EC Number   |
Protein Variants |
Reference |
|---|
    1.2.1.10 | C131A |
inactive |
724341 |
| 1.2.1.10 | C131S |
inactive |
724341 |
| 1.2.1.10 | D208A |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
724341 |
| 1.2.1.10 | I159A |
site-directed mutagenesis, the barrier into the dehydrogenase active site region has been virtually eliminated such that acetaldehyde is transported from one active site to the other in a downhill process |
-, 727173 |
| 1.2.1.10 | I171A |
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover. The mutation results in a 35% reduction in acetaldehyde channeling efficiency |
724341 |
| 1.2.1.10 | I171F |
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme |
724341 |
| 1.2.1.10 | I195A |
the variant has a 20fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate acetaldehyde. The mutation results in a 35% reduction in acetaldehyde channeling efficiency |
724341 |
| 1.2.1.10 | I195F |
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme |
724341 |
| 1.2.1.10 | I195W |
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme |
724341 |
| 1.2.1.10 | more |
expression of a mutant enzyme (with a glycine to aspartic acid mutation in the NADH binding site of the ADH domain of AdhE) in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted results in a reduced ethanol production to the background level |
-, 738990 |
