化学
立体化学
乙酰胆碱酯酶
阳离子聚合
去甲亮氨酸
活动站点
酶
氨基酸
生物化学
有机化学
蛋氨酸
作者
Carlos Červeñanský,Rosario Durán,Evert Karlsson
出处
期刊:Toxicon
[Elsevier]
日期:1996-06-01
卷期号:34 (6): 718-721
被引量:4
标识
DOI:10.1016/0041-0101(95)00155-7
摘要
Norleucine methylester was coupled to carboxylates of fasciculin 2, a snake toxin that inhibits acetylcholinesterase (AChE). This neutralized negative charges but had no effect on the activity, suggesting that carboxyls do not participate in binding to AChE. Earlier results are discussed. Modification of three aromatic amino acids in the peripheral site of AChE, the binding site for fasciculin, decreased the affinity 100 to one million times. Neutralizing the charge of cationic groups of fasciculin lowered the affinity only three to seven times. A change in either the toxin or enzyme part of a binding site should have about the same effect. Since this was not so, it suggests that cationic groups of fasciculin do not bind to aromatic rings in the peripheral site.
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