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Substrated and inhibitors of the nitrile hydratase and amidase of corynebacterium nitrilophilus



Substrated and inhibitors of the nitrile hydratase and amidase of corynebacterium nitrilophilus



Biotechnology & Applied Biochemistry 11(1): 49-59



Corynebacterium nitrilophilus grown on acetonitrile as a carbon source produces two intracellular enzymes, a nitrile hydratase which hydrates nitriles to amides and an amidase which hydrolyzes amides to carboxylic acids and ammonia. The enzymes were studied in the whole bacterial cells as well as in the cell free extract, and no difference was detected in their enzymatic properties. Both the hydratase and the amidase acted on a wide range of aliphatic and aromatic nitriles and amides but the highest rates of reaction were observed with short chain aliphatic substrates. Aldehydes were powerful reversible inhibitors of the amidase without affecting the activity of nitrile hydratase and, by incorporating a low concentration of acetaldehyde into the reaction mixture, nitriles were converted quantitatively to amides although amidase was present. The nitrile hydratase was strongly and reversibly inhibited by .alpha.-amino and .alpha.-hydroxynitriles and by potassium cyanide. The enzyme was also inhibited by acetate and by mercury, silver, and copper ions. The hydratase exhibited a fairly broad pH optimum between pH 6 and 8. The activity dropped sharply below pH 5.5 and decreased moderately between pH 8 and 11.

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