Abstract
Summary: The wide spectrum amidase from Brevibacterium sp. R312, which can hydrolyse many amides tothe corresponding acids, was shown to transfer the acyl groups of amides, acids and esters to hydroxylamine. The transfer rates ofthese reactions in cytoplasmic fractions were measured and compared. The K m and V max were determined for different substrates in the presence of hydroxylamine. The enzyme was also shown to transfer the acyl group of the amide analogue N–methylacetamide to hydroxylamide and that of acetamide to the hydroxylamine analogue methylhydroxylamine.
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