EC Number   |
Protein Variants |
Reference |
|---|
   1.1.1.B3 | I86A |
site-directed mutagensis, the secondary alcohol dehydrogenase I86A mutant is stereospecific for (R)-alcohols instead of (S)-alcohols, in contrast to the wild-type enzyme, the mutation I86A allows large substituents to fit into the large pocket of I86ATeSADH, which corresponds to the small pocket in wild-type TeSADH, modeling of the stereopreference of TeSADH I86A |
723841 |
| 1.1.1.B3 | I86A |
the mutant shows reversed stereoselectivity (R) compared to the wild type enzyme |
762089 |
| 1.1.1.B3 | more |
covalent immobilization of the purified recombinant enzyme on different supports, i.e. on glyoxyl agarose, amino epoxy agarose, CNBr-activated sepharose, monoaminoethyl-N-ethylagarose-glutaraldehyde, monoaminoethyl-N-ethyl agarose, or polyethyleneimine agarose, immobilized enzyme activities, overview |
-, 701031 |
| 1.1.1.B3 | N179S |
about 40fold increase in specific activity |
740303 |
| 1.1.1.B3 | N179S/I214F/S215G |
about 50fold increase in specific activity |
740303 |
| 1.1.1.B3 | S174G |
about 7fold increase in specific activity |
740303 |
| 1.1.1.B3 | W110A |
the mutant shows imperfect wild type stereoselectivity (S) |
762089 |
| 1.1.1.B3 | W110A/I86A |
the mutant enzyme is completely non-stereoselective for the reduction of 2-hexanone.Additionally, an extremely low level of stereoselectivity (i.e. from 10% to 24%) is observed for the reduction of aryl-aliphatic ketones and aliphatic ketones |
762089 |
| 1.1.1.B3 | W288A |
(R)-selective mutant |
-, 760421 |
| 1.1.1.B3 | W288I |
(R)-selective mutant |
-, 760421 |
