EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.24.15 | Ca2+ |
Ca2+-dependent interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation. Overexpression of calmodulin in HEK293 cells is sufficient to greatly increase the A23187-stimulated secretion of EP24.15, which can be inhibited by the calmodulin inhibitor calmidazolium |
708478 |
| 3.4.24.15 | Ca2+ |
extracellular Ca2+ concentration has no effect on the total amount of extracellular enzyme. Absence of Ca2+ favors the enzyme shedding from the plasma membrane into the medium. In presence of Ca2+, change of preference to R-R bonds instead of L-R bonds of substrates 2-aminobenzoyl-GGFLRRVQ-(N-(2,4-dinitrophenyl)-ethylenediamine) and 2-aminobenzoyl-GGFLRRDQ-(N-(2,4-dinitrophenyl)-ethylenediamine) |
668548 |
| 3.4.24.15 | Ca2+ |
increases the affinity for the substrate 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-Lys-dinitropheyol |
651326 |
| 3.4.24.15 | Ca2+ |
restores activity after EDTA treatment |
37055 |
| 3.4.24.15 | Cd2+ |
restores activity after EDTA treatment |
37055 |
| 3.4.24.15 | Co2+ |
restores activity after EDTA treatment |
37055, 37059 |
| 3.4.24.15 | KCl |
strong activation |
651130 |
| 3.4.24.15 | Mn2+ |
restores activity after EDTA treatment |
37055 |
| 3.4.24.15 | more |
EP24.15 is a metalloendopeptidase |
683813 |
| 3.4.24.15 | more |
metallopeptidase |
683488 |
