EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.71 | D194A |
the mutation results in substantial catalytic deficiency (2.8% compared to the wild type enzyme) |
737536 |
| 1.1.1.71 | E43K/S97C/T148S/A155H/P210C/L227V/Y244F |
site-directed mutagenesis, mutant ADHA-0381, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme |
760769 |
| 1.1.1.71 | E43K/S97C/T148S/T194V/M206D/P210C/L227V |
site-directed mutagenesis, mutant ADHA-0398, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme |
-, 760769 |
| 1.1.1.71 | G198D |
site-directed mutagenesis, the variant of the NAD(P)H-dependent ADH, TeSADH, shows a significant switch of cofactor dependence from NADPH towards NADH compared to the wild-type enzyme |
760921 |
| 1.1.1.71 | H198A |
inactive |
737536 |
| 1.1.1.71 | H267A |
inactive |
737536 |
| 1.1.1.71 | H281A |
inactive |
737536 |
| 1.1.1.71 | H363A |
the mutant with full activity is not able to grow on butanal-containing medium |
737536 |
| 1.1.1.71 | more |
development of improved enzyme variants ADHA-0398 and -0381 shows +26°C improved melting temperature and 17fold higher oxidative activity at pH 6.5 towards (4R,6S)-6-(chloromethyl)oxane-2,4-diol but only 6fold at pH 7.5, method development, overview |
-, 760769 |
| 1.1.1.71 | P704L/H734R |
the ethanol tolerant phenotype of Clostridium thermocellum is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene (adhE). The mutant displays a complete loss of NADH-dependent activity with concomitant acquisition of NADPH-dependent activity. The reduction in specific activity with respect to NADH is far greater (about 25fold less activity) than the increase with respect to NADPH. Although total ADH activity dropps by 25fold, ethanol production does not drop significantly between strains under these conditions |
739526 |
