Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-18903
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dc.contributor.authorHayashi, Takahiro-
dc.contributor.authorLigibel, Mathieu-
dc.contributor.authorSager, Emine-
dc.contributor.authorVoss, Moritz-
dc.contributor.authorHunziker, Jürg-
dc.contributor.authorSchroer, Kirsten-
dc.contributor.authorSnajdrova, Radka-
dc.contributor.authorBuller, Rebecca-
dc.date.accessioned2019-12-13T14:02:08Z-
dc.date.available2019-12-13T14:02:08Z-
dc.date.issued2019-10-
dc.identifier.issn1433-7851de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/18903-
dc.descriptionThis is the peer reviewed version which has been published in final form at [https://doi.org/10.1002/anie.201907245]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.de_CH
dc.description.abstractNon‐heme iron halogenases represent synthetically valuable biocatalysts that are capable of halogenating unactivated sp3‐hybridized carbon centers with exquisite stereo‐ and regioselectivity. The reported substrate scope of these enzymes, however, is limited primarily to the natural substrates and their analogues. Here we engineered the recently discovered halogenase WelO5* for chlorination of a pharmaceutically interesting martinelline‐derived fragment. Using structure‐guided evolution, a halogenase variant with a more than 290‐fold higher total turnover number and a 400‐fold higher apparent kcat compared to the wild‐type enzyme was generated. Moreover, we identified key positions in the active site which allowed directing the halogen to different positions in our target substrate. This report provides the first example of enzyme engineering to expand the substrate scope of a non‐heme iron halogenase beyond the native indole alkaloid‐type substrates. The highly evolvable nature of WelO5* underscores the usefulness of this enzyme family for the late‐stage halogenation of value‐added chemicals.de_CH
dc.language.isoende_CH
dc.publisherWileyde_CH
dc.relation.ispartofAngewandte Chemie: International Editionde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subject.ddc660: Technische Chemiede_CH
dc.titleEvolved aliphatic halogenases enable regiocomplementary C‐H functionalization of an added‐value chemicalde_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/anie.201907245de_CH
dc.identifier.doi10.21256/zhaw-18903-
zhaw.funding.euNode_CH
zhaw.issue51de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end18539de_CH
zhaw.pages.start18535de_CH
zhaw.publication.statusacceptedVersionde_CH
zhaw.volume58de_CH
zhaw.embargo.end2020-10-31de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.webfeedBiokatalysede_CH
zhaw.author.additionalNode_CH
Appears in collections:Publikationen Life Sciences und Facility Management

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