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Literature summary for 3.4.21.35 extracted from
- Roles of the P1, P2, and P3 residues in determining inhibitory specificity of kallistatin toward human tissue kallikrein (2000), J. Biol. Chem., 275, 38457-38466.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| kallistatin | complex formation, highly specific; kinetics; serine protease inhibitor, i.e. serpin, with unique P1 Phe; wild-type human kallistatin and mutants with amino acid substitutions at each P1, P2, or P3 residue, inhibitory potentials, overview | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| polypeptide + H2O | Homo sapiens | - |
peptides | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-Val-Leu-Arg-p-nitroanilide + H2O | - |
Homo sapiens | D-Val-Leu-Arg + p-nitroaniline | - |
? | |
| polypeptide + H2O | - |
Homo sapiens | peptides | - |
? | |
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