An Iron-Dependent Alcohol Dehydrogenase Is Involved in Ethanol Metabolism of Aromatoleum aromaticum by Yvonne Gemmecker Iris Schall Andreas Seubert Nicole Paczia & Johann Heider

Author:Yvonne Gemmecker, Iris Schall, Andreas Seubert, Nicole Paczia & Johann Heider
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Tags: The NAD+-dependent alcohol dehydrogenase AdhB from Aromatoleum aromaticum EbN1 belongs to family III of Fe-dependent alcohol dehydrogenases. It was recombinantly produced in Escherichia coli and biochemically characterized, showing activity only with ethanol or n-propanol. The enzyme contained substoichiometric amounts of Fe, Zn, and Ni and a yet unidentified nucleotide-like cofactor, as indicated by mass spectrometric data. As suggested by its narrow substrate spectrum and complementation of a related species to growth on ethanol, the most probable physiological function of AdhB is the oxidation of short aliphatic alcohols such as ethanol or n-propanol. The enzyme also exhibits a very high tolerance to ethanol and n-propanol, showing moderately substrate-inhibited Michaelis–Menten kinetics up to concentrations of 20% (v/v). AdhB can also be applied biotechnologically to convert acetate to ethanol in coupled enzyme assays with the tungsten enzyme aldehyde oxidoreductase, showing activity with either another aldehyde or pre-reduced benzyl viologen as electron donors., alcohol dehydrogenase; enzyme kinetics; alcohol tolerance; aliphatic alcohols; growth experiments; coupled enzyme assay


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