EC Number   |
General Stability |
Reference |
|---|
   3.4.22.54 | 15% autolysis after 1 min exposure to 0.0025 mM Ca2+ |
663588 |
| 3.4.22.54 | autodigestion with 50% loss of total activity after exposure to 0.1 mM Ca2+ |
649028 |
| 3.4.22.54 | calpain-3 undergoes extremely rapid and exhaustive autolysis. Autolyzed fragments spontaneously associate each other to reconstitute the proteolytic activity. These unique properties of CAPN3 are dependent on IS1 and IS2, two CAPN3-characterizing sequences that do not exist in other calpains or any other proteases. Amino acid sequence alignment of representative vertebrate CAPN3s are carried out |
753363 |
| 3.4.22.54 | enzyme is not autolyzed with exhaustive exercise in humans |
663588 |
| 3.4.22.54 | isolation of the intact 94000 Da enzyme is difficult to achieve due to its rapid autolysis. The C-terminally truncated form of the enzyme that comprises the protease core, domains I and II, alone with its insertion sequence, IS1, and N-terminal leader sequence, NS. This 47000 Da p94I-II minicalpain is stable during purification. In the presence of Ca2+, p94I-II cleaves itself within the NS and IS1 sequences. Autolysis is an intramolecular event |
649031 |
| 3.4.22.54 | no autolysis after 1 min exposure to 0.0025 mM Ca2+ |
663588 |
| 3.4.22.54 | rapid autodigestion |
649030 |
| 3.4.22.54 | the enzyme undergoes extremely rapid and exhaustive autodegradation |
752852 |
| 3.4.22.54 | up to 60 min, in presence of 200 nM Ca2+, no spontaneous autolysation |
698991 |
