Alcohol Dehydrogenases

In JLBEC we are extensively studying various alcohol dehydrogenases originating from the denitrifying bacterium Aromatoleum aromaticum (EbN1). One of the first and most efficient enzymes in this group is (S)-1-phenylethanol dehydrogenase (PEDH), which is a NAD /NADH dependent short-chain dehydrogenase/aldehyde reductase. PEDH is the second biocatalyst in the Aromatoleum aromaticum (EbN1) ethylbenzene mineralization pathway and it catalyzes the NAD+-dependent stereospecific oxidation of (S)-1-phenylethanol to acetophenone. Moreover, in the case of acetophenone accumulation, it catalyzes the reverse reaction, i.e. the NADH-dependent stereospecific reduction of acetophenone to (S)-1-phenylethanol. PEDH has a very wide substrate spectrum which enables its application in the synthesis of numerous chiral alcohols. What's more, it exhibits unmatched resistance to organic solvents. 

 

 

 

The research of PEDH focuses on its application in the industrial synthesis of chiral, pure alkylaromatic alcohols. 

Recently we have expanded our portfolio of dehydrogenases from A. aromaticum by two new enzymes: (R)- and (S)-specific 1-(4-hydroxyphenyl)-ethanol  dehydrogenases ((R)-HPED and (S)-HPED), which are involved in the metabolism of 4-ethylphenol. Although the mechanism of short-chain dehydrogenases is generally known in JBLEC we managed for the first time to describe it with QM methods which enabled quantitative prediction of reaction equilibrium and kinetics. We have also developed a ready-for-use method of chiral alcohol synthesis that bases on whole-cells or immobilized enzyme. 

List of papers on the topic:

  1. P. Borowiecki, N. Telatycka, M. Tataruch, A. Żądło‐Dobrowolska, T. Reiter, K. Schühle, J. Heider, M. Szaleniec, W. Kroutil, "Biocatalytic Asymmetric Reduction of γ‐Keto Esters to Access Optically Active γ‐Aryl‐γ‐butyrolactones", Adv. Synth. Catal., 10.1002/adsc.201901483

  2. I. Stawoska, A. Dudzik, M. Wasylewski, M. Jemioła‑Rzemińska, A. Skoczowski, K. Strzałka, M. Szaleniec, "DFT-based prediction of reactivity of short-chain alcohol dehydrogenase", J Comput Aided Mol Des, 31(6) (2017) 587-602

  3. A. Dudzik, W. Snoch, P. Borowiecki, J. Opalinska-Piskorz, M. Witko, J. Heider, M. Szaleniec, "Asymmetric reduction of ketones and β-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum", App. Microbiol. Biotechnol., 99 (2015) 5055-5069

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