N-Acyl Specificity of Taka-N-acetyl-β-D-glucosaminidase Studied by Synthetic Substrate Analogs

II. Preparation of Some p-Nitrophenyl 2-Halogenoacetylamino-2-deoxy-β-D-glucopyranosides and Their Susceptibility to Enzymic Hydrolysis

Abstract

Some of p-nitrophenyl 2-acylamino-2-deoxy-β-D-glucopyranosides with monofluoroacetyl, monochloroacetyl, monobromoacetyl, difluoroacetyl, dichloroacetyl, and trifluoroacetyl group as N-substituent were prepared in order to investigate the N-acyl specificity of Taka-N-acetyl-β-D-glucosaminidase [EC 3. 2. 1. 30].
All of the substrate analogs prepared in this experiment, except the N-dichloroacetyl derivative, were hydrolyzed by this enzyme.
Comparison of the hydrolytic rate ofeach substrate analog to the N-acetyl derivative led to the conclusion that monohalogen substitutionon the N-acetyl group of the substrate, even di-, and tri-substitution in the case of fluorine atom, is permissible in the N-acyl specificity and the specificity is predominantly controlled by the steric factor of the N-substituent of substrate.