The Amidase Activity of Acetyl- and Butylryl-Cholinesterases

摘要

The report describes the hydrolysis of amides by acetyl- and butyryl-cholinesterases. The structure-activity pattern is quite different from that of the more conventional carboxylic ester substrates. Thus, quaternary amides resist hydrolysis. All of the active compounds contain electron withdrawing groups - although there appears to be no direct relationship between the number of such groups and the rate of the enzymatic reaction. Because of their exceptional storage stability, and their resistance to reaction with oximes, the amides offer considerable potentialities for improvement of existing assay methods for the determination of cholinesterase. One current limitation is their reduced sensitivity when compared to existing ester substrates. Resistance to oxime reaction offers the possibility of developing a field detector method for distinguishing oxime-treatable anticholinesterase agents from those which are not oxime-treatable. (Author)