EC Number   |
Protein Variants |
Reference |
|---|
    4.3.1.25 | F102Y |
the turnover rate for L-Tyr is improved 3.6fold, whereas the turnover rate for L-Phe is unaffected. Km values for both L-Tyr and L-Phe are increased by 7.6- and 24fold, respectively, which causes reduced enzyme efficiency for both substrates |
748991 |
| 4.3.1.25 | H123F |
the mutant shows 6.2fold elevation in catalytic efficiency (kcat/Km) for L-Phe, mainly due to a 5.7fold decrease in Km. The mutant enzyme loses activity for L-Tyr. The loss of polarity in the H123F mutant orients both L-Tyr and L-Phe in similar positions, where the ortho-carbon is closer to the methylidene carbon of 4-methylidene-imidazole-5-one |
748991 |
| 4.3.1.25 | H123Y |
the catalytic efficiency of the mutant enzyme for L-Phe is reduced, mainly due to a 10fold decrease in the turnover rate. The H123Y mutant also loses activity against L-Tyr |
748991 |
| 4.3.1.25 | K443E |
the mutant enzyme shows no measurable activity against any of the three substrates, L-Phe, L-Tyr, and L-His |
748991 |
| 4.3.1.25 | R123A |
modest improvements in resistance against protease inactivation |
749285 |
| 4.3.1.25 | R123H |
modest improvements in resistance against protease inactivation |
749285 |
| 4.3.1.25 | R123Q |
modest improvements in resistance against protease inactivation |
749285 |
| 4.3.1.25 | Y110A |
modest improvements in resistance against protease inactivation |
749285 |
| 4.3.1.25 | Y110H |
modest improvements in resistance against protease inactivation |
749285 |
| 4.3.1.25 | Y110L |
modest improvements in resistance against protease inactivation |
749285 |
