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Fig. 1 | BMC Plant Biology

Fig. 1

From: Functional characterization of the cytochrome P450 monooxygenase CYP71AU87 indicates a role in marrubiin biosynthesis in the medicinal plant Marrubium vulgare

Fig. 1

Proposed marrubiin-biosynthetic pathway. MvCPS1 and MvELS form a diterpene synthase pair that converts the central precursor geranylgeranyl diphosphate (GGPP) into 9,13-epoxy labd-14-ene 1 (and possibly additional closely related products including labda-13(16),14-dien-9-ol 2) via the prenyl diphosphate intermediate peregrinol diphosphate. Cytochrome P450 monooxygenases are hypothesized to catalyze position-specific functional modifications to yield premarrubiin possibly via the CYP71AU87 product 9,13-epoxy labd-14-en-19-ol 5 and other pathway intermediates such as premarrubenol previously identified in M. vulgare tissues. Subsequent lactone formation would form premarrubiin, from which marrubiin will derive through enzymatic or spontaneous ring opening to yield the free hydroxyl group at C-9. Dashed lines represent enzyme products identified in co-expression assays of MvCPS1 and MvELS in this study

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BMC Plant Biology

ISSN: 1471-2229

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