesterase; however, compounds 1 and 2 are characterized as the essential activators of butyrylcholinesterase. Therefore, compounds 1 and 2 mimic the substrate in the acetylcholinesterase‐catalyzed reactions, but the behavior of compounds 1 and 2 mimics the substrate activation in the butyrylcholinesterase‐catalyzed reactions. © 2007 Wiley Periodicals, Inc. J Biochem Mol Toxicol 21:24–31, 2007; Published online in Wiley InterScience ( www.interscience.wiley.com ). DOI 10.1002/jbt.20158