EC Number   |
Protein Variants |
Reference |
|---|
    1.4.3.2 | C254I |
the mutant enzyme shows 5times higher specific activity of oxidase activity than that of the wild type enzyme |
742530 |
| 1.4.3.2 | D165K |
slight increase in kcat/KM value for phenylpyruvate |
-, 739920 |
| 1.4.3.2 | D165K/F263M |
slight increase in kcat/KM value for phenylpyruvate |
-, 739920 |
| 1.4.3.2 | D165K/F263M/L336 |
2fold increase in kcat/KM value for phenylpyruvate |
739920 |
| 1.4.3.2 | D165K/L336M |
slight increase in kcat/KM value for phenylpyruvate |
739920 |
| 1.4.3.2 | D165K/S179L/F263V/L336V |
slight increase in kcat/KM value for phenylpyruvate |
-, 739920 |
| 1.4.3.2 | D238A |
the interaction of Asp238 with the terminal, positively charged group of the substratesis critical for substrate binding but not for catalytic control between the oxidase/monooxygenase activities |
763035 |
| 1.4.3.2 | D238E |
mutant displays increased catalytic activities |
763035 |
| 1.4.3.2 | D238F |
mutant exhibits altered substrate specificity to long hydrophobic substrates |
763035 |
| 1.4.3.2 | F263M |
slight increase in kcat/KM value for phenylpyruvate |
-, 739920 |
