Angiotensin-converting Enzyme (CD143)

Angiotensin-converting enzyme or ACE2, may also called ACEH (ACE homologue), is an integral membrane protein and a zinc metalloprotease of the ACE family that also includes somatic and germinal ACE. Mouse ACE2 has about 40% amino acid identity to the N-and C-terminal domains of mouse somatic ACE. The predicted mouse ACE 2 protein sequence consists of 798 amino acids, including a N-terminal signal peptide, a single catalytic domain, a C-terminal membrane anchor, and a short cytoplasmic tail. ACE 2 cleaves angiotensins I and II as a carboxypeptidase. ACE2 mRNA is found at high levels in testis, kidney and heart and at moderate levels in colon, small intestine and ovary. Classical ACE inhibitors such as captopril and lisinopril do not inhibit ACE2 activity. Novel peptide inhibitors of ACE2 do not inhibit ACE activity. Genetic data from Drosophila, mice and rats show that ACE2 is an essential regulator of heart function in vivo. In addition, ACE2 is a key SARSCoV Spike protein receptor in vivo and has a critical function in acute lung injury.