Structure and function of angiotensin converting enzyme and its inhibitors.
- Author:
Yulan ZHAO
1
;
Chuanlian XU
Author Information
1. College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
- Publication Type:Journal Article
- MeSH:
Angiotensin-Converting Enzyme Inhibitors;
pharmacology;
Antihypertensive Agents;
pharmacology;
Humans;
Peptidyl-Dipeptidase A;
chemistry;
genetics;
metabolism;
Polymorphism, Genetic;
Structure-Activity Relationship
- From:
Chinese Journal of Biotechnology
2008;24(2):171-176
- CountryChina
- Language:Chinese
-
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 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 I and bradykin are different. Therefore, it would likely provide a new way for exploiting novel ACE inhibitors with fewer side-effects by specifically-targeting the individual active sites of somatic ACE.
