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dc.contributor.authorGrötzinger, Stefan W.
dc.contributor.authorKaran, Ram
dc.contributor.authorStrillinger, Eva
dc.contributor.authorBader, Stefan
dc.contributor.authorFrank, Annika
dc.contributor.authorAl Rowaihi, Israa
dc.contributor.authorGespers (Akal), Anastassja
dc.contributor.authorWackerow, Wiebke
dc.contributor.authorArcher, John A.C.
dc.contributor.authorRueping, Magnus
dc.contributor.authorWeuster-Botz, Dirk
dc.contributor.authorGroll, Michael
dc.contributor.authorEppinger, Jörg
dc.contributor.authorArold, Stefan T.
dc.date.accessioned2017-12-07T13:16:38Z
dc.date.available2017-12-07T13:16:38Z
dc.date.issued2017-12-18
dc.identifier.citationGrötzinger SW, Karan R, Strillinger E, Bader S, Frank A, et al. (2017) Identification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes. ACS Chemical Biology. Available: http://dx.doi.org/10.1021/acschembio.7b00792.
dc.identifier.issn1554-8929
dc.identifier.issn1554-8937
dc.identifier.doi10.1021/acschembio.7b00792
dc.identifier.urihttp://hdl.handle.net/10754/626319
dc.description.abstractBecause only 0.01% of prokaryotic genospecies can be cultured and in situ observations are often impracticable, culture-independent methods are required to understand microbial life and harness potential applications of microbes. Here, we report a methodology for the production of proteins with desired functions based on single amplified genomes (SAGs) from unculturable species. We use this method to resurrect an alcohol dehydrogenase (ADH/D1) from an uncharacterized halo-thermophilic archaeon collected from a brine pool at the bottom of the Red Sea. Our crystal structure of 5,6-dihydroxy NADPH-bound ADH/D1 combined with biochemical analyses reveal the molecular features of its halo-thermophily, its unique habitat adaptations, and its possible reaction mechanism for atypical oxygen activation. Our strategy offers a general guide for using SAGs as a source for scientific and industrial investigations of ‘microbial dark matter’.
dc.description.sponsorshipThe research reported in this publication was supported by the King Abdullah University of Science and Technology (KAUST) through the baseline fund and the Office of Sponsored Research (OSR) under award nos. URF/1/1976.06, URF/1/2602.01.01, and URF/1/1974. The authors are thankful for support for E.S. and S.G. from the International Graduate School of Science and Engineering (IGGSE), Technical University of Munich (TUM), project 8.03.
dc.publisherAmerican Chemical Society (ACS)
dc.relation.urlhttp://pubs.acs.org/doi/abs/10.1021/acschembio.7b00792
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Chemical Biology, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/abs/10.1021/acschembio.7b00792.
dc.subjectHalophilic
dc.subjectthermophilic
dc.subjectextremozyme
dc.subjectsingle.cell amplified genome
dc.subject5,6.dihydroxy NADPH
dc.subjectbiotechnology
dc.titleIdentification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes
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.departmentKAUST Catalysis Center (KCC)
dc.contributor.departmentOffice of the VP
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.contributor.departmentStructural Biology and Engineering
dc.identifier.journalACS Chemical Biology
dc.eprint.versionPost-print
dc.contributor.institutionTechnical University of Munich, Department of Mechanical Engineering, Institute of Biochemical Engineering, Garching, Germany
dc.contributor.institutionTechnical University of Munich, Center for Integrated Protein Science Munich in the Department Chemistry, Garching, Germany
kaust.personGrötzinger, Stefan W.
kaust.personKaran, Ram
kaust.personStrillinger, Eva
kaust.personBader, Stefan
kaust.personAl Rowaihi, Israa
kaust.personAkal, Anastassja
kaust.personWackerow, Wiebke
kaust.personArcher, John A.C.
kaust.personRueping, Magnus
kaust.personEppinger, Jorg
kaust.personArold, Stefan T.
kaust.grant.numberURF/1/1976.06
kaust.grant.numberURF/1/2602.01.01
kaust.grant.numberURF/1/1974
refterms.dateFOA2018-11-30T00:00:00Z
dc.date.published-online2017-12-18
dc.date.published-print2018-01-19


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