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

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Abstract
Some of p-nitrophenyl 2-acylamino-2-deoxy-β-D-glucopyranosides with monofluoro-acetyl, 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 of each substrate analog to the N-acetyl derivative led to the conclusion that monohalogen substitution on 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.

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