EC Number |
Protein Variants |
Reference |
---|
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 | H198A |
inactive |
737536 |
1.1.1.71 | H267A |
inactive |
737536 |
1.1.1.71 | H281A |
inactive |
737536 |
1.1.1.71 | S97C/M206D/P210C |
site-directed mutagenesis, mutant ADHA-0278, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme |
-, 760769 |
1.1.1.71 | S97C/M206D |
site-directed mutagenesis, mutant ADHA-0279, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme |
-, 760769 |
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 | S97C/T148S/A155H/P210C/L227V/Y244F |
site-directed mutagenesis, mutant ADHA-0384, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme |
760769 |
1.1.1.71 | S97C/T148S/A155H/P210C/L227V |
site-directed mutagenesis, mutant ADHA-0391, 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 |