EC Number   |
Protein Variants |
Reference |
|---|
    1.2.1.4 | A200E |
the mutant shows strongly reduced activity (50fold) with NADP+ compared to the wild type enzyme |
724459 |
| 1.2.1.4 | A200E/V210Q |
the mutant shows strongly reduced activity (250fold) with NADP+ and about 3fold increased activity with NAD+ compared to the wild type enzyme |
724459 |
| 1.2.1.4 | D176S |
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme |
-, 762562 |
| 1.2.1.4 | D176S/M262I |
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme |
762562 |
| 1.2.1.4 | D176S/S206K |
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme |
762562 |
| 1.2.1.4 | D176S/S206K/M262I |
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme |
762562 |
| 1.2.1.4 | D176S/S206K/M262I/W271Y/W275V |
site-directed mutagenesis, the mutation results in increased activity with NAD+ compared to NADP+ and the wild-type enzyme |
762562 |
| 1.2.1.4 | F34M/Y399C/S405N |
site-directed mutagenesis, crystal structure analysis |
-, 762562 |
| 1.2.1.4 | M262I |
site-directed mutagenesis, the mutation results in 30% higher activity with NAD+ compared to wild-type enzyme, the surface mutation M262I has influence on the solubility |
762562 |
| 1.2.1.4 | more |
construction of an enzyme mutant with deletion of the catalytic residues |
-, 763375 |
