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dc.contributor.authorPeters, Christin-
dc.contributor.authorFrasson, David-
dc.contributor.authorSievers, Martin-
dc.contributor.authorBuller, Rebecca-
dc.date.accessioned2019-03-28T13:23:57Z-
dc.date.available2019-03-28T13:23:57Z-
dc.date.issued2019-02-
dc.identifier.issn1439-4227de_CH
dc.identifier.issn1439-7633de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/16372-
dc.description.abstractMany drug candidate molecules contain at least one chiral centre and consequently, the development of biocatalytic strategies to complement existing metal- and organocatalytic approaches is of high interest. However, time is a critical factor in chemical process development and thus, the introduction of biocatalytic steps, even if more suitable, is often prevented by the limited availability of off-the-shelf enzyme libraries. To expand the biocatalytic toolbox with additional ene reductases, we screened 19 bacterial strains for double bond reduction activity using the model substrates cyclohexanone and carvone. Overall, we identified 47 genes coding for putative ene reductases. Remarkably, bioinformatic analysis of all genes and the biochemical characterization of four representative novel ene reductases led us to propose the existence of two new Old Yellow Enzyme subclasses, which we named OYE class III and class IV. Our results demonstrate that while on a DNA level each new OYE subclass features a distinct combination of sequence motifs previously known from the classical and the thermophilic-like group, their substrate scope more closely resembles the latter subclass.de_CH
dc.language.isoende_CH
dc.publisherWileyde_CH
dc.relation.ispartofChemBioChemde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subjectBiocatalytic toolboxde_CH
dc.subjectEne reductasede_CH
dc.subjectEnzyme sourcingde_CH
dc.subjectNovel Old Yellow Enzyme subclassesde_CH
dc.subjectPhylogenetic analysisde_CH
dc.subject.ddc660.6: Biotechnologiede_CH
dc.titleNovel Old Yellow Enzyme subclassesde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.1002/cbic.201800770de_CH
dc.identifier.pmid30758121de_CH
zhaw.funding.euNode_CH
zhaw.originated.zhawYesde_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.webfeedBiokatalysede_CH
Appears in collections:Publikationen Life Sciences und Facility Management

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