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A Monooxygenase from Boreostereum vibrans Catalyzes Oxidative Decarboxylation in a Divergent Vibralactone Biosynthesis Pathway
Author(s) -
Yang YanLong,
Zhou Hui,
Du Gang,
Feng KeNa,
Feng Tao,
Fu XiaoLi,
Liu JiKai,
Zeng Ying
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201510928
Subject(s) - prenylation , biosynthesis , monooxygenase , decarboxylation , oxidative decarboxylation , biochemistry , chemistry , prenyltransferase , stereochemistry , oxidative phosphorylation , enzyme , cytochrome p450 , catalysis
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.