Formation of a chiral hydroxamic acid with an amidase from Rhodococcus erythropolis MP50 and subsequent chemical lessen rearrangement to a chiral amine

The amidase from Rhodococcus erythropolis MP50 demonstrated, in the presence of hydroxylamine, acyl-transferase activity and catalyzed the formation of hydroxamates from amides and hydroxylamine. The rates of acyltransferase activity of the purified amidase for the substrates acetamide, phenylacetamide, and 2-phenylpropionamide were higher than the corresponding rates for the hydrolysis reactions. With the substrate 2-phenylpropionamide the hydrolysis reaction and the acyltransferase activity were highly enantioselective. The optically active 2-phenylpropionhydroxmate was converted by a chemical Lossen rearrangement in an aqueous medium into the enantiopure S-1-phenylethylamine.