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Molecules 2015, 20(9), 15616-15630; doi:10.3390/molecules200915616

Molecular Cloning and Characterization of a Xanthone Prenyltransferase from Hypericum calycinum Cell Cultures

1
Institute of Pharmaceutical Biology, Technische Universität Braunschweig, Mendelssohnstraße 1, Braunschweig 38106, Germany
2
Center of Pharmaceutical Engineering (PVZ), Technische Universität Braunschweig, Franz-Liszt-Straße 35 A, Braunschweig 38106, Germany
3
Institute of Pharmacology, Toxicology and Clinical Pharmacy, Technische Universität Braunschweig, Mendelssohnstraße 1, Braunschweig 38106, Germany
4
Central NMR Laboratory, Technische Universität Braunschweig, Hagenring 30, Braunschweig 38106, Germany
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Thomas J. Schmidt
Received: 30 June 2015 / Revised: 17 August 2015 / Accepted: 20 August 2015 / Published: 27 August 2015
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Abstract

In plants, prenylation of metabolites is widely distributed to generate compounds with efficient defense potential and distinct pharmacological activities profitable to human health. Prenylated compounds are formed by members of the prenyltransferase (PT) superfamily, which catalyze the addition of prenyl moieties to a variety of acceptor molecules. Cell cultures of Hypericum calycinum respond to elicitor treatment with the accumulation of the prenylated xanthone hyperxanthone E. A cDNA encoding a membrane-bound PT (HcPT) was isolated from a subtracted cDNA library and transcript preparations of H. calycinum. An increase in the HcPT transcript level preceded hyperxanthone E accumulation in cell cultures of H. calycinum treated with elicitor. The HcPT cDNA was functionally characterized by expression in baculovirus-infected insect cells. The recombinant enzyme catalyzed biosynthesis of 1,3,6,7-tetrahydroxy-8-prenylxanthone through regiospecific C–8 prenylation of 1,3,6,7-tetrahydroxyxanthone, indicating its involvement in hyperxanthone E formation. The enzymatic product shared significant structural features with the previously reported cholinesterase inhibitor γ-mangostin. Thus, our findings may offer a chance for semisynthesis of new active agents to be involved in the treatment of Alzheimer’s disease. View Full-Text
Keywords: aromatic prenyltransferase; xanthone; Hypericum; membrane-bound enzyme; Alzheimer’s disease aromatic prenyltransferase; xanthone; Hypericum; membrane-bound enzyme; Alzheimer’s disease
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Fiesel, T.; Gaid, M.; Müller, A.; Bartels, J.; El-Awaad, I.; Beuerle, T.; Ernst, L.; Behrends, S.; Beerhues, L. Molecular Cloning and Characterization of a Xanthone Prenyltransferase from Hypericum calycinum Cell Cultures. Molecules 2015, 20, 15616-15630.

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