A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool
Type
ArticleAuthors
Akal, Anastassja L.Karan, Ram
Hohl, Adrian
Alam, Intikhab
Vogler, Malvina M.

Grötzinger, Stefan W.
Eppinger, Jörg

Rueping, Magnus

KAUST Department
Biological & Organometallic Catalysis LaboratoriesBiological and Environmental Sciences and Engineering (BESE) Division
Bioscience Program
Chemical Science Program
Computational Bioscience Research Center (CBRC)
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
KAUST Catalysis Center (KCC)
Office of the VP
Physical Science and Engineering (PSE) Division
Date
2018-12-18Permanent link to this record
http://hdl.handle.net/10754/630173
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Show full item recordAbstract
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.Citation
Akal AL, Karan R, Hohl A, Alam I, Vogler M, et al. (2018) A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool. FEBS Open Bio. Available: http://dx.doi.org/10.1002/2211-5463.12557.Sponsors
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.Publisher
WileyJournal
FEBS Open BioAdditional Links
https://febs.onlinelibrary.wiley.com/doi/abs/10.1002/2211-5463.12557ae974a485f413a2113503eed53cd6c53
10.1002/2211-5463.12557
Scopus Count
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Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program; Physical Science and Engineering (PSE) Division; Chemical Science Program; KAUST Catalysis Center (KCC); Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Science and Engineering (CEMSE) Division
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