Inhibitors | Comment | Organism | Structure |
---|---|---|---|
DRVYIYbetaPF | angiotensin II chimera prepared by combining key elements of ACE2 binding and proteolytic stability, 90% inhibition at 10 microM and complete resistance to cleavage over 5 h | Homo sapiens | |
DRVYIYPF | angiotensin II chimera prepared by combining key elements of ACE2 binding and proteolytic stability, 96% inhibition at 10 microM and 18% cleavage over 5h | Homo sapiens | |
PHVF | angiotensin II analog, shows almost saturating levels of inhibition at the screening concentration of 100 microm | Homo sapiens | |
PYPF | angiotensin II analog, shows almost saturating levels of inhibition at the screening concentration of 100 microm | Homo sapiens | |
PYVF | angiotensin II analog, shows almost saturating levels of inhibition at the screening concentration of 100 microm | Homo sapiens |
Organism | UniProt | Comment | Textmining |
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Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(7-methoxycoumarin-4-yl)-acetyl-Ala-Pro-Lys(2,4-dinitrophenyl) + H2O | - |
Homo sapiens | (7-methoxycoumarin-4-yl)-acetyl-Ala-Pro + N6-(2,4-dinitrophenyl)-L-Lys | - |
? | |
additional information | the requirements for ACE2 binding at the first position of a tetrapeptide substrate, i.e. fourth position from the Ang II C-terminus XHPF, are a preference for non-polar, hydrophobic or cyclic residues, with Val and Pro substitutions showing enhanced binding. No strict preference is observed at position two of the tetrapeptide IXPF. Apolar cyclic residues Phe and Pro are not tolerated at the position. Substitution of position three results in moderate increases in binding for Val, 77% and decreases for Ile. The only other functional group tolerated at this position is naphthalene. Peptides PYPF/PHVF/PYVF show almost equivalent ACE2 binding compared to full-length angiotensin II | Homo sapiens | ? | - |
? |