Angiotensin-converting enzyme (ACE) (ACE)

Angiotensin-converting enzyme (ACE) is a zinc-dependent dicarboxypeptidase and a central component of the renin-angiotensin-aldosterone system (RAAS), primarily expressed on the surface of vascular endothelial cells [UniProt P12821]. Its primary biological role is the conversion of the inactive decapeptide angiotensin I into the potent vasoconstrictor angiotensin II, while simultaneously inactivating the vasodilator bradykinin [NIH, 2022]. The phrase "related vascular enzymes" typically refers to a broader class of peptidases including ACE2, which counter-regulates ACE by producing the vasodilator angiotensin-(1-7), and neprilysin, which degrades natriuretic peptides [PubMed, 2020]. ACE is a major therapeutic target for cardiovascular and renal diseases; its inhibition leads to reduced systemic vascular resistance and decreased sodium retention, making ACE inhibitors a first-line treatment for hypertension and heart failure [StatPearls, 2023]. Despite their efficacy, these drugs are associated with specific safety concerns, most notably a persistent dry cough and rare but life-threatening angioedema, both linked to the accumulation of bradykinin [PubMed, 2021].

Other names

ACE1Peptidyl-dipeptidase AKininase IICD143Dipeptidyl carboxypeptidase 1

Competitive inhibition of the angiotensin-converting enzyme, which prevents the conversion of angiotensin I to angiotensin II and inhibits the degradation of bradykinin [StatPearls, 2023].