Biochemistry and cell biology of angiotensin-converting enzyme and converting enzyme inhibitors.
Biochemistry and cell biology of angiotensin-converting enzyme and converting enzyme inhibitors.
复制标题
血管紧张素转换酶和转换酶抑制剂的生物化学和细胞生物学。
DOI：
10.1007/978-1-4899-0952-7_9
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发表时间：
1995
影响因子：
--
通讯作者：
Zhang,L
中科院分区：
文献类型：
--
作者：
Berecek,KH;Zhang,L
血管紧张素I(AI)是肾素作用于糖蛋白底物血管紧张素原而产生的非活性十肽，通过Skeggs等人在血浆中首次发现和分离的外肽酶将其转化为活性升压八肽血管紧张素II(AII)。他们据此命名为血管紧张素转换酶(ACE)。这种酶后来被发现与激氨酸酶II是同一种酶，并能够水解缓激肽和各种其他多肽。2，3大多数循环中的AI向AII的转化发生在通过肺的过程中。4然而，这种二肽基羧肽酶已被发现以膜结合的胞外酶的形式广泛分布于全身许多组织的血管内皮细胞和上皮细胞的表面。
Angiotensin I (AI), a nonactive decapeptide generated by action of the enzyme, renin, on a glycoprotein substrate, angiotensinogen, is converted to the active pressor octapeptide angiotensin II (AII) by an exopeptidase first identified and isolated in plasma by Skeggs et al.1who accordingly named this angiotensin-converting enzyme (ACE). This enzyme was later found to be the same enzyme as Kininase II, and is able to hydrolyze bradykinin and various other peptides.2,3Most of the conversion of circulating AI to AII occurs during passage through the lungs.4However, this dipeptidyl carboxypeptidase has been found to be widely distributed throughout the body as a membrane bound ectoenzyme on the surface of vascular endothelial cells and epithelial cells of many organs.5–7