EC Number   |
Protein Variants |
Reference |
|---|
   1.1.3.10 | D452A/R472A |
the mutant shows drastic effects on the binding constant for D-glucose |
725714 |
| 1.1.3.10 | E539K |
increase in catalytic activity, shift in optimum temperature by 10 degrees |
762594 |
| 1.1.3.10 | E540K |
mutant with increased thermo- and pH-stability compared with wild-type, concomitantly with increased catalytic efficiencies (turnover number/KM-value) for D-xylose and L-sorbose |
654320 |
| 1.1.3.10 | E542K |
inserted into plasmid pCL22 |
686372 |
| 1.1.3.10 | E542K |
mutant, analysis of kinetic parameters |
697917 |
| 1.1.3.10 | E542K |
the mutant is characterized by reduced KM values for both D-glucose and D-galactose and significantly increased stability |
712222 |
| 1.1.3.10 | E542R |
mutant, analysis of kinetic parameters |
697917 |
| 1.1.3.10 | F454A |
the mutant shows about 40fold reduced catalytic efficiency compared to the wild type enzyme |
741252 |
| 1.1.3.10 | F454A/S455A/Y456A |
the mutant shows decreased catalytic efficiency for D-glucose/O2 compared to the wild type enzyme |
711984 |
| 1.1.3.10 | F454A/Y456A |
the mutant shows decreased catalytic efficiency for D-glucose/O2 compared to the wild type enzyme |
711984 |
