EC Number   |
Protein Variants |
Reference |
|---|
    1.1.2.3 | A198G |
turnover reduced to 50% |
348070, 348075 |
| 1.1.2.3 | A198G/L230A |
crystallization data |
654766 |
| 1.1.2.3 | A198G/L230A |
double mutant enzyme shows significant activity towards L-mandelate |
348075 |
| 1.1.2.3 | A198G/L230A |
double mutant, turnover reduced to less than 10% |
348070 |
| 1.1.2.3 | A289K |
mutant |
348076 |
| 1.1.2.3 | A67L |
reaction proceeds slower than in wild type, no inhibition by monoclonal antibody inhibiting electron transfer via flavocytochrome b2 |
654520 |
| 1.1.2.3 | A67L |
site-directed mutagenesis, comparison of the mutant kinetics in electron transfer from flavin to heme to the wild-type kinetics |
696302 |
| 1.1.2.3 | A67Q |
reaction proceeds slower than in wild type, no inhibition by monoclonal antibody inhibiting electron transfer via flavocytochrome b2 |
654520 |
| 1.1.2.3 | A67Q |
site-directed mutagenesis, comparison of the mutant kinetics in electron transfer from flavin to heme to the wild-type kinetics |
696302 |
| 1.1.2.3 | analysis |
a L-lactate-selective microbial biosensor is developed using permeabilized cells of gene-engineered thermotolerant methylotrophic yeast Hansenula polymorpha, over-producing FCb2. The HpCYB2 gene, encoding FCb2, under the control of the strong Hansenula polymorpha alcohol oxidase promoter in the frame of a plasmid for multicopy integration is transformed to the recipient strain Hansenula polymorpha C-105 (gcr1 catX) impaired in glucose repression and devoid of catalase activity. The biosensor based on recombinant yeast cells exhibit a higher Km value (Km: 3.02 mM) and hence expanded linear range toward l-lactate as compared to a similar sensor based on the initial cells of Hansenula polymorpha C-105 (Km: 0.33 mM) |
685700 |
