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Molecular Genetic and Crystal Structural Analysis of 1-(4-Hydroxyphenyl)-Ethanol Dehydrogenase from 'Aromatoleum aromaticum' EbN1.

Büsing I, Höffken HW, Breuer M, Wöhlbrand L, Hauer B, Rabus R
J Mol Microbiol Biotechnol 25 327-39 (2015)
Cited: 9 times
EuropePMC logo PMID: 26488297

Abstract

The dehydrogenation of 1-(4-hydroxyphenyl)-ethanol to 4-hydroxyacetophenone represents the second reaction step during anaerobic degradation of p-ethylphenol in the denitrifying bacterium 'Aromatoleum aromaticum' EbN1. Previous proteogenomic studies identified two different proteins (ChnA and EbA309) as possible candidates for catalyzing this reaction [Wöhlbrand et al: J Bacteriol 2008;190:5699-5709]. Physiological-molecular characterization of newly generated unmarked in-frame deletion and complementation mutants allowed defining ChnA (renamed here as Hped) as the enzyme responsible for 1-(4-hydroxyphenyl)-ethanol oxidation. Hped [1-(4-hydroxyphenyl)-ethanol dehydrogenase] belongs to the 'classical' family within the short-chain alcohol dehydrogenase/reductase (SDR) superfamily. Hped was overproduced in Escherichia coli, purified and crystallized. The X-ray structures of the apo- and NAD(+)-soaked form were resolved at 1.5 and 1.1 Å, respectively, and revealed Hped as a typical homotetrameric SDR. Modeling of the substrate 4-hydroxyacetophenone (reductive direction of Hped) into the active site revealed the structural determinants of the strict (R)-specificity of Hped (Phe(187)), contrasting the (S)-specificity of previously reported 1-phenylethanol dehydrogenase (Ped; Tyr(93)) from strain EbN1 [Höffken et al: Biochemistry 2006;45:82-93].

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  1. Towards the Response Threshold for p-Hydroxyacetophenone in the Denitrifying Bacterium "Aromatoleum aromaticum" EbN1. Vagts J, Scheve S, Kant M, Wöhlbrand L, Rabus R. Appl Environ Microbiol 84 e01018-18 (2018)
  2. DFT-based prediction of reactivity of short-chain alcohol dehydrogenase. Stawoska I, Dudzik A, Wasylewski M, Jemioła-Rzemińska M, Skoczowski A, Strzałka K, Szaleniec M. J Comput Aided Mol Des 31 587-602 (2017)
  3. Crystal structure and iterative saturation mutagenesis of ChKRED20 for expanded catalytic scope. Zhao FJ, Jin Y, Liu Z, Guo C, Li TB, Li ZY, Wang G, Wu ZL. Appl Microbiol Biotechnol 101 8395-8404 (2017)
  4. Tungsten Enzyme Using Hydrogen as an Electron Donor to Reduce Carboxylic Acids and NAD. Winiarska A, Hege D, Gemmecker Y, Kryściak-Czerwenka J, Seubert A, Heider J, Szaleniec M. ACS Catal 12 8707-8717 (2022)
  5. Biocatalytic characterization of an alcohol dehydrogenase variant deduced from Lactobacillus kefir in asymmetric hydrogen transfer. Rudzka A, Zdun B, Antos N, Montero LM, Reiter T, Kroutil W, Borowiecki P. Commun Chem 6 217 (2023)
  6. Stabilization of Multimeric Proteins via Intersubunit Cyclization. Zhu L, Wang S, Tian W, Zhang Y, Song Y, Zhang J, Mu B, Peng C, Deng Z, Ma H, Qu X. Appl Environ Microbiol 83 e01239-17 (2017)
  7. The NADH recycling enzymes TsaC and TsaD regenerate reducing equivalents for Rieske oxygenase chemistry. Tian J, Boggs DG, Donnan PH, Barroso GT, Garcia AA, Dowling DP, Buss JA, Bridwell-Rabb J. J Biol Chem 299 105222 (2023)


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