EC Number   |
Protein Variants |
Reference |
|---|
    2.7.1.26 | D168A |
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme |
737678 |
| 2.7.1.26 | 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 |
| 2.7.1.26 | D66A |
site-directed mutagenesis, inactive mutant |
737678 |
| 2.7.1.26 | E268A |
inactive |
721983 |
| 2.7.1.26 | E268D |
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme |
721983 |
| 2.7.1.26 | E86Q |
destroying the kinase domain, purified as C-terminal glutathione S-transferase fusionprotein |
705886 |
| 2.7.1.26 | H28A |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
722414 |
| 2.7.1.26 | H28D |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
722414 |
| 2.7.1.26 | H31A |
the mutant shows increased catalytic efficiency compared to the wild type enzyme |
722414 |
| 2.7.1.26 | more |
engineering of the FAD synthetase from Corynebacterium ammoniagenes by deleting its N-terminal adenylation domain leads to a biocatalyst that is stable and efficient for direct and quantitative phosphorylation of riboflavin and riboflavin analogues to their corresponding FMN cofactors at preparative-scale. Deletion of the N-terminal adenosyl transfer domain in the truncated C-terminal RF kinase domain, tcRFK, variants results in a drop in the TM value from 40°C (parental CaFADS) to 35°C for tcRFK. Addition of the C-terminal poly-His tag further reduces the TM to 30°C, presumably due to the conformationally flexible tail formed by the extra amino acids |
739570 |
