Amidases are a class of enzymes which convert amides to acids and have potential value in the development of commercial bioprocesses for the production of useful chemicals. A gene encoding an amidase inPseudomonas putida5B has been cloned, sequenced, and overexpressed inEscherichia coli. An additional open reading frame (P38K) encoding a putative protein of 38 kDa was found immediately upstream of the amidase gene. This work continues our characterization of aP. putidaoperon, which now appears to include P38K, amidase, and a stereo-specific nitrile hydratase. This characterization underlies continuing efforts in biocatalyst development.
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