Identification and characterization of cytochrome P450 monooxygenases for monoterpenoid indole alkaloid diversification

dc.contributor.advisorQu, Yang
dc.contributor.authorMai, Zhan
dc.date.accessioned2025-05-22T17:09:29Z
dc.date.available2025-05-22T17:09:29Z
dc.date.issued2025-03
dc.description.abstractCytochrome P450 monooxygenases (CYPs) play a crucial role in monoterpenoid indole alkaloid (MIA) biosynthesis, mediating oxidation reactions like hydroxylation, epoxidation, and ring modifications that drive structural diversity. Despite advances in MIA pharmaceutical biosynthesis, many tailoring reactions remain poorly understood. By integrating transcriptomic and metabolomic data from Tabernaemontana litoralis and Vinca minor, I identified a novel MIA, 11-hydroxypseudovincadifformine, and characterized five CYPs involved in MIA oxidation. TliTbE from T. litoralis catalyzes pachysiphine formation, a lochnericine stereoisomer. TliPs18H is the first CYP modifying a pseudoaspidosperma skeleton. TliC10H hydroxylates voaphylline, while VmPs10H in V. minor completes akuammine biosynthesis and hydroxylates related MIAs. VmV10H further oxidizes structurally diverse MIAs. This study expands our understanding of MIA biosynthesis and enzyme function, unlocking new biocatalysts for MIA production and demonstrating the untapped potential of these plants in alkaloid diversification.
dc.description.copyrightZhan Mai, 2025
dc.format.extentxi, 208
dc.format.mediumelectronic
dc.identifier.urihttps://unbscholar.lib.unb.ca/handle/1882/38305
dc.language.isoen
dc.publisherUniversity of New Brunswick
dc.rightshttp://purl.org/coar/access_right/c_abf2
dc.subject.disciplineChemistry
dc.titleIdentification and characterization of cytochrome P450 monooxygenases for monoterpenoid indole alkaloid diversification
dc.typemaster thesis
oaire.license.conditionother
thesis.degree.disciplineChemistry
thesis.degree.grantorUniversity of New Brunswick
thesis.degree.levelmasters
thesis.degree.nameM.Sc.

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