EC Number   |
General Stability |
Reference |
|---|
   3.4.24.27 | After precipitation with trichloroacetic acid the purified enzyme irreversibly loses activity and solubility at neutral pH |
31136 |
| 3.4.24.27 | Ca2+ increases thermal stability |
31145 |
| 3.4.24.27 | Ca2+ stablizes the enzyme |
734109 |
| 3.4.24.27 | Calcium is necessary to stabilize the structure of thermolysin |
31145 |
| 3.4.24.27 | enzyme is stable in presence of CaCl2 |
695306 |
| 3.4.24.27 | important role of Asn116 in the activity and stability of thermolysin presumably by stabilizing the beta-hairpin structure. In the N-terminal domain of thermolysin, two antiparallel beta-strands, Asn112-Ala113-Phe114-Trp115 and Ser118-Gln119-Met120-Val121-Tyr122 are connected by an Asn116-Gly117 turn to form a beta-hairpin structure |
734109 |
