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dc.contributor.authorZhao, Qing
dc.contributor.authorCui, Meng-Ying
dc.contributor.authorLevsh, Olesya
dc.contributor.authorYang, Dongfeng
dc.contributor.authorLiu, Jie
dc.contributor.authorLi, Jie
dc.contributor.authorHill, Lionel
dc.contributor.authorYang, Lei
dc.contributor.authorHu, Yonghong
dc.contributor.authorWeng, Jing-Ke
dc.contributor.authorChen, Xiao-Ya
dc.contributor.authorMartin, Cathie
dc.date.accessioned2018-07-13T16:31:15Z
dc.date.available2018-07-13T16:31:15Z
dc.date.issued2017-08
dc.date.submitted2017-08
dc.identifier.issn1752-9859
dc.identifier.issn1752-9867
dc.identifier.urihttp://hdl.handle.net/1721.1/116980
dc.description.abstractBaicalein, wogonin, and their glycosides are major bioactive compounds found in the medicinal plant Scutellaria baicalensis Georgi. These flavones can induce apoptosis in a variety of cancer cell lines but have no effect on normal cells. Furthermore, they have many additional benefits for human health, such as anti-oxidant, antiviral, and liver-protective properties. Here, we report the isolation and characterization of two CYP450 enzymes, SbCYP82D1.1 and SbCYP82D2, which function as the flavone 6-hydroxylase (F6H) and flavone 8-hydroxylase (F8H), respectively, in S. baicalensis. SbCYP82D1.1 has broad substrate specificity for flavones such as chrysin and apigenin and is responsible for biosynthesis of baicalein and scutellarein in roots and aerial parts of S. baicalensis, respectively. When the expression of SbCYP82D1.1 is knocked down, baicalin and baicalein levels are reduced significantly while chrysin glycosides accumulate in hairy roots. SbCYP82D2 is an F8H with high substrate specificity, accepting only chrysin as its substrate to produce norwogonin, although minor 6-hydroxylation activity can also be detected. Phylogenetic analysis suggested that SbCYP82D2 might have evolved from SbCYP82D1.1 via gene duplication followed by neofunctionalization, whereby the ancestral F6H activity is partially retained in the derived SbCYP82D2. We report the characterization of two CYP450 enzymes, which 6- and 8-hydroxylate chrysin to form the 4′-deoxyflavone bioactives in roots of Scutellaria baicalensis. Like the main 4′-deoxyflavone enzymes, these decorating enzymes have evolved their functionalities by convergence with the more ubiquitous 4′-hydroxyflavone pathway enzymes. Key words: Scutellaria baicalensis; Huangqin; baicalein; wogonin; flavone 6-hydroxylase; flavone 8-hydroxylaseen_US
dc.publisherElsevieren_US
dc.relation.isversionofhttp://dx.doi.org/10.1016/J.MOLP.2017.08.009en_US
dc.rightsCreative Commons Attribution 4.0 International Licenseen_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.sourceElsevieren_US
dc.titleTwo CYP82D Enzymes Function as Flavone Hydroxylases in the Biosynthesis of Root-Specific 4′-Deoxyflavones in Scutellaria baicalensisen_US
dc.typeArticleen_US
dc.identifier.citationZhao, Qing et al. “Two CYP82D Enzymes Function as Flavone Hydroxylases in the Biosynthesis of Root-Specific 4′-Deoxyflavones in Scutellaria Baicalensis.” Molecular Plant 11, 1 (January 2018): 135–148 © 2017 The Authorsen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.mitauthorLevsh, Olesya
dc.contributor.mitauthorWeng, Jing-Ke
dc.relation.journalMolecular Planten_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2018-07-13T12:34:43Z
dspace.orderedauthorsZhao, Qing; Cui, Meng-Ying; Levsh, Olesya; Yang, Dongfeng; Liu, Jie; Li, Jie; Hill, Lionel; Yang, Lei; Hu, Yonghong; Weng, Jing-Ke; Chen, Xiao-Ya; Martin, Cathieen_US
dspace.embargo.termsNen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-8229-8642
mit.licensePUBLISHER_CCen_US


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