Abstract
The Brevibacterium R 312 strain has an amidase with a wide substrate spectrum previously named “acetamidase”. The study of its activity showed that this enzyme was able to hydrolyze a large number of amides into their corresponding organic acids. The affinity of this enzyme for the substrates varied according to the length of the carbon chain and the spatial crowding of the molecule. The comparison of the specific rates of hydrolysis showed that propionamide was the amide substrate most quickly hydrolyzed.
We confirmed the inducible feature of this enzyme and noted that only acetamide and N-methylacetamide were inducers of this enzyme among the compounds tested. Thioacetamide and N-methylpropionamide, both as amide analogues, were shown to inhibit the biosynthesis of acetamidase. Similarly, the organic acids, products of the hydrolysis reaction, showed a strong repression action on the biosynthesis of the enzyme.
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Maestracci, M., Thiéry, A., Bui, K. et al. Activity and regulation of an amidase (acylamide amidohydrolase, EC 3.5.1.4) with a wide substrate spectrum from a Brevibacterium sp.. Arch. Microbiol. 138, 315–320 (1984). https://doi.org/10.1007/BF00410897
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DOI: https://doi.org/10.1007/BF00410897