A coumarin‐specific prenyltransferase catalyzes the crucial biosynthetic reaction for furanocoumarin formation in parsley

• DOI: 10.1111/tpj.12409
• Publication Date: 2013-12-13T12:34:49Z
• Authors: Fazeelat Karamat; Alexandre Olry; Ryosuke Munakata; Takao Koeduka; Akifumi Sugiyama; Cedric Paris; Alain Hehn; Frédéric Bourgaud; Kazufumi Yazaki
• Keywords: Furanocoumarin; Umbelliferone; Prenyltransferase

Furanocoumarins constitute a sub-family of coumarin compounds with important defense properties against pathogens and insects, as well allelopathic functions in plants. are divided into two sub-groups according to the alignment furan ring lactone structure: linear psoralen angular angelicin derivatives. Determination furanocoumarin type is based on prenylation position common precursor all furanocoumarins, umbelliferone, at C6 or C8, which gives rise derivatives, respectively. Here, we identified membrane-bound prenyltransferase PcPT from parsley (Petroselinum crispum), characterized gene product. expression various tissues increased by UV irradiation, concomitant increase production. This enzyme has strict substrate specificity towards umbelliferone dimethylallyl diphosphate, strong preference for prenylated product (demethylsuberosin), leading furanocoumarins. The C8-prenylated derivative (osthenol) also formed, but much lesser extent. protein targeted plastids planta. Introduction this coumarin-producing plant Ruta graveolens showed consumption endogenous umbelliferone. Expression 4-coumaroyl CoA 2'-hydroxylase Nicotiana benthamiana, does not produce resulted formation demethylsuberosin, indicating that production may be reconstructed metabolic engineering approach. results demonstrate single prenyltransferase, such PcPT, opens pathway furanocoumarins parsley, catalyze synthesis osthenol, first intermediate committed pathway, other