EC Number   |
Protein Variants |
Reference |
|---|
   3.1.1.73 | A126C/N152C |
introduction of a disulfide bridge, increase of temperature optimum by 6°C and increase in thermal inactivation half-live |
739416 |
| 3.1.1.73 | A140T |
random mutagenesis, the mutant shows 2.4fold increased thermostability compared to the mutant D93G/S187F |
729418 |
| 3.1.1.73 | C202A |
site-directed mutagenesis, almost inactive mutant |
730917 |
| 3.1.1.73 | C202A/C458A |
site-directed mutagenesis, almost inactive mutant |
730917 |
| 3.1.1.73 | C235S |
random mutagenesis, the mutant shows 3.2fold increased thermostability compared to the mutant D93G/S187F |
-, 729418 |
| 3.1.1.73 | C458A |
site-directed mutagenesis, almost inactive mutant |
730917 |
| 3.1.1.73 | D174A |
site-directed mutagenesis, the mutant does not show changes in thermal stability compared to the wild-type enzyme |
-, 714497 |
| 3.1.1.73 | D190A |
about 10% residual activity with methyl ferulate |
737656 |
| 3.1.1.73 | D214A |
mutation within catalytic triad, complete loss of activity |
-, 744117 |
| 3.1.1.73 | D77I |
higher catalytic efficiency towards alpha-naphtylbutyrate and alpha-naphtylcaprylate, some activity towards long-acyl chain esters, no activity towards phenolic acid methyl esters and feruloylated arabinoxylan, increased pH-optimum |
667790 |
