Open AccessStructure and Function of Angiotensin Converting Enzyme and Its Inhibitors
Author(s) -
Yulan Zhao,
Chuanlian Xu
Publication year - 2008
Publication title -
chinese journal of biotechnology/shengwu gongcheng xuebao
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.153
H-Index - 19
eISSN - 1872-2075
pISSN - 1000-3061
DOI - 10.1016/s1872-2075(08)60007-2
Subject(s) - angiotensin converting enzyme , chemistry , renin–angiotensin system , enzyme , angiotensin ii , biochemistry , amino acid residue , active site , peptidyl dipeptidase a , ace inhibitor , amino acid , potency , membrane , pharmacology , enzyme inhibitor , endocrinology , blood pressure , gene , in vitro , peptide sequence , biology , receptor
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.