EC Number |
Protein Variants |
Reference |
---|
1.1.1.85 | A172D |
enhanced thermostability compared to wild-type enzyme |
639158 |
1.1.1.85 | A172D |
melting temperature is reduced by 2.7°C compared to wild-type enzyme |
639160 |
1.1.1.85 | A172E |
enhanced thermostability compared to wild-type enzyme |
639158 |
1.1.1.85 | A172F |
melting temperature is increased by 1.8°C compared to wild-type enzyme |
639160 |
1.1.1.85 | A172F |
mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme |
639160 |
1.1.1.85 | A172G |
melting temperature is reduced by 0.3°C compared to wild-type enzyme, crystal structure is similar to that of the wild-type enzyme |
639160 |
1.1.1.85 | A172I |
melting temperature is increased by 2°C compared to wild-type enzyme |
639160 |
1.1.1.85 | A172L |
melting temperature is increased by 3°C compared to wild-type enzyme |
639160 |
1.1.1.85 | A172L |
mutation causes rearrangement in domain structure, which leads to a higher thermostability compared to wild-type enzyme |
639160 |
1.1.1.85 | A172L |
the mutant shows improved thermal stability compared to the wild type enzyme |
-, 739436 |