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Updated: Jan 29, 2026

Preparation of SNS CobaltII Pincer Model Complexes of Liver Alcohol Dehydrogenase
Published on: March 19, 2020
A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool
Anastassja L Akal1,2, Ram Karan1, Adrian Hohl1,2
1KAUST Catalysis Center (KCC) King Abdullah University of Science and Technology (KAUST) Thuwal Saudi Arabia.
Abstract:
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 (ADH) 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.
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