EC Number   |
Protein Variants |
Reference |
|---|
   1.21.3.3 | C166A |
mutant, lacking one of the covalent linkages to the cofactor FAD |
698918 |
| 1.21.3.3 | C166A |
site-directed mutagenesis, the mutant protein still has residual activity, but reduced to about 6% of the turnover rate observed for wild-type berberine bridge enzyme, the reductive half-reaction is greatly influenced by the lack of the 6-S-cysteinyl linkage, resulting in a 370fold decrease in the rate of flavin reduction |
687593 |
| 1.21.3.3 | E417Q |
mutant, based on structural information, Glu417 essential amino acid for substrate oxidation, bicovalent flavin linkage is not affected by the mutation |
700353 |
| 1.21.3.3 | E417Q |
solvent isotope effects on kred are equal to 1 for both wild-type and the E417Q mutant, indicating that solvent exchangeable protons are not in flight during or before flavin reduction, thus eliminating a fully concerted mechanism |
727000 |
| 1.21.3.3 | H104A |
mutant, lacking one of the covalent linkages to the cofactor FAD |
698918 |
| 1.21.3.3 | H104T |
no activity |
393870 |
| 1.21.3.3 | H174A |
mutation leads to substantial changes in all kinetic parameters and a decrease in midpoint potential. The crystal structure of the variant shows significant structural rearrangements compared to wild-type enzyme |
726994 |
| 1.21.3.3 | H308S |
5% activity of wild-type |
393870 |
| 1.21.3.3 | H39G |
40% activity of wild-type |
393870 |
| 1.21.3.3 | H459A |
mutant, based on structural information, His459 do not directly interact with the substrate, bicovalent flavin linkage is not affected by the mutation |
700353 |
