EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.1 | A25Y |
mutation in the dimer-dimer interface, leads to a more thermostable enzyme and a change in the rate-determining step at low temperature |
-, 736412 |
| 1.1.1.1 | A93F |
isozyme alphaalpha, altered active site structure and inhibitor binding |
654727 |
| 1.1.1.1 | C243S |
site-directed mutagenesis, the mutant shows increased specific activity, the mutation at Cys243 does not significantly affect ADH kinetic efficiency |
762242 |
| 1.1.1.1 | C257L |
mutation introduced to improve stability under oxidzing conditions. Mutant exhibits prolonged stability and an elevated inactivation temperature |
735548 |
| 1.1.1.1 | C47S |
site-directed mutagenesis, the mutation Ser causes an almost complete loss of the enzyme activity |
762242 |
| 1.1.1.1 | D223G |
highly reduced activity compared to the wild-type enzyme |
655649 |
| 1.1.1.1 | D223G/G225R |
nearly inactive mutant |
655649 |
| 1.1.1.1 | D49N |
highly reduced activity compared to the wild-type enzyme |
655649 |
| 1.1.1.1 | DELTAA200/A201L |
highly reduced activity compared to the wild-type enzyme |
655649 |
| 1.1.1.1 | E68Q |
highly reduced activity compared to the wild-type enzyme |
655649 |
