Author/Authors :
Panin, N.V Lomonosov Moscow State University - Belozersky Institute of Physicochemical Biology, Russia , Nikulin, M.V Lomonosov Moscow State University - Belozersky Institute of Physicochemical Biology, Russia , Tiurin, E.S Lomonosov Moscow State University - Department of Chemistry,Moscow, Russia , Drobot, V.V Lomonosov Moscow State University - Belozersky Institute of Physicochemical Biology, Russia , Morozova, I.A Lomonosov Moscow State University - Belozersky Institute of Physicochemical Biology, Russia , Švedas, V.K Lomonosov Moscow State University - Belozersky Institute of Physicochemical Biology, Russia
Abstract :
The possibility of using amides of halogen-substituted acetic acids as acyl donors in penicillin acy-lase-catalyzed reactions has been investigated, and the ability of this group of compounds to inactivate enzymes in the course of the catalytic conversion has been established. The strongest inactivating effect was demon-strated by iodoacetamide and bromoacetamide. However, the negative contribution of this side activity can be minimized by decreasing the temperature, when the rate of acyl donor conversion by penicillin acylases is still high enough, but the impact of enzyme inactivation becomes less significant. The catalytic activity of penicillin acylase from Alcaligenes faecalis in the conversion of 2-haloacetamides was significantly (5–8 times) higher than that of penicillin acylase from Escherichia coli.
Keywords :
inactivation during the reaction , 2-haloacetamides , substrate specificity , Penicillin acylases
