EC Number   |
General Stability |
Reference |
|---|
    4.1.1.48 | guanidinium-induced denaturation. Unfolding mechanism closely approaches a two-state model at pH 7.0 and a more complex mechanism at pH 9.0 |
4610 |
| 4.1.1.48 | half-life after trypsinolysis in 0.1 M Tris acetate at pH 7.8 and 25°C: wild-type enzyme (120 min), mutant enzyme P2S (60 min), mutant enzyme F246S (40 min), mutant enzyme G212E (40 min), mutant enzyme P2S/F246S (8 min), mutant enzyme P2S/G212E (15 min) |
724261 |
| 4.1.1.48 | optimal stabilization by 0.8 M sucrose |
4593 |
| 4.1.1.48 | the enzyme is strongly stabilized in phosphate buffer (t1/2: 46 min at 87°C) in comparison to HEPPS buffer (t1/2: 4.4 min at 89°C) |
724261 |
| 4.1.1.48 | the higher stability of the enzyme from Sulfolobus solfataricus compared with the enzyme from E. coli seems to be the result of several improved interactions. Including a large number of salt bridges, stabilization of alpha-helices and strengthening of both polypeptide chain termini and solvent-exposed loops |
4615 |
