Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Kang, Suk Woo | - |
dc.contributor.author | Antoney, James | - |
dc.contributor.author | Lupton, David W. | - |
dc.contributor.author | Speight, Robert | - |
dc.contributor.author | Scott, Colin | - |
dc.contributor.author | Jackson, Colin J. | - |
dc.date.accessioned | 2024-01-19T10:00:10Z | - |
dc.date.available | 2024-01-19T10:00:10Z | - |
dc.date.created | 2023-04-06 | - |
dc.date.issued | 2023-04 | - |
dc.identifier.issn | 1439-4227 | - |
dc.identifier.uri | https://pubs.kist.re.kr/handle/201004/113871 | - |
dc.description.abstract | Asymmetric 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.language | English | - |
dc.publisher | John Wiley & Sons Ltd. | - |
dc.title | Asymmetric Ene-Reduction by F420-Dependent Oxidoreductases B (FDOR-B) from Mycobacterium smegmatis | - |
dc.type | Article | - |
dc.identifier.doi | 10.1002/cbic.202200797 | - |
dc.description.journalClass | 1 | - |
dc.identifier.bibliographicCitation | ChemBioChem, v.24, no.8 | - |
dc.citation.title | ChemBioChem | - |
dc.citation.volume | 24 | - |
dc.citation.number | 8 | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.identifier.wosid | 000945793100001 | - |
dc.identifier.scopusid | 2-s2.0-85149513706 | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Medicinal | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Pharmacology & Pharmacy | - |
dc.type.docType | Article; Early Access | - |
dc.subject.keywordPlus | F420H2-DEPENDENT REDUCTASES | - |
dc.subject.keywordPlus | COFACTOR | - |
dc.subject.keywordPlus | COENZYME | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | F-420 | - |
dc.subject.keywordPlus | GLUCOSE-6-PHOSPHATE-DEHYDROGENASE | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | COVERAGE | - |
dc.subject.keywordPlus | ENZYMES | - |
dc.subject.keywordAuthor | biocatalysis | - |
dc.subject.keywordAuthor | deazaflavin | - |
dc.subject.keywordAuthor | F-420 | - |
dc.subject.keywordAuthor | ene-reductases | - |
dc.subject.keywordAuthor | Mycobacterium smegmatis | - |
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