Kolodzeĭskaia M V, Verbilenko S V, Konoplich L A
Ukr Biokhim Zh (1978). 1979 Jan-Feb;51(1):56-60.
The paper deals with the role of metals in the catalytic action of Asp. oryzae aminopeptidase. Cobalt ions are more specific activators than Mn2+ and Mn2+ and evoke its maximal activity. Sinergic activation of Co2+ in combination with Mn2+ and Mg2+ was not found in contrast to some aminopeptidases of animal origin. Activation of the enzyme with cobalt chloride depends on temperature. By the 10th minute of incubation the activation reaches its maximum: 650 and 900% at 20 and 40 degrees C, respectively. EDTA (10(-2) M) inactivates completely aminopeptidase for 3h; this process is intensified in the presence of leucine (10(-3) M). Aminopeptidase is also inactivated by chelating agents, such as o-phenantroline and 2,2'-dipyridyl. When the temperature rises from 20 to 40 degrees C the intensification of these reagents effect is insignificant. Cobalt ions reduce and activate to some extent the enzyme after inhibition with EDTA.
本文探讨了金属在米曲霉氨肽酶催化作用中的作用。钴离子比Mn2+更具特异性激活剂,能引发其最大活性。与一些动物源氨肽酶不同,未发现Co2+与Mn2+和Mg2+协同激活的情况。用氯化钴激活该酶取决于温度。孵育到第10分钟时,激活作用达到最大值:在20℃和40℃时分别为650%和900%。10(-2)M的EDTA能在3小时内完全使氨肽酶失活;在亮氨酸(10(-3)M)存在的情况下,这一过程会加剧。氨肽酶也会被螯合剂如邻菲罗啉和2,2'-联吡啶失活。当温度从20℃升至40℃时,这些试剂作用的增强并不显著。在用EDTA抑制后,钴离子能在一定程度上使酶还原并激活。