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FEBS Open Bio. 2018 Dec 18;9(2):194-205. doi: 10.1002/2211-5463.12557. eCollection 2019 Feb.

A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool.

Author information

1
KAUST Catalysis Center (KCC) King Abdullah University of Science and Technology (KAUST) Thuwal Saudi Arabia.
2
Center for Integrated Protein Science Munich at the Department of Chemistry Technical University of Munich (TUM) Garching Germany.
3
Computational Bioscience Research Center (CBRC) King Abdullah University of Science and Technology (KAUST) Thuwal Saudi Arabia.
4
Institute of Biochemical Engineering Technical University of Munich (TUM) Garching Germany.
5
Institute of Organic Chemistry RWTH Aachen Aachen Germany.

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.

KEYWORDS:

alcohol dehydrogenase; extremophiles; extremozyme; halophiles; thermophiles

PMID:
30761247
PMCID:
PMC6356862
DOI:
10.1002/2211-5463.12557
[Indexed for MEDLINE]
Free PMC Article

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