血管紧张素转换酶的结构功能及相关抑制剂.pdfVIP

生 物 工 程 学 报 Chin J Biotech 2008, February 25; 24(2): 171− 176 Chinese Journal of Biotechnology ISSN 1000-3061 cjb@ © 2008 Institute of Microbiology, CAS CSM, All rights reserved 综 述 赵钰岚, 许传莲 , 310018 : 血管紧张素转化酶(angiotensin converting enzyme, ACE, EC )是一种位于细胞膜上, 依赖锌离子的羧二 肽酶, 催化水解十肽血管紧张素I 羧基末端两个氨基酸, 生成具有血管收缩作用的八肽血管紧张素II 。ACE 在血压调节 系统renin - angiotensin system (RAS 系统) 中具有重要作用, 从ACE 的结构功能、基因多态性及其抑制剂等方面进行了 详细综述。发现体细胞ACE 两个活性中心催化血管紧张素I 和缓激肽的机制不同, 因此以体细胞ACE 单个活性中心为 靶点的研究, 将会为研制开发副作用更少, 安全性更高的ACE 抑制剂提供新的途径。 : 血管紧张素转化酶, 结构功能, 基因多态性, 抑制剂 Structure and Function of Angiotensin Converting Enzyme and Its Inhibitors Yulan Zhao, and Chuanlian Xu College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China Abstract: Angiotensin converting enzyme (ACE, EC ) is a membrane-bound, zinc dependent dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the potent vasopressor ocatapeptide angiotensin II, by removing two C-terminal amino acids. ACE is well known as a key part of the renin angiotenisn system that regulates blood pressure, and its inhibitors have potential for the treatment of hypertension. This paper reviewed the characteristics of ACE in aspects of its structure-function relationship, gene polymorphism and inhibitor development. In particular, the catalytic mechanisms of the two active sites of somatic ACE in the cleavage of angiotensin Ⅰand bradykin are different. Therefore, it would likely provide a new way for exploiting novel ACE inhibi- tors with fewer side-effects by specifically-targeting the individual active sites of somatic ACE. Keywords: agiotensin converting enzyme, structur