Flavoprotein monooxygenases (FPMOs) are single-or two-component enzymes that
catalyze a diverse set of chemo-, regio-and enantioselective oxyfunctionalization reactions …

The enzymatic generation of carbon–halogen bonds is a powerful strategy used by both
nature and synthetic chemists to tune the bioactivity, bioavailability and reactivity of …

Enzymes are powerful catalysts for site-selective C–H bond functionalization. Identifying
suitable enzymes for this task and for biocatalysis in general remains challenging, however …

Flavoprotein monooxygenases create valuable compounds that are of high interest for the
chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases …

Fungi are a prolific source of bioactive compounds, some of which have been developed as
essential medicines and life-enhancing drugs. Genome sequencing has revealed that fungi …

Prenyltransfer is an early-stage carbon–hydrogen bond (C–H) functionalization prevalent in
the biosynthesis of a diverse array of biologically active bacterial, fungal, plant, and …

Covering: up to February 2017 Various fungi of the genera Aspergillus, Penicillium, and
Malbranchea produce prenylated indole alkaloids possessing a bicyclo [2.2. 2] diazaoctane …

The ability to site-selectively modify equivalent functional groups in a molecule has the
potential to streamline syntheses and increase product yields by lowering step counts …

Prenylated indole alkaloids featuring spirooxindole rings possess a 3 R or 3 S carbon
stereocenter, which determines the bioactivities of these compounds. Despite the …

Flavin-dependent halogenases catalyse halogenation of aromatic compounds. In most
cases, this reaction proceeds with high regioselectivity and requires only the presence of …