Unique animal prenyltransferase with monoterpene synthase activity |
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Authors: | Anna B Gilg Claus Tittiger Gary J Blomquist |
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Institution: | (1) Department of Biochemistry and Molecular Biology/MS 330, University of Nevada, Reno, Reno, NV, 89557-0014, USA |
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Abstract: | Monoterpenes are structurally diverse natural compounds that play an essential role in the chemical ecology of a wide array
of organisms. A key enzyme in monoterpene biosynthesis is geranyl diphosphate synthase (GPPS). GPPS is an isoprenyl diphosphate
synthase that catalyzes a single electrophilic condensation reaction between dimethylallyl diphosphate (C5) and isopentenyl diphosphate (C5) to produce geranyl diphosphate (GDP; C10). GDP is the universal precursor to all monoterpenes. Subsequently, monoterpene synthases are responsible for the transformation
of GDP to a variety of acyclic, monocyclic, and bicyclic monoterpene products. In pheromone-producing male Ips pini bark beetles (Coleoptera: Scolytidae), the acyclic monoterpene myrcene is required for the production of the major aggregation
pheromone component, ipsdienol. Here, we report monoterpene synthase activity associated with GPPS of I. pini. Enzyme assays were performed on recombinant GPPS to determine the presence of monoterpene synthase activity, and the reaction
products were analyzed by coupled gas chromatography–mass spectrometry. The functionally expressed recombinant enzyme produced
both GDP and myrcene, making GPPS of I. pini a bifunctional enzyme. This unique insect isoprenyl diphosphate synthase possesses the functional plasticity that is characteristic
of terpene biosynthetic enzymes of plants, contributing toward the current understanding of product specificity of the isoprenoid
pathway. |
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Keywords: | Pheromone Mevalonate pathway Isoprenyl diphosphate Monoterpene |
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