EC Number   |
Metals/Ions |
Reference  |
|---|
   3.4.22.53 | Sr2+ |
activates |
643987 |
| 3.4.22.53 | Ca2+ |
Ka-value: 0.7 mM |
643988 |
| 3.4.22.53 | Sr2+ |
activates, Ka: 5.1 mM |
643988 |
| 3.4.22.53 | Al3+ |
millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+ |
644005 |
| 3.4.22.53 | Ca2+ |
activates. The results support the hypothesis that Ca2+ induces movement of domains I and II closer together to form the functional active site of calpain |
644017 |
| 3.4.22.53 | Ca2+ |
half-maximal activity is 0.242 mM for wilde-type enzyme, 0.129 mM for the E504S mutant, 0.226 mM for the K226S mutant, 0.261 mM for the K230S mutant, 0.183 mM for the K234 mutant, 0.256 mM for the K230E mutant and 0.159 mM for the K234E mutant |
644019 |
| 3.4.22.53 | Ca2+ |
half-maximal activity of wild-type enzyme at 0.242 mM |
644019 |
| 3.4.22.53 | Ca2+ |
Ca2+-binding must induce conformational changes that reorient the protease domains to form a functional active site |
644020 |
| 3.4.22.53 | Ca2+ |
absolute requirement |
644025 |
| 3.4.22.53 | Ba2+ |
5 mM 85.4% of the activation with 5 mM Ca2+ |
644026 |
