EC Number   |
Protein Variants |
Reference |
|---|
    2.7.7.2 | C126S |
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity about 2times higher than that of the wild type enzyme. The activity of the mutant in presence of Co2+ is very low |
721625 |
| 2.7.7.2 | C143S |
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity approximately wild type activity. The activity of the mutant in presence of Co2+ is very low |
721625 |
| 2.7.7.2 | D168A |
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme |
737678 |
| 2.7.7.2 | D181A |
site-directed mutagenesis, the mutant shows reduced sensitivity to inhibition by FAD compared to the wild-type enzyme and has a much faster turnover rate than the wild-type enzyme |
737678 |
| 2.7.7.2 | D298A |
mutation at the macromolecular interface between two protomers within the trimer |
762436 |
| 2.7.7.2 | D298E |
mutation at the macromolecular interface between two protomers within the trimer |
762436 |
| 2.7.7.2 | D66A |
site-directed mutagenesis, inactive mutant |
737678 |
| 2.7.7.2 | E203A |
mutation at the macromolecular interface between two protomers within the trimer |
762436 |
| 2.7.7.2 | E268A |
active, involved in riboflavin kinase activity |
691501 |
| 2.7.7.2 | E268A |
the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme |
721983 |
