Appl Environ Microbiol. 1997 Sep;63(9):3390-3. doi: 10.1128/aem.63.9.3390-3393.1997.
The amidase from Rhodococcus erythropolis MP50 demonstrated, in the presence of hydroxylamine, acyltransferase 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-phenylpropionhydroxamate was converted by a chemical Lossen rearrangement in an aqueous medium into the enantiopure S-1-phenylethylamine.
红球菌 MP50 的酰胺酶在羟胺存在下表现出酰基转移酶活性，并催化酰胺和羟胺形成羟肟酸盐。纯化的酰胺酶对乙酰酰胺、苯乙酰胺和 2-苯丙酰胺等底物的酰基转移酶活性比相应的水解反应速率更高。对于 2-苯丙酰胺底物，水解反应和酰基转移酶活性具有高度的对映选择性。在水性介质中，通过化学 Lossen 重排，将光学活性的 2-苯丙酰基羟肟酸转化为对映纯的 S-1-苯乙胺。
