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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).
Original language | English |
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Article number | 717 |
Number of pages | 10 |
Journal | Scientific Reports |
Volume | 2 |
DOIs | |
Publication status | Published - 9 Oct 2012 |
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Dive into the research topics of 'Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides'. Together they form a unique fingerprint.Projects
- 1 Finished
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Structural Studies on Human Angiotensin-1 Converting Enzyme (ACE) and the Design of Novel Domain-Specific Inhibitors
Acharya, R. (PI)
1/10/11 → 30/09/14
Project: Research council