Alcohol Dehydrogenases

Oxidation of primary alcohols

Propanediol oxidoreductase (FucO) from Escherichia coli, oxidizes (S)-1,2-propane diol into the corresponding aldehyde. This enzyme belongs to the iron-dependent class III group of alcohol dehydrogenases. The tertiary structure of the enzyme reveals a substrate binding site adapted for binding of low-molecular weight diols such as its natural substrate. The structure, however, also invites to manipulation through directed evolution to generate enzyme forms which may accommodate also larger substrates such as aromatic diols.

Our studies on FucO aims to...

  • establish structure/function relationships of enzyme-catalyzed oxidation of primary alcohols.
  • isolate new FucO enzyme variants, by directed evolution, with tailored substrate selectivities which act on diol derivatives in a stereoselective manner.

Oxidation of secondary alcohols


The alcohol dehydrogenase from Rhodococcus ruber DSM 44541, ADHA, catalyzes the interconversion between secondary alcohols and their corresponding ketones. ADH-A is a NAD+/NADH and zinc dependent alcohol dehydrogenase with structural similarity to horse liver and yeast alcohol dehydrogenase. The enzyme display high catalytic activity with phenyl-substituted secondary alcohols but relatively poor activity with vicinal diols. This low activity with diols makes this enzyme an interesting starting structure to, by directed evolution, obtain ADH-A variants exhibiting adequate activities with aryl-substituted vicinal diols.

Our studies on ADH-A aims to…

  • establish structure/function relationship of enzyme-catalyzed oxidation of secondary alcohols.
  • isolate new ADH-A variants which can catalyze secondary alcohol derivatives in a stereospecific manner.