Title : The Pharmacogenetic Footprint of ACE Inhibition: A Population-Based Metabolomics Study.

Pub. Date : 2016

PMID : 27120469






4 Functional Relationships(s)
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1 Although it is known that ACE especially cleaves COOH-terminal dipeptides from active polypeptides, the whole range of substrates and products is still unknown. Dipeptides angiotensin I converting enzyme Homo sapiens
2 Two of these resulting dipeptides, namely aspartylphenylalanine and phenylalanylserine, showed significant associations with blood pressure which qualifies them-and perhaps also the other dipeptides-as readouts of ACE-activity. Dipeptides angiotensin I converting enzyme Homo sapiens
3 Since so far ACE activity measurement is substrate specific due to the usage of only one oligopeptide, taking several dipeptides as potential products of ACE into account may provide a broader picture of the ACE activity. Dipeptides angiotensin I converting enzyme Homo sapiens
4 Since so far ACE activity measurement is substrate specific due to the usage of only one oligopeptide, taking several dipeptides as potential products of ACE into account may provide a broader picture of the ACE activity. Dipeptides angiotensin I converting enzyme Homo sapiens