Panin N V, Nikulin M V, Tiurin E S, Drobot V V, Morozova I A, Švedas V K
Lomonosov Moscow State University, Belozersky Institute of Physicochemical Biology, Lenin Hills 1 , bldg. 40, Moscow, 119991, Russia.
Lomonosov Moscow State University, Department of Chemistry, Lenin Hills 1, bldg. 3, Moscow, 119991 , Russia.
Acta Naturae. 2019 Apr-Jun;11(2):77-81. doi: 10.32607/20758251-2019-11-2-77-81.
The possibility of using amides of halogen-substituted acetic acids as acyl donors in penicillin acylase-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 demonstrated 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 in the conversion of 2-haloacetamides was significantly (5-8 times) higher than that of penicillin acylase from .
研究了在青霉素酰化酶催化反应中使用卤素取代乙酸酰胺作为酰基供体的可能性,并确定了这类化合物在催化转化过程中使酶失活的能力。碘乙酰胺和溴乙酰胺表现出最强的失活作用。然而,当青霉素酰化酶对酰基供体的转化速率仍然足够高,但酶失活的影响变得不那么显著时,通过降低温度可以将这种副反应的负面影响降至最低。[来源]的青霉素酰化酶在2-卤代乙酰胺转化中的催化活性明显(5-8倍)高于[来源]的青霉素酰化酶。