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- W2042181704 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)." @default.
- W2042181704 created "2016-06-24" @default.
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- W2042181704 date "2012-10-09" @default.
- W2042181704 modified "2023-10-01" @default.
- W2042181704 title "Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides" @default.
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- W2042181704 doi "https://doi.org/10.1038/srep00717" @default.
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