EC Number   |
Protein Variants  |
Reference |
|---|
   1.14.20.5 | A120M |
when the purified recombinant mutant enzyme is incubated with naringenin as substrate, the ratio of 2-hydroxynaringenin to apigenin is reduced. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 162% of the catalytic activity relative to wild-type enzyme |
742512 |
| 1.14.20.5 | F146I |
when the purified recombinant mutant enzyme is incubated with naringenin as substrate, the ratio of 2-hydroxynaringenin to apigenin is reduced. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 86% of the catalytic activity relative to wild-type enzyme |
742512 |
| 1.14.20.5 | F146I/A120M |
the enzyme activity of the double mutant is reduced to a level of about 10% of the activity of the wild type enzyme and the only product generated is apigenin |
742512 |
| 1.14.20.5 | L311F |
when the purified recombinant mutant enzyme is incubated with naringenin as substrate, the ratio of 2-hydroxynaringenin to apigenin is reduced. The mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 355% of the catalytic activity relative to wild-type enzyme |
742512 |
| 1.14.20.5 | L311F/A120M |
the double mutant catalyzes the formation of 2-hydroxynaringenin and apigenin, although the ratio of these two compounds iss lower than that generated by the wild type enzyme |
742512 |
| 1.14.20.5 | L311F/F146I |
the double mutant catalyzes the formation of 2-hydroxynaringenin and apigenin, although the ratio of these two compounds iss lower than that generated by the wild type enzyme |
742512 |
| 1.14.20.5 | L311F/F146I/A120M |
the activity of the triple mutant falls to about 5% of the wild type enzyme |
742512 |
| 1.14.20.5 | L311F/F146I/Y240P |
inactive mutant |
742512 |
| 1.14.20.5 | L311F/F146I/Y240P/A120M |
inactive mutant |
742512 |
| 1.14.20.5 | L311F/Y240P |
the double mutant exhibits less flavone synthase activity than either the wild type or the Y240P single mutant enzymes |
742512 |
