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dc.contributor.authorAkal, Anastassja L.
dc.contributor.authorKaran, Ram
dc.contributor.authorHohl, Adrian
dc.contributor.authorAlam, Intikhab
dc.contributor.authorVogler, Malvina M.
dc.contributor.authorGrötzinger, Stefan W.
dc.contributor.authorEppinger, Jörg
dc.contributor.authorRueping, Magnus
dc.date.accessioned2018-12-05T08:04:20Z
dc.date.available2018-12-05T08:04:20Z
dc.date.issued2018-12-18
dc.identifier.citationAkal 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.
dc.identifier.issn2211-5463
dc.identifier.doi10.1002/2211-5463.12557
dc.identifier.urihttp://hdl.handle.net/10754/630173
dc.description.abstractEnzymes 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.
dc.description.sponsorshipThe 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.
dc.publisherWiley
dc.relation.urlhttps://febs.onlinelibrary.wiley.com/doi/abs/10.1002/2211-5463.12557
dc.rightsThis is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectExtremophiles
dc.subjecthalophiles
dc.subjectthermophiles
dc.subjectextremozyme
dc.subjectalcohol dehydrogenase
dc.titleA polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool
dc.typeArticle
dc.contributor.departmentBiological & Organometallic Catalysis Laboratories
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentChemical Science Program
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
dc.contributor.departmentKAUST Catalysis Center (KCC)
dc.contributor.departmentOffice of the VP
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.identifier.journalFEBS Open Bio
dc.eprint.versionPost-print
dc.contributor.institutionTechnical University of Munich (TUM); Center for Integrated Protein Science; Munich at the Department of Chemistry; Garching 85748 Germany
dc.contributor.institutionTechnical University of Munich (TUM); Institute of Biochemical Engineering; Garching 85748 Germany
dc.contributor.institutionRWTH Aachen, Institute of Organic Chemistry; Aachen 52074 Germany
kaust.personAkal, Anastassja L.
kaust.personKaran, Ram
kaust.personHohl, Adrian
kaust.personAlam, Intikhab
kaust.personVogler, Malvina M.
kaust.personGrötzinger, Stefan W.
kaust.personEppinger, Jorg
kaust.personRueping, Magnus
refterms.dateFOA2018-12-05T10:43:15Z


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This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Except where otherwise noted, this item's license is described as This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.