Substrate Specificity of Carboxylesterase (E. C. 3. 1. 1. 1) from Several Animals

Abstract

Experiments were made to see the substrate specificity of purified esterase from various origins using p-nitrophenyl acetate, α-naphthyl acetate and trans-4-aminomethyl-cyclohexanecarboxylic acid esters as a substrate. And attension was focused on the influence of structural properties of trans-4-aminomethylcyclohexanecarboxylic acid esters. The hydrolysis rate of α-naphthyl acetate of p-nitrophenyl acetate differed markedly according to animal species. In all the enzymes from rats, guinea pigs, rabbits, and pigs, phenyl ester was hydrolyzed more readily than benzyl ester or alkyl ester. The hydrolysis rate of phenyl esters was affected by the steric as well as electronic effect of the substituents.