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- Title
A Monooxygenase from Boreostereum vibrans Catalyzes Oxidative Decarboxylation in a Divergent Vibralactone Biosynthesis Pathway.
- Authors
Yang, Yan‐Long; Zhou, Hui; Du, Gang; Feng, Ke‐Na; Feng, Tao; Fu, Xiao‐Li; Liu, Ji‐Kai; Zeng, Ying
- Abstract
The oxidative decarboxylation of prenyl 4-hydroxybenzoate to prenylhydroquinone has been frequently proposed for the biosynthesis of prenylated (hydro)quinone derivates (sometimes meroterpenoids), yet no corresponding genes or enzymes have so far been reported. A FAD-binding monooxygenase (VibMO1) was identified that converts prenyl 4-hydroxybenzoate into prenylhydroquinone and is likely involved in the biosynthesis of vibralactones and other meroterpenoids in the basidiomycete Boreostereum vibrans. Feeding of 3-allyl-4-hydroxybenzylalcohol, an analogue of the vibralactone pathway intermediate 3-prenyl-4-hydroxybenzylalcohol, generated 20 analogues with different scaffolds. This demonstrated divergent pathways to skeletally distinct compounds initiating from a single precursor, thus providing the first insight into a novel biosynthetic pathway for 3-substituted γ-butyrolactones from a shikimate origin.
- Subjects
MONOOXYGENASES; HYDROXYBENZOATES; DECARBOXYLATION; BASIDIOMYCETES; BUTYROLACTONES
- Publication
Angewandte Chemie, 2016, Vol 128, Issue 18, p5553
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201510928