EC Number |
Metals/Ions |
Reference |
---|
3.4.17.23 | Zn2+ |
- |
707036, 709990 |
3.4.17.23 | Cl- |
ACE2 activity is regulated by chloride ions. The presence of chloride increases the hydrolysis of angiotensin I by ACE2, but inhibits cleavage of the vasoconstrictor angiotensin II |
692319 |
3.4.17.23 | Cl- |
binding ligands are Tyr207 and Arg514, possible model for chloride activation, effect is substrate dependent: activation with angiotensin I and (7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl)-OH, inhibition with angiotensin II |
657967 |
3.4.17.23 | Zn2+ |
contains zinc-binding consensus sequence HEXXH, amino acids 374-378, zinc-binding protease |
658963 |
3.4.17.23 | Zn2+ |
dependent |
678102 |
3.4.17.23 | Cl- |
enhances activity by about 10fold |
659172 |
3.4.17.23 | F- |
enhances activity by about 10fold |
659172 |
3.4.17.23 | Zn2+ |
metallopeptidase |
693733 |
3.4.17.23 | more |
metalloprotease |
658455 |
3.4.17.23 | more |
no effect of Br- |
659172 |