Abstract

ω-Amidase (ω-amidodicarboxylate amidohydrolase, EC 3.5.1.3) from Bacillus subtilis 168 and Thermus aquaticus YT-1 were purified to a high degree of purity, as demonstrated by acrylamide gel electrophoresis. Their respective molecular weights, as indicated by Sephadex gel filtration, were approximately 120,000 and 36,000. The temperature optimum for the B. subtilis ω-amidase was 45 °C, and for the T. aquaticus ω-amidase it was 80 °C. These ω-amidases catalyze the hydrolysis of dicarboxylic acid amides and the formation of hydroxamates from the amides (amide transfer) of the corresponding acids (acyl transfer). There is no requirement for any cofactors or metal ions for hydroxamate formation. The specificities of the microbial ω-amidases for dicarboxylic acids showed that these enzymes were similar to the ω-amidase previously reported from mammalian tissues. B. subtilis ω-amidase utilized asparagine, T. aquaticus ω-amidase utilized fumarate, and both utilized succinamate, succinate, succinamide, succinimide, and malate in the transfer reactions. There was no reaction with monocarboxylic acids.

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