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Updated: May 17, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory
Geoffrey Masuyer1, Sylva L U Schwager, Edward D Sturrock
1Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath, UK.
Abstract:
Angiotensin-I converting enzyme (ACE), a two-domain dipeptidylcarboxypeptidase, is a key regulator of blood pressure as a result of its critical role in the renin-angiotensin-aldosterone and kallikrein-kinin systems. Hence it is an important drug target in the treatment of cardiovascular diseases. ACE is primarily known for its ability to cleave angiotensin I (Ang I) to the vasoactive octapeptide angiotensin II (Ang II), but is also able to cleave a number of other substrates including the vasodilator bradykinin and N-acetyl-Ser-Asp-Lys-Pro (Ac-SDKP), a physiological modulator of hematopoiesis. For the first time we provide a detailed biochemical and structural basis for the domain selectivity of the natural peptide inhibitors of ACE, bradykinin potentiating peptide b and Ang II. Moreover, Ang II showed selective competitive inhibition of the carboxy-terminal domain of human somatic ACE providing evidence for a regulatory role in the human renin-angiotensin system (RAS).
Related Concept Videos
Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors
Antihypertensive Drugs: Direct Renin Inhibitors
Heart Failure Drugs: Inhibitors of Renin-Angiotensin System
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Antihypertensive Drugs: Angiotensin II Receptor Blockers
Hormonal Regulation
