Open AccessA polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool
Author(s) -
Akal Anastassja L.,
Karan Ram,
Hohl Adrian,
Alam Intikhab,
Vogler Malvina,
Grötzinger Stefan W.,
Eppinger Jörg,
Rueping Magnus
Publication year - 2019
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12557
Subject(s) - brine , chemistry , alcohol dehydrogenase , ketone , cinnamyl alcohol , enzyme , biochemistry , alcohol , food science , organic chemistry , catalysis , selectivity
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 KC l) 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.