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丁酰胆碱酯酶结构研究新进展
引用本文:魏婉丽,孙曼霁.丁酰胆碱酯酶结构研究新进展[J].生物化学与生物物理进展,2000,27(1):37-40.
作者姓名:魏婉丽  孙曼霁
作者单位:军事医学科学院毒物药物研究所,北京,100850
摘    要:丁酰胆碱酯酶(butyrylcholinesterase, BChE, EC 3.1.1.8),能与有机磷毒剂或杀虫剂结合,并能水解许多酯类、肽类及酰胺类化合物,对这些化合物的中毒具有防治作用.近年来通过计算机模拟技术及定点突变技术对其结构研究取得了重要进展,对人BChE外周阴离子部位的结构有了新的认识, 并通过氨基酸替换使BChE获得了水解有机磷酸酐的新功能.

关 键 词:丁酰胆碱酯酶,蛋白质结构,定点突变
收稿时间:1998/12/21 0:00:00
修稿时间::

Progress in Structure of Human Butyrylcholin-esterase
WEI Wan-Li and SUN Man-Ji.Progress in Structure of Human Butyrylcholin-esterase[J].Progress In Biochemistry and Biophysics,2000,27(1):37-40.
Authors:WEI Wan-Li and SUN Man-Ji
Institution:Beijing Institute of Pharmacology and Toxicology, The Academy of Military Medical Sciences, Beijing 100850, China;Beijing Institute of Pharmacology and Toxicology, The Academy of Military Medical Sciences, Beijing 100850, China
Abstract:Human butyrylcholinesterase (BChE, EC, 3.1.1.8) is capable of binding with organophosphate poisons and pesticides. Besides, it is able to catalyse the hydrolysis of many esters, peptides and amides. It is effective in prophylaxis or therapy of the intoxication of these compounds. Its structure study was made important progress by modeling and site-directed mutagenesis. It shed a light on the structure of peripheral anionic site of human BChE, and made the enzyme exhibiting organophosphorus acid anhydride hydrolase activity by amino acid substitution.
Keywords:butyrylcholinesterase  protein  structure    site  directed mutagenesis
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