EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.17.23 | glycoprotein |
- |
669404, 679300, 763883 |
| 3.4.17.23 | glycoprotein |
7 potential N-glycosylation sites |
659147 |
| 3.4.17.23 | glycoprotein |
five glycans in ACE2 are in close proximity to the receptor-binding domain (RBD). N90, and to a lesser extent N322, of ACE2 establish contacts with RBD. N53 can form a large number of contacts with the RBD residues, whereas the RBD glycan N343 makes very few contacts with ACE2's head protein residues or glycans. Structural basis for the negative effect of glycan of N90 on receptor-binding domain (RBD) binding. Glycan N53 is involved in ACE2 homodimer and ACE2-RBD heterodimer contacts |
762804 |
| 3.4.17.23 | glycoprotein |
SARSCoV-2 receptor-binding domain (RBD) interacts with the N-linked glycan on Asn90 of ACE2. This interaction is mostly absent in the SARS-CoV-1 RBDACE2 complex. After removing N-linked glycans on ACE2, its mechanical binding strength with SARS-CoV-2 RBD decreases to a similar level of the SARS-CoV-1 RBD-ACE2 interaction |
762803 |
| 3.4.17.23 | glycoprotein |
the lager membraneous and smaller soluble enzyme forms are glycosylated |
707055 |
| 3.4.17.23 | proteolytic modification |
ACE2 is is shed from human airway epithelia, constitutive generation of soluble ACE2 is inhibited by ADAM17 inhibitor DPC 333, i.e. (2R)-2-[(3R)-3-amino-3(4-[2-methyl-(4-quinolinyl) methoxy] phenyl)-2-oxopyrrolidinyl]-N-hydroxy-4-methylpentanamide, but not by while ADAM10 inhibitor GI254023, while phorbol ester, ionomycin, endotoxin, and IL-1beta and TNFalpha acutely induce ACE2 release, thus, the regulation of ACE2 cleavage involves a disintegrin and metalloprotease 17, ADAM17, and ADAM10, overview. The ACE2 ectodomain regulates its release and residue L584 might be part of a putative sheddase recognition motif |
707074 |
