Purification and properties of benzyl alcohol dehydrogenase from a denitrifying Thauera sp.

Abstract

Toluene and related aromatic compounds are anaerobically degraded by the denitrifying bacterium Thauera sp. strain K172 via oxidation to benzoyl-CoA. The postulated initial step is methylhydroxylation of toluene to benzyl alcohol, which is either a free or enzyme-bound intermediate. Cells grown with toluene or benzyl alcohol contained benzyl alcohol dehydrogenase, which is possibly the second enzyme in the proposed pathway. The enzyme was purified from benzyl-alcohol-grown cells and characterized. It has many properties in common with benzyl alcohol dehydrogenase from Acinetobacter and Pseudomonas species. The enzyme was active as a homotetramer of 160kDa, with subunits of 40kDa. It was NAD+-specific, had an alkaline pH optimum, and was inhibited by thiol-blocking agents. No evidence for a bound cofactor was obtained. Various benzyl alcohol analogues served as substrates, whereas non-aromatic alcohols were not oxidized. The N-terminal amino acid sequence indicates that the enzyme belongs to the class of long-chain Zn2+-dependent alcohol dehydrogenases, although it appears not to contain a metal ion that can be removed by complexing agents.

DOI: 10.1007/BF00272130

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@article{Biegert1995PurificationAP, title={Purification and properties of benzyl alcohol dehydrogenase from a denitrifying Thauera sp.}, author={Thomas Biegert and Uwe Altenschmidt and Christoph Eckerskorn and Georg Fuchs}, journal={Archives of Microbiology}, year={1995}, volume={163}, pages={418-423} }