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Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
Molecular cloning and characterization of a geranyl diphosphate-specific aromatic prenyltransferase from lemon
Ryosuke Munakata1, Tsuyoshi Inoue1, Takao Koeduka1
1Laboratory of Plant Gene Expression, Research Institute for Sustainable Humanosphere (R.M., A.S., K.T., K.Y.), and Institute for Chemical Research (T.K.), Kyoto University, Gokasho, Uji 611-0011, Japan;Division of Environmental Science and Technology, Graduate School of Agriculture, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan (T.I., J.-I.A.);Institut National de la Recherche Agronomique (F.K., A.O., A.D., A.H., F.B.), and Université de Lorraine (F.K., A.O., A.D., A.H., F.B.), Unité Mixte de Recherche 1121 Laboratoire Agronomie et Environnement Nancy-Colmar, TSA 40602, 54518 Vandœuvre-lès-Nancy cedex, France;Centre de Coopération Internationale en Recherche Agronomique pour le Développement, Unité Mixte de Recherche Amélioration Génétique et Adaptation des Plantes Méditerranéennes et Tropicales, F-34398 Montpellier, France (Y.F.); andDepartment of Life System, Institute of Technology and Science, Graduate School, University of Tokushima, Tokushima 770-8506, Japan (R.T., Y.U., H.H.).
Abstract:
Prenyl residues confer divergent biological activities such as antipathogenic and antiherbivorous activities on phenolic compounds, including flavonoids, coumarins, and xanthones. To date, about 1,000 prenylated phenolics have been isolated, with these compounds containing various prenyl residues. However, all currently described plant prenyltransferases (PTs) have been shown specific for dimethylallyl diphosphate as the prenyl donor, while most of the complementary DNAs encoding these genes have been isolated from the Leguminosae. In this study, we describe the identification of a novel PT gene from lemon (Citrus limon), ClPT1, belonging to the homogentisate PT family. This gene encodes a PT that differs from other known PTs, including flavonoid-specific PTs, in polypeptide sequence. This membrane-bound enzyme was specific for geranyl diphosphate as the prenyl donor and coumarin as the prenyl acceptor. Moreover, the gene product was targeted to plastid in plant cells. To our knowledge, this is the novel aromatic PT specific to geranyl diphosphate from citrus species.
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