EC Number   |
Protein Variants |
Reference |
|---|
    1.8.1.12 | A34E/R37W |
glutathione reductase mutant, activity switches to trypanothione reductase, termed GRTR, 700fold more activity with trypanothione disulfide than with glutathione |
394776 |
| 1.8.1.12 | C53A |
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+ |
-, 394800 |
| 1.8.1.12 | C53S |
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+ |
-, 394800 |
| 1.8.1.12 | C58S |
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+ |
-, 394800 |
| 1.8.1.12 | E201D |
by site-directed mutagenesis, 5% reductive activity and 50fold increased oxidative activity both compared to wild-type, enhanced quinone reductase activity |
394792 |
| 1.8.1.12 | E201Q |
by site-directed mutagenesis, 5% reductive activity and 50fold increased oxidative activity both compared to wild-type, enhanced quinone reductase activity |
394792 |
| 1.8.1.12 | E436A |
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme |
724758 |
| 1.8.1.12 | Q439A |
the mutant shows slightly increased catalytic efficiency compared to the wild type enzyme |
724758 |
| 1.8.1.12 | W81A |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
724758 |
