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dc.contributor.authorKang, Suk Woo-
dc.contributor.authorAntoney, James-
dc.contributor.authorLupton, David W.-
dc.contributor.authorSpeight, Robert-
dc.contributor.authorScott, Colin-
dc.contributor.authorJackson, Colin J.-
dc.date.accessioned2024-01-19T10:00:10Z-
dc.date.available2024-01-19T10:00:10Z-
dc.date.created2023-04-06-
dc.date.issued2023-04-
dc.identifier.issn1439-4227-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/113871-
dc.description.abstractAsymmetric reduction by ene-reductases has received considerable attention in recent decades. While several enzyme families possess ene-reductase activity, the Old Yellow Enzyme (OYE) family has received the most scientific and industrial attention. However, there is a limited substrate range and few stereocomplementary pairs of current ene-reductases, necessitating the development of a complementary class. Flavin/deazaflavin oxidoreductases (FDORs) that use the uncommon cofactor F-420 have recently gained attention as ene-reductases for use in biocatalysis due to their stereocomplementarity with OYEs. Although the enzymes of the FDOR-As sub-group have been characterized in this context and reported to catalyse ene-reductions enantioselectively, enzymes from the similarly large, but more diverse, FDOR-B sub-group have not been investigated in this context. In this study, we investigated the activity of eight FDOR-B enzymes distributed across this sub-group, evaluating their specific activity, kinetic properties, and stereoselectivity against alpha,beta-unsaturated compounds. The stereochemical outcomes of the FDOR-Bs are compared with enzymes of the FDOR-A sub-group and OYE family. Computational modelling and induced-fit docking are used to rationalize the observed catalytic behaviour and proposed a catalytic mechanism.-
dc.languageEnglish-
dc.publisherJohn Wiley & Sons Ltd.-
dc.titleAsymmetric Ene-Reduction by F420-Dependent Oxidoreductases B (FDOR-B) from Mycobacterium smegmatis-
dc.typeArticle-
dc.identifier.doi10.1002/cbic.202200797-
dc.description.journalClass1-
dc.identifier.bibliographicCitationChemBioChem, v.24, no.8-
dc.citation.titleChemBioChem-
dc.citation.volume24-
dc.citation.number8-
dc.description.isOpenAccessY-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000945793100001-
dc.identifier.scopusid2-s2.0-85149513706-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryChemistry, Medicinal-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaPharmacology & Pharmacy-
dc.type.docTypeArticle; Early Access-
dc.subject.keywordPlusF420H2-DEPENDENT REDUCTASES-
dc.subject.keywordPlusCOFACTOR-
dc.subject.keywordPlusCOENZYME-
dc.subject.keywordPlusFAMILY-
dc.subject.keywordPlusF-420-
dc.subject.keywordPlusGLUCOSE-6-PHOSPHATE-DEHYDROGENASE-
dc.subject.keywordPlusIDENTIFICATION-
dc.subject.keywordPlusCOVERAGE-
dc.subject.keywordPlusENZYMES-
dc.subject.keywordAuthorbiocatalysis-
dc.subject.keywordAuthordeazaflavin-
dc.subject.keywordAuthorF-420-
dc.subject.keywordAuthorene-reductases-
dc.subject.keywordAuthorMycobacterium smegmatis-
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