Genome Mining Reveals the Biosynthesis of Sativene and Its Oxidative Conversion to <i>seco</i>-Sativene
Huaran Zhang, Hai-yan Zhao, Yuqi Huang, Yi Zou
Abstract
Sativene ( 1 ) and seco -sativene are an important family of fungal sesquiterpenoids that feature unique tricyclo[4.4.0.0 1,7 ]decane and bicyclo[3.2.1]octane skeletons, respectively. Herein, we identify a three-enzyme cassette: SatA cyclizes farnesyl diphosphate (FPP) to form compound 1; CYP450 SatB catalyzes C14–C15 dihydroxylations and subsequent bond cleavage; and reductase SatC regioselectively reduces C14 aldehyde and mediates hemiacetal ring closure to generate prehelminthosporol ( 2 ). Our findings clarify the synthetic step of sativene and its oxidative transformation processes into seco -sativene.
Topics & Concepts
ChemistryHemiacetalStereochemistryOxidative cleavageOxidative phosphorylationAldehydeOctaneRing (chemistry)DecaneReductaseBiocatalysisEnzymeBicyclic moleculeBiosynthesisBiochemistryCatalysisOrganic chemistryIonic liquidPlant biochemistry and biosynthesisMicrobial Natural Products and BiosynthesisFungal Biology and Applications