钝齿棒杆菌产精氨酸关键酶分析

Analysis the Key Enzymes Producing Arginine from Corynebacterium crenatum

采用亲和层析和SDS-PAGE方法分析钝齿棒杆菌产精氨酸关键酶。实验表明此菌产精氨酸关键酶之一是乙酰谷氨酸激酶,其分子量为34kD;同时另一分子量为49kD的蛋白质亦对精氨酸有较高的亲和性,揭示钝齿棒杆菌产精氨酸的代谢途径中受精氨酸抑制的酶不是唯一的。实验对限速酶之一——乙酰谷氨酸激酶的酶学性质做了初步研究,结果显示,此酶的最适反应温度为49℃,最适pH为8.0;金属离子Pb2+、Cu2+、Mn2+和Fe2+对乙酰谷氨酸激酶有强烈的抑制作用;DTT对该酶的活力有一定的影响。

The key enzymes producing arginine from Corynebavterium crenatum were investigated by the methods of affinity and SDS-PAGE. The results indicated that one of the key enzymes was acetylglutamate kinase with around 34 kD. estimated by SDS-PAGE, and the other protein with around 49kD. estimated by SDS-PAGE, showed the affinity to arginine. The above mentioned results indicated that the key enzymes, restrained by arginine in arginine metabolize path of Corynebacterium crenatum, were not the only one. The properties of acetylglutamate kinase were also primarily studied. The results indicated that the optimum reaction temperature was 49℃ and optimum pH 8.0. The protease activity of the enzyme was strongly inhibited by Pb2+、Cu2+、Mn2+ and Fe2+, and was affected definitely by DTT.