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A Polyextremophilic Alcohol Dehydrogenase From the Atlantis II Deep Red Sea Brine Pool

A Polyextremophilic Alcohol Dehydrogenase From the Atlantis II Deep Red Sea Brine Pool

Anastassja L Akal, Ram Karan, Adrian Hohl, Intikhab Alam, Malvina Vogler, Stefan W Grötzinger, Jörg Eppinger, Magnus Rueping

FEBS Open Bio. 2018 Dec 18;9(2):194-205.

PMID: 30761247

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP69617841	Raspberry alcohol		69617-84-1	Price

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