Angiotensin I-converting enzyme (ACE)

Angiotensin I-converting enzyme (ACE) is a membrane-bound zinc metallopeptidase that plays a central role in regulating blood pressure through its critical function within the renin–angiotensin system. It catalyzes the conversion of inactive angiotensin I into active angiotensin II—a potent vasoconstrictor—and degrades bradykinin and other vasoactive peptides. By increasing levels of angiotensin II while reducing vasodilatory substances like bradykinin, ACE indirectly raises blood pressure and influences fluid-electrolyte homeostasis. The enzyme is widely expressed on endothelial cells throughout the body but is especially abundant in pulmonary capillaries. ACE has been extensively validated as a therapeutic target for cardiovascular diseases such as hypertension, heart failure, myocardial infarction recovery, diabetic nephropathy prevention/progression delay, and some forms of chronic kidney disease. Numerous small-molecule inhibitors are approved for clinical use; these drugs have revolutionized management strategies for several major diseases but carry risks including cough and rare but serious angioedema due to altered peptide metabolism. Genetic polymorphisms affecting expression or function can modulate individual susceptibility to cardiovascular conditions as well as drug response profiles.

Other names

Angiotensin-converting enzymeACEDipeptidyl carboxypeptidase IPeptidase PDipeptide hydrolasePeptidyl dipeptidaseKininase IICarboxycathepsinPeptidyldipeptide hydrolaseEndothelial cell peptidyl dipeptidaseCD143

Drugs targeting this molecule act by **competitively inhibiting the enzymatic activity** of ACE. This prevents conversion of angiotensin I to angiotensin II, leading to vasodilation, reduced blood pressure, decreased aldosterone secretion, and increased bradykinin levels.