Phenolic 3-hydroxylases in land plants: biochemical diversity and molecular evolution

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dc.contributor.authorAlber, Annette Veronika
dc.contributor.supervisorEhlting, Jürgen
dc.contributor.supervisorWerck, Danièle
dc.date.accessioned2016-12-02T20:19:10Z
dc.date.copyright2016en_US
dc.date.issued2016-12-02
dc.degree.departmentDepartment of Biologyen_US
dc.degree.levelDoctor of Philosophy Ph.D.en_US
dc.description.abstractPlants produce a rich variety of natural products to face environmental constraints. Enzymes of the cytochrome P450 CYP98 family are key actors in the production of phenolic bioactive compounds. They hydroxylate phenolic esters for lignin biosynthesis in angiosperms, but also produce various other bioactive phenolics. We characterized CYP98s from a moss, a lycopod, a fern, a conifer, a basal angiosperm, a monocot and from two eudicots. We found that substrate preference of the enzymes has changed during evolution of land plants with typical lignin-related activities only appearing in angiosperms, suggesting that ferns, similar to lycopods, produce lignin through an alternative route. A moss CYP98 knock-out mutant revealed coumaroyl-threonate as CYP98 substrate in vivo and showed a severe phenotype. Multiple CYP98s per species exist only in the angiosperms, where we generally found one isoform presumably involved in the biosynthesis of monolignols, and additional isoforms, resulting from independent duplications, with a broad range of functions in vitroen_US
dc.description.scholarlevelGraduateen_US
dc.identifier.urihttp://hdl.handle.net/1828/7651
dc.languageEnglisheng
dc.language.isoenen_US
dc.rightsAvailable to the World Wide Weben_US
dc.subjectcytochrome P450en_US
dc.subjectland plant evolutionen_US
dc.subjectmonolignolen_US
dc.subjectCYP98en_US
dc.subjectC3'Hen_US
dc.subjectPopulus trichocarpaen_US
dc.subjectPhyscomitrella patensen_US
dc.subjectphenolic conjugateen_US
dc.subjecthydroxycinnamicen_US
dc.subjectligninen_US
dc.subjectcoumaroyl-threonateen_US
dc.subjectcoumaroyl-shikimateen_US
dc.titlePhenolic 3-hydroxylases in land plants: biochemical diversity and molecular evolutionen_US
dc.typeThesisen_US

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