Angiotensin-converting enzyme

Angiotensin-converting enzyme (ACE) is a zinc-dependent enzyme that converts angiotensin I to angiotensin II and breaks down bradykinin. It helps regulate blood pressure and fluid balance.

Angiotensin I: A relatively inactive peptide produced from angiotensinogen by renin. ACE cleaves this precursor to produce angiotensin II.
ACE inhibitor: A drug that inhibits angiotensin-converting enzyme. These drugs lower angiotensin II production and reduce bradykinin breakdown.
Angiotensinogen: A circulating precursor protein produced chiefly by the liver. Renin acts on angiotensinogen to begin the pathway that supplies ACE’s substrate.
Angiotensin-converting enzyme 2: A carboxypeptidase that converts angiotensin II into angiotensin-(1–7) and processes other peptides. ACE2 often counterbalances ACE by reducing angiotensin II signaling.
Angiotensin II: A peptide hormone that constricts blood vessels and promotes aldosterone release. This is the main product of ACE’s conversion of angiotensin I.
Captopril: An oral ACE inhibitor introduced for treating hypertension and heart failure. It was the first widely used drug designed to inhibit ACE.
Renin: A protease released mainly by kidney juxtaglomerular cells that cleaves angiotensinogen. Renin produces angiotensin I, which ACE then converts.
Neprilysin: A membrane-bound metalloprotease that degrades several peptides, including natriuretic peptides. Unlike ACE, neprilysin inhibition can preserve vasodilatory natriuretic peptides.
Bradykinin: A peptide that promotes blood-vessel dilation, increases vascular permeability, and contributes to pain signaling. ACE degrades bradykinin, limiting its vasodilatory effects.
Hypertension: Persistently elevated arterial blood pressure. ACE inhibitors lower blood pressure partly by reducing angiotensin II formation.

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