Abstract Angiotensin converting enzyme (ACE, EC 3.4.15.1) is a membrane-bound, zinc dependent dipeptidase that catalyzes the conversion of the decapeptide angiotensin I to the potent vasopressor octapeptide angiotensin II by removing the two C-terminal amino acids. ACE is well known to be a key part of the rennin-angiotensin system that regulates blood pressure. The inhibitors of ACE have the potency of treating hypertension. This article reviews the structure-function relationship of ACE as well as its gene polymorphism and inhibitor development. In particular, it has been found that the catalytic mechanisms of the two active sites of somatic ACE in the cleavage of angiotensin I and bradykin are different. Therefore, by specifically targeting the individual active sites of somatic ACE, it will likely offer a new way to develop novel ACE inhibitors with fewer side effects.
Structure and Function of Angiotensin Converting Enzyme and Its Inhibitors