EC Number   |
Protein Variants |
Reference |
|---|
  3.7.1.11 | H28A |
site-directed mutagenesis, the mutant enzyme is much less able to catalyze the C-C bond formation as the wild-type enzyme, while the ability for C-C bond cleavage is still intact, the H28A variant shows an 8fold decrease in the formation of (R)-phenylacetylcarbinol (12%), but 1,2-diketone cleavage is nearly unaffected (78% conversion) |
-, 733089 |
| 3.7.1.11 | H28A/N484A |
site-directed mutagenesis, the double mutant catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol, variant H28A/N484A shows acceptable formation of (R)-phenylacetylcarbinol (73%), but conversion toward the cleavage product is decreased by a factor of five (17% conversion), the mutant is also active with 1,2-diketone in contrast to the wild-type enzyme, mutant substrate specificity amd enantioselectivity, overview |
-, 733089 |
| 3.7.1.11 | H76A |
site-directed mutagenesis, inactive mutant |
-, 733089 |
| 3.7.1.11 | H76A/Q116A |
site-directed mutagenesis, inactive mutant |
733089 |
| 3.7.1.11 | more |
substrate specificities and enantioselectivities of wild-type and mutant enzymes, overview |
-, 733089 |
| 3.7.1.11 | Q116A |
site-directed mutagenesis, inactive mutant |
-, 733089 |
