Ermer A, Baumann H, Steude G, Peters K, Fittkau S, Dolaschka P, Genov N C
Institute of Biochemistry, Faculty of Medicine, Martin-Luther-University, Halle (Saale), GDR.
J Enzyme Inhib. 1990;4(1):35-42. doi: 10.3109/14756369009030386.
Peptide diazomethyl ketones, well known as specific cysteine protease inhibitors are also potent inhibitors of the microbial serine proteases thermitase (EC 3.4.21.14) and subtilisin Carlsberg (EC 3.4.21.14). The affinity of the enzymes towards the synthetic inhibitors Z-Ala(n)-PheCHN2 (n = 0, 1, 2) depends on the chain length and is in the same range as for the corresponding chloromethyl ketones. Both kinds of inhibitors react irreversibly in a 1:1 ratio with the enzymes and covalently bind to the active site histidine of both subtilisin Carlsberg and thermitase despite the fact that thermitase contains an active-site cysteinyl residue. The mechanism of the inhibition reaction is discussed.
肽重氮甲基酮作为特异性半胱氨酸蛋白酶抑制剂而广为人知，同时也是微生物丝氨酸蛋白酶嗜热菌蛋白酶（EC 3.4.21.14）和枯草杆菌蛋白酶卡尔伯格（EC 3.4.21.14）的有效抑制剂。这些酶对合成抑制剂Z-Ala(n)-PheCHN2（n = 0、1、2）的亲和力取决于链长，并且与相应的氯甲基酮处于相同范围。尽管嗜热菌蛋白酶含有一个活性位点半胱氨酰残基，但这两种抑制剂都以1:1的比例与这些酶发生不可逆反应，并与枯草杆菌蛋白酶卡尔伯格和嗜热菌蛋白酶的活性位点组氨酸共价结合。文中讨论了抑制反应的机制。
