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Abstract
Acetylcholinesterase catalyzes the hydrolysis of thiolacetic acid. The undissociated acid molecules are the direct reactants. The dissociation constant of the conjugate acid of the basic group of the enzyme calculated from the pH dependence of this reaction is about 3.10 −7. This reaction is very strong evidence that the enzyme catalyzes oxygen exchange between acids and water, a necessary condition for the correctness of the proposed theory of enzymic activity, involving an acylated enzyme as intermediate. Trimethylammonium ion and 1:10-decane bis(trimethylammonium) bromide even in enormous excess only partially inhibit the reaction, whereas ethyl acetate hydrolysis is completely inhibited, thus indicating a spacial and functional separation of the anionic and esteratic enzyme sites. Prostigmine which reacts with both sites completely inhibits thiolacetic acid hydrolysis.
Published Version
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