Application | Comment | Organism |
---|---|---|
synthesis | enzyme catalyzes the asymmetric reduction of ketones using cheap reductants, such as ethanol, with high stereoselectivity, but the reaction is too slow to obtain good yields. For developing biotransformations of industrial interest using nicotinoprotein alcohol dehydrogenases, the attention should be focused on enzymes with a higher reactivity towards prochiral ketones and secondary alcohols | Rhodococcus erythropolis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus erythropolis | - |
strain DSM 1069 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetophenone + 1-propanol | 4.3% yield, enantiomeric excess of 0.99 for (S)-product chiral secondary alcohol | Rhodococcus erythropolis | ? | 3.8% yield, enantiomeric excess of 0.99 for (S)-product | r | |
acetophenone + cyclohexanol | 2.8-3.7% yield, depending on the ratio of substrates, enantiomeric excess of 0.95-0.99 for (S)-product chiral secondary alcohol | Rhodococcus erythropolis | ? | 3.8% yield, enantiomeric excess of 0.99 for (S)-product | r | |
acetophenone + ethanol | 3.8% yield, enantiomeric excess of 0.99 for (S)-product chiral secondary alcohol | Rhodococcus erythropolis | ? | 3.8% yield, enantiomeric excess of 0.99 for (S)-product | r | |
additional information | catalyzes the asymmetric reduction of ketones using cheap reductants, such as ethanol, with high stereoselectivity, but the reaction is too slow to obtain good yields | Rhodococcus erythropolis | ? | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Rhodococcus erythropolis |