Enzymes originating from hostile environments offer exceptional stability under industrial conditions and are therefore highly in demand. Using single-cell genome data, we identified the alcohol dehydrogenase gene, adh/a1a, from the Atlantis II Deep Red Sea brine pool. ADH/A1a is highly active at elevated temperatures and high salt concentrations (optima at 70 °C and 4 M KCl), and withstands organic solvents. The polyextremophilic ADH/A1a exhibits a broad substrate scope including aliphatic and aromatic alcohols and is able to reduce cinnamyl-methyl-ketone and raspberry ketone in the reverse reaction, making it a possible candidate for the production of chiral compounds. Here, we report the affiliation of ADH/A1a to a rare enzyme family of microbial cinnamyl-alcohol dehydrogenases and explain unique structural features for halo- and thermoadaptation.
Bibliographical noteKAUST Repository Item: Exported on 2020-10-01
Acknowledgements: The research reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST). We thank Prof. Michael Groll for the support. We thank Jullian R. Vittenet for the support with the ICP-OES measurement.