EC Number   |
Protein Variants |
Reference |
|---|
    1.4.3.21 | D298A |
Km-value for 2-phenylethylamine is 85% of the wild-type enzyme, kcat for 2-phenylethylamine is 360000fold lower than wild-type enzyme |
672146 |
| 1.4.3.21 | D298K |
in contrast to M602K and wild-type enzyme, the quinone in D298K does not react with any of the hydrazines. D298K shows no activity toward oxidative deamination of 2-phenylethylamine. The quinone formed in D298K is trapped in a conformation that can not react with amines. D298K contains a quinone other than topaquinone |
687276 |
| 1.4.3.21 | D383E |
turnover-number of mutant enzyme is reduced up to 2000fold, depending on pH-value |
654501 |
| 1.4.3.21 | D383N |
catalytically inactive mutant enzyme |
654501 |
| 1.4.3.21 | F190Y |
the mutant loses the activity within the range of pH 6.8-8.5 |
724537 |
| 1.4.3.21 | F384G |
the mutant loses the activity within the range of pH 6.8-8.5 |
724537 |
| 1.4.3.21 | H456A |
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme |
-, 703506 |
| 1.4.3.21 | H458A |
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme |
-, 703506 |
| 1.4.3.21 | H460A |
site-directed mutagenesis, the active site residue mutant shows reduced activity compared to the wild-type enzyme |
-, 703506 |
| 1.4.3.21 | H621A |
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme |
-, 703506 |
