ACE

ACE is a two-domain dipeptidylcarboxypeptidase that regulates blood pressure through the renin-angiotensin-aldosterone system and kallikrein-kinin system^[1]. Mechanistically, ACE converts Ang I to Ang II and degrades bradykinin, linking vasoconstrictor generation with vasodilator peptide inactivation^[1][2]. In vivo, the C-domain is the predominant site for Ang I cleavage, whereas both ACE domains can hydrolyze bradykinin^[3][1]. Compared with ACE2, ACE functions as a dipeptidylcarboxypeptidase, while ACE2 is a carboxypeptidase that metabolizes angiotensin peptides and is not inhibited by typical ACE inhibitors^[4][5]. Therefore, ACE and ACE2 define distinct but connected enzymatic axes for cardiovascular, renal, and inflammatory research^[4][6]. For experimental applications, ACE inhibitors, C-domain-selective inhibitors, and structural ACE-lisinopril complexes support studies of substrate processing, domain selectivity, and cardiovascular drug mechanisms^[7][8].- C-domain inhibition helps dissect Ang I-dependent vasoconstriction without blocking all ACE activity^[8]. - ACE2 comparisons separate classical ACE signaling from counter-regulatory Ang-(1-7)/Mas-axis mechanisms^[6]. - ACE inhibitor models remain useful for cardiovascular, renal, bradykinin, and RAAS pathway studies^[2][7].