EC Number   |
Protein Variants |
Reference |
|---|
    3.7.1.9 | A129V |
improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents |
-, 672388 |
| 3.7.1.9 | A129V |
the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate |
-, 749943 |
| 3.7.1.9 | A129V/I199V/V227I |
combination of mutations incompatible for correct folding |
-, 672388 |
| 3.7.1.9 | C254S |
1% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes |
247049 |
| 3.7.1.9 | D224A |
aggregates into inclusion bodies and thus can not be purified |
-, 674958 |
| 3.7.1.9 | D228A |
activity below detection |
247049 |
| 3.7.1.9 | D233A |
residual activity of 62.6% |
-, 674348 |
| 3.7.1.9 | D65V |
activity below detection. Unstable, decreases in cellular extrects after 10 min |
247049 |
| 3.7.1.9 | F104M |
mutation does not have any significant effect on enzyme characteristics |
672388 |
| 3.7.1.9 | F108M |
18% of the activity of wild-type enzyme, enzyme displays greater thermostability than the wild-type enzyme |
247049 |
