EC Number   |
Protein Variants |
Reference |
|---|
   3.4.22.2 | D158N |
clear kinetic and pH depndence differences from the wild-type enzyme |
95699 |
| 3.4.22.2 | D72A |
the mutant undergoes autoactivation at pH 5.0 compared to pH 4.0 for wild-type enzyme. The general proteolytic activity of the D72A mutant remains similar to that of wild-type |
753357 |
| 3.4.22.2 | K174R |
mutation introduced according to thermostable homologue ervatamin C, unstable |
710471 |
| 3.4.22.2 | K174R/V32S |
mutation introduced according to thermostable homologue ervatamin C, improvement of thermal stability |
710471 |
| 3.4.22.2 | K174R/V32S/G36S |
mutation introduced according to thermostable homologue ervatamin C, improvement of thermal stability |
710471 |
| 3.4.22.2 | V133A/S205E |
change in specificity compared to wild-type enzyme |
95700 |
| 3.4.22.2 | V133A/V157G/S205E |
important decrease in activity, change in specificity compared to the wild-type enzyme |
95700 |
