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Literature summary extracted from

  • Schenkels, P.; De Vries, S.; Straathof, A.J.J.
    Scope and limitations of the use of nicotinoprotein alcohol dehydrogenase for the coenzyme-free production of enantiopure fine-chemicals (2001), Biocatal. Biotransform., 19, 191-212.
No PubMed abstract available

Application

EC Number Application Comment Organism
1.1.99.36 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

EC Number Organism UniProt Comment Textmining
1.1.99.36 Rhodococcus erythropolis
-
 strain DSM 1069
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.36 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
1.1.99.36 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
1.1.99.36 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
1.1.99.36 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

EC Number Cofactor Comment Organism Structure
1.1.99.36 NADH
-
 Rhodococcus erythropolis