Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Cl- | kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity | Bos taurus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cl- | kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity | Bos taurus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.4 | - |
benzyloxycarbonyl-Phe-His-Leu | pH 7.5 | Bos taurus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
testis | - |
Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzyloxycarbonyl-Phe-His-Leu + H2O | - |
Bos taurus | benzyloxycarbonyl-Phe + His-Leu | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
21.5 | - |
benzyloxycarbonyl-Phe-His-Leu | pH 7.5 | Bos taurus |