ACE2

ACE2 is a single-pass, transmembrane protease enzyme that has high homology with angiotensin-converting enzyme (ACE). It is the host cell receptor for several coronaviruses but also plays a role in the renin-angiotensin system where it inactivates angiotensin II by converting it to angiotensin 1-7.

Products
Background

Substrates

Cat. No. Product Name / Activity
1563 Angiotensin I (human, mouse, rat)
Potent endogenous vasoconstrictor peptide; substrate for ACE and ACE2
1158 Angiotensin II
Potent endogenous vasoconstrictor peptide; substrate for ACE2

Other

Cat. No. Product Name / Activity
7199 (±)-Eriodictyol
Predicted by modeling studies to bind ACE2; potent TRPV1 antagonist and antioxidant
7233 SBP1
ACE2 derived peptide; binds SARS-CoV-2 spike protein receptor binding domain
7232 SBP1-FITC
Fluorescent ACE2-derived peptide; binds receptor binding domain of SARS-CoV-2 spike protein
7322 SP 10
Highly potent inhibitor of SARS-CoV Spike (S) protein and ACE2 interaction

ACE2 (E.C. 3.4.17.23), also known as angiotensin-converting enzyme homolog (ACEH) is a single-pass, transmembrane zinc metalloprotease enzyme, found in the lungs, heart, arteries, kidneys, intestines and several brain areas. The protein structure of ACE2 has a single extracellular catalytic domain and a C-terminal transmembrane anchor with a short cytoplasmic tail. ACE2 has a high homology with angiotensin-converting enzyme (ACE) and plays a role in the Renin-Angiotensin System. The primary function of ACE2 is to cleave angiotensin I (Ang I) to give angiotensin 1-9 and angiotensin II (Ang II) to give angiotensin 1-7 (Ang 1-7). Ang 1-7 is a vasodilator peptide that acts at the G-protein coupled receptor, MAS1, counteracting vasoconstriction caused by Ang II. ACE2 can also cleave a number of other peptides including apelin, neurotensin, and ghrelin.

ACE2 is the point of entry for coronaviruses into cells, including SARS-CoV, which causes severe acute respiratory syndrome (SARS) and SARS-CoV-2, which causes COVID-19. The spike S glycoprotein found on the viral cell surface mediates host-cell receptor recognition and membrane fusion by binding to the protease domain of ACE2, enabling viral entry by endocytosis. This entry process is assisted by priming of the S protein by the host cell serine protease, TMPRSS2.

Human ACE2 protein structure

Figure 1: Structure of human ACE2. Structure taken from Protein Data Bank, PDBID: 1R42. Towler et al (2004) ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. J Biol Chem 279: 17996-18007

External sources of pharmacological information for ACE2 :