EC Number   |
Protein Variants |
Reference |
|---|
    3.2.1.1 | A209V |
more thermostable than wild type enzyme |
393467 |
| 3.2.1.1 | A53S |
in comparison to the wild type, calcium ion has more effect on the catalytic efficiency, kcat/Km, and half-life (at 60°C) of A53S mutant, although the overall activity (kcat/Km) has not improved, about 80% of activity is maintained in the case of A53S mutant |
-, 701772 |
| 3.2.1.1 | D197A |
no activity |
654643 |
| 3.2.1.1 | D197N |
no activity |
654643 |
| 3.2.1.1 | D231N |
the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH |
-, 703339 |
| 3.2.1.1 | D233N |
the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively |
-, 703339 |
| 3.2.1.1 | D300A |
0.0005% of wild-type starch hydrolyzing activity |
654643 |
| 3.2.1.1 | D300N |
0.0005% of wild-type starch hydrolyzing activity |
654643 |
| 3.2.1.1 | D325N |
site-directed mutagenesis, inactive mutant |
-, 664823 |
| 3.2.1.1 | D438G |
the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH |
-, 703339 |
