Inhibitors | Comment | Organism | Structure |
---|---|---|---|
alpha1-Aantichymotrypsin | native chymase-heparin proteoglycan complex is largely resistant to inhibition by alpha1-antichymotrypsin | Rattus norvegicus | |
additional information | endogenous mast cell heparin proteoglycan significantly blocks the inhibition of the enzyme by the serpins alpha1-protease inhibitor and alpha1-antichymotrypsin as well as the inhibition by alpha2-macroglobulin, soybean trypsin inhibitor and plasma. Native chymase-heparin proteoglycan complex is largely resistant to inhibition by alpha1-antichymotrypsin and alpha1-protease inhibitor | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide | in presence of heparin proteoglycan | Rattus norvegicus | |
1.8 | - |
methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide | in absence of heparin | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | the association of the enzyme with heparin proteoglycan may serve both to potentiate the catalytic activity of the enzyme and to increase the life-span of the chymase by preventing their inhibition after exocytosis | Rattus norvegicus | - |
- |
secretory granule | - |
Rattus norvegicus | 30141 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
mast cell | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O | - |
Rattus norvegicus | methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline | - |
? |