Characterization of a coumarin C -/ O -prenyltransferase and a quinolone C -prenyltransferase from Murraya exotica .
Na LiXiao LiuMingliang ZhangZekun ZhangBeibei ZhangXiaohui WangJuan WangPengfei TuXiaoni AiShe-Po ShiPublished in: Organic & biomolecular chemistry (2022)
Prenyltransferases (PTs) play important roles in the biosynthesis and structural diversification of natural products. In the present study, two new PTs were characterized from a medicinal plant Murraya exotica . MePT1 unprecedentedly catalyses the formation of two C -geranylated products 8/6- C -geranylumbelliferone together with a trace product 7- O -geranylumbelliferone from umbelliferone. MePT2 regio-specifically catalyses the formation of C-3 dimethylallylated products from quinolone alkaloids. This is the first report that a plant PT catalyses the simultaneous formation of C - and O -prenylated products, and a plant PT specifically utilizes quinolone alkaloids as prenyl acceptors. The results not only provide important insight into the functional diversity of plant PTs and the biosynthesis of the prenylated coumarins, quinolone and carbazole alkaloids in Murraya plants, but also pave the way for the overproduction of the prenylated coumarins and alkaloids using metabolic engineering approaches.
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