EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.67 | D230A |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
741375 |
| 1.1.1.67 | D69A |
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is equally utilized as NAD(H) |
686764 |
| 1.1.1.67 | D69A |
utilizes NAD(H) and NADP(H) with similar catalytic efficiencies. Uses NADP(H) almost as well as wild-type enzyme uses NAD(H) |
686764 |
| 1.1.1.67 | E133A |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
741375 |
| 1.1.1.67 | E133Q |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
741375 |
| 1.1.1.67 | E292A |
mutation partially disrupts the catalytic cycle. Role for residue Glu292 as a gate in a water chain mechanism of proton translocation. Removal of gatekeeper control in the E292A mutant results in a selective, up to 120fold slowing down of microscopicsteps immediately preceding catalytic oxidation of mannitol, consistent with the notion that formation of the productive enzyme-NAD-mannitol complex is promoted by a corresponding position change of Glu292 |
725508 |
| 1.1.1.67 | E68K |
site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, which is switched to NADP(H), EC 1.1.1.138, NADP(H) is preferred by 10fold over NAD(H) |
686764 |
| 1.1.1.67 | E68K/D69A |
shows about a 10fold preference for NADP(H) over NAD(H), accompanied by a small decrease in catalytic efficiency for NAD(H)-dependent reactions as compared to wild-type enzyme |
686764 |
| 1.1.1.67 | H303A |
mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 300fold below the wild-type value |
654504 |
| 1.1.1.67 | H303A |
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme |
741375 |
