EC Number   |
Protein Variants |
Reference |
|---|
    3.1.3.8 | A35E/P42S/Q168R/T248R |
thermostable mutant. Molecular dynamics simulation and comparison with wild-type show that among secondary structure elements, loops have the most impact on the thermal stability of Aspergillus niger phytase. In addition, the location rather than the number of hydrogen bonds has an important contribution to thermostability. Salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly |
730886 |
| 3.1.3.8 | A58E/P65S |
increased activity at pH 5.5 |
677690 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R |
increased activity and improved thermostability retaining 20% greater activity after being heated at 80°C for 10 min and has a 7°C higher melting temperature than that of wild type PhyA |
677690 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R |
retains 20% greater activity after being heated at 80°C for 10 min and has 7°C higher melting temperature than that of the wild type enzyme |
677774 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R/E228K |
pH-activity profile-improved mutant, optimum shift to pH 4.0, 64% increased specific activity at pH 3.5 |
677774 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R/E228K/K300E |
pH-activity profile-improved mutant, eliminates the activity dip at pH 3.5 shown in the wild type |
677774 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R/E228K/S149P |
improved thermostability |
677774 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R/E228K/S149P/F131L |
improved thermostability |
677774 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R |
Although the substitution of K112R is supposed to create a new hydrogen bond with Y113 at a distance of 2.56 A, it does not offer extra benefit to thermostability |
677774 |
| 3.1.3.8 | A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R |
27% increased specific activity at pH 5.5, 100% increased specific activity at pH 3.5 |
677774 |
