EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.35 | kallistatin | complex formation, highly specific; inhibitor protein mutants with amino acid substitutions of basic residues at a heparin binding site, which is essential for inhibition of kallikrein; positively charged loop on the surface of kallistatin enhances inhibition of tissue kallikrein by acting as a secondary binding site for kallikrein, model, chimeric mutants; serine protease inhibitor, i.e. serpin, with unique P1 Phe | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.35 | polypeptide + H2O | Homo sapiens | - |
peptides | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.35 | Homo sapiens | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.35 | D-Val-Leu-Arg-p-nitroanilide + H2O | - |
Homo sapiens | D-Val-Leu-Arg + p-nitroaniline | - |
? | |
3.4.21.35 | polypeptide + H2O | - |
Homo sapiens | peptides | - |
? |