Abstract
1. 1. The purification and properties of an enzyme from Nocardia sp. which catalyses the conversion of p-hydroxybenzonitrile to p-hydroxybenzoic acid and ammonia without intermediate formation of the amide is described. 2. 2. The enzyme displayed a broad pH optimum between 7.0 and 9.5 and exhibited Michaelis-Menten kinetics with K m of 1.27mM for p-hydroxybenzonitrile. 3. 3. The 12-unit multimeric enzyme possessed a mol. wt of 560,000 and was sensitive to thiol-specific reagents. 4. 4. Although aliphatic nitriles were not substrates for the enzyme a broad range of substituted aromatic nitriles were attacked with a general preference being shown for those with meta substitution.
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