蛋白酵素
蛋白质水解
半胱氨酸
半胱氨酸蛋白酶
脱氮酶
生物化学
蛋白酶
化学
酶
蛋白质前体
泛素
基因
作者
Małgorzata Rzychon,Dorota Chmiel,Justyna Steć-Niemczyk
出处
期刊:PubMed
日期:2004-01-01
卷期号:51 (4): 861-73
被引量:25
摘要
Cysteine proteases are involved in many physiological processes and their hyperactivity may lead to severe diseases. Nature has developed various strategies to protect cells and whole organisms against undesired proteolysis. One of them is the control of proteolytic activity by inhibition. This paper presents the mechanisms underlying the action of proteinaceous inhibitors of cysteine proteinases and covers propeptides binding backwards relative to the substrate or distorting the protease catalytic centre similarly to serpins, the p35 protein binding covalently to the enzyme, and cystatins that are exosite binding inhibitors. The paper also discusses tyropins and chagasins that, although unrelated to cystatins, inhibit cysteine proteinases by a similar mechanism, as well as inhibitors of the apoptosis protein family that bind in a direction opposite to that of the substrate, similarly to profragments. Special attention is given to staphostatins, a novel family of inhibitors acting in an unusual manner.
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