geranyl-pyrophosphate and myrcene

geranyl-pyrophosphate has been researched along with myrcene* in 2 studies

Other Studies

2 other study(ies) available for geranyl-pyrophosphate and myrcene

ArticleYear
Transcriptome profiling of the Australian arid-land plant Eremophila serrulata (A.DC.) Druce (Scrophulariaceae) for the identification of monoterpene synthases.
    Phytochemistry, 2017, Volume: 136

    Plant terpenoids are a large and highly diverse class of metabolites with an important role in the immune defense. They find wide industrial application as active pharmaceutical ingredients, aroma and fragrance compounds. Several Eremophila sp. derived terpenoids have been documented. To elucidate the terpenoid metabolism, the transcriptome of juvenile and mature Eremophila serrulata (A.DC.) Druce (Scrophulariaceae) leaves was sequenced and a transcript library was generated. We report on the first transcriptomic dataset of an Eremophila plant. IlluminaMiSeq sequencing (2 × 300 bp) revealed 7,093,266 paired reads, which could be assembled to 34,505 isogroups. To enable detection of terpene biosynthetic genes, leaves were separately treated with methyl jasmonate, a well-documented inducer of plant secondary metabolites. In total, 21 putative terpene synthase genes were detected in the transcriptome data. Two terpene synthase isoenzymatic genes, termed ES01 and ES02, were successfully expressed in E. coli. The resulting proteins catalyzed the conversion of geranyl pyrophosphate, the universal substrate of monoterpene synthases to myrcene and Z-(b)-ocimene, respectively. The transcriptomic data and the discovery of the first terpene synthases from Eremophila serrulata are the initial step for the understanding of the terpene metabolism in this medicinally important plant genus.

    Topics: Acetates; Acyclic Monoterpenes; Alkenes; Alkyl and Aryl Transferases; Australia; Cyclopentanes; Eremophila Plant; Escherichia coli; Gene Expression Profiling; Intramolecular Lyases; Monoterpenes; Oxylipins; Plant Proteins; Polyisoprenyl Phosphates; Scrophulariaceae; Terpenes

2017
Unique animal prenyltransferase with monoterpene synthase activity.
    Die Naturwissenschaften, 2009, Volume: 96, Issue:6

    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 (C(5)) and isopentenyl diphosphate (C(5)) to produce geranyl diphosphate (GDP; C(10)). 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.

    Topics: Acyclic Monoterpenes; Alkenes; Alkyl and Aryl Transferases; Animals; Coleoptera; Dimethylallyltranstransferase; Diphosphates; Diterpenes; DNA Primers; Escherichia coli; Hydroxylation; Kinetics; Monoterpenes; Polymerase Chain Reaction; Recombinant Proteins; Restriction Mapping

2009