EC Number   |
Protein Variants |
Reference |
|---|
  3.5.1.86 | F150L |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type |
755893 |
| 3.5.1.86 | F433A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type |
755893 |
| 3.5.1.86 | F433L |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type |
755893 |
| 3.5.1.86 | G202A |
site-directed mutagenesis. Gly202 appears to control the preference for aromatic substrates as the G202A variant shows three orders of magnitude decrease in kcat/Km for (R)- and (S)-mandelamide |
694955 |
| 3.5.1.86 | G202A/Q207H/Q382E |
site-directed mutagenesis |
694955 |
| 3.5.1.86 | G202S/Q207H/R236C/R369M/Q382E |
site-directed mutagenesis |
694955 |
| 3.5.1.86 | G202V |
site-directed mutagenesis. Reduction in activity increases to six orders of magnitude for the G202V variant |
694955 |
| 3.5.1.86 | I437N |
site-directed mutagenesis |
694955 |
| 3.5.1.86 | K100A |
no enzymic activity |
650254 |
| 3.5.1.86 | K100A |
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant |
755893 |
