EC Number   |
Protein Variants |
Reference |
|---|
   3.4.22.B37 | BIII-D613N/D614N |
retains 30% of the wild-type Ca2+-binding capacity |
665513 |
| 3.4.22.B37 | BIII-D617N/D618 |
retains 60% of the wild-type Ca2+-binding capacity |
665513 |
| 3.4.22.B37 | BIII-E610A/D611A/P612A, delta613-620 deletion mutant |
unable to bind Ca2+ |
665513 |
| 3.4.22.B37 | BIII-E610Q/D611N/D613N/D614N |
retains 16.2% of the wild-type Ca2+-binding capacity |
665513 |
| 3.4.22.B37 | BIII-E615Q/D616N/D617N/D618N |
retains 36% of the wild-type Ca2+-binding capacity |
665513 |
| 3.4.22.B37 | BIII-P612A, delta613-620 deletion mutant |
retains one-third of the original Ca2+- binding capacity |
665513 |
| 3.4.22.B37 | C314A |
inactive |
708483 |
| 3.4.22.B37 | D613N/D614N |
enhances specific activity to 114% of the wild-type activity |
665513 |
| 3.4.22.B37 | D617N/D618N |
reduces specific activity to 66% of the wild-type activity |
665513 |
| 3.4.22.B37 | Q73G/N74V/A75P/N223A/Q224V |
mutation within the autolytic cleavage sites, autolysis is not arrested by the mutations but its site shifts to new, nearby peptide bonds. In the case of site between Q224 and N225, two new sites emerge: one at F215-T216 and one at G230-R231. In the case of site between N74 and A75, modification gives rise to low intensity, blurred bands which can not be analyzed by sequencing |
649006 |
