Catalysis by hog‐kidney aminoacylase does not involve a covalent intermediate

Abstract
Hog kidney aminoacylase (N‐acylamino acid amidohydrolase; acylase I) is shown to catalyze the exchange of acetate oxygens with water at a significant rate only when alanine is present simultaneously. These studies, conducted using the 18O‐isotope induced shift on 13C‐NMR spectra, provide evidence in favor of a linear kinetic mechanism as opposed to a ‘ping‐pong’ double‐displacement mechanism. At pH values above neutrality, aminoacylase I also catalyzes the exchange of alanine oxygens with those of water. Ionic strength and pH effects on the kinetics of aminoacylase I are examined and the results are interpreted in terms of a model of the enzyme active site.

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