A Study of the Mechanism of the Reactions Catalyzed by the Amidase Brevibacterium sp. R312 |
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| Authors: | Marc Maestracci Alain Thiery Alain Arnaud Pierre Galzy |
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| Affiliation: | Chaire de Génétique et Microbiologie, Ecole Nationale Supérieure Agronomique, Place Viala, 34060 Montpellier Cedex, France |
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| Abstract: | Besides its amide hydrolase activity, the amidase from Brevibacterium sp. R312 also exhibits an acyl-transferase activity.The mechanism of the transfer reaction of the acyl from acetamide to hydroxylamine was studied. This is a “Bi Bi Ping Pong” type reaction. The kinetic parameters of the reaction were determined: – Apparent Vm = 135 μmol · min –1 · mg–1– Acetamide Km = 18.2 mM– Hydroxylamine Km = 131 mM |
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