ArticleThe Journal of biological chemistry2013
The biosynthetic origin of irregular monoterpenes in Lavandula: isolation and biochemical characterization of a novel cis-prenyl diphosphate synthase gene, lavandulyl diphosphate synthase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 108 citations in OpenAlex.
- Structural classification, biosynthesis, metabolic engineering and ecological functions for the terpenes produced in tobacco.Frontiers in plant science · 2026Review
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- Biosynthesis of irregular monoterpene lavandulol inSynthetic and systems biotechnology · 2025Article
- Advances in the Biosynthesis of Plant Terpenoids: Models, Mechanisms, and Applications.Plants (Basel, Switzerland) · 2025Review
- Efficient accumulation of new irregular monoterpene malonyl glucosides inFrontiers in plant science · 2025Article
- Article
- Metabolic engineering of terpene metabolism in lavender.Beni-Suef University journal of basic and applied sciences · 2024Review
- Decoupling subgenomes within hybrid lavandin provide new insights into speciation and monoterpenoid diversification of Lavandula.Plant biotechnology journal · 2023Article
- Evaluation of VariousJournal of microbiology and biotechnology · 2023Article
- Plant terpene specialized metabolism: complex networks or simple linear pathways?The Plant journal : for cell and molecular biology · 2023Review
- Lavandula Species, Their Bioactive Phytochemicals, and Their Biosynthetic Regulation.International journal of molecular sciences · 2023Review
- Plant (di)terpenoid evolution: from pigments to hormones and beyond.Natural product reports · 2023Review
- Grapevine mono- and sesquiterpenes: Genetics, metabolism, and ecophysiology.Frontiers in plant science · 2023Review
- Alternative metabolic pathways and strategies to high-titre terpenoid production inNatural product reports · 2022Review
- Engineering of a Plant Isoprenyl Diphosphate Synthase for Development of Irregular Coupling Activity.Chembiochem : a European journal of chemical biology · 2022Article
- The chromosome-based lavender genome provides new insights into Lamiaceae evolution and terpenoid biosynthesis.Horticulture research · 2021Article
- Isoprenoid Metabolism and Engineering in Glandular Trichomes ofFrontiers in plant science · 2021Review
- The biosynthesis of the anti-microbial diterpenoid leubethanol in Leucophyllum frutescens proceeds via an all-cis prenyl intermediate.The Plant journal : for cell and molecular biology · 2020Article
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
- Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.Natural product reports · 2020Review
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Lavender essential oils are constituted predominantly of regular monoterpenes, for example linalool, 1,8-cineole, and camphor. However, they also contain irregular monoterpenes including lavandulol and lavandulyl acetate. Although the majority of genes responsible for the production of regular monoterpenes in lavenders are now known, enzymes (including lavandulyl diphosphate synthase (LPPS)) catalyzing the biosynthesis of irregular monoterpenes in these plants have not been described. Here, we report the isolation and functional characterization of a novel cis-prenyl diphosphate synthase cDNA, termed Lavandula x intermedia lavandulyl diphosphate synthase (LiLPPS), through a homology-based cloning strategy. The LiLPPS ORF, encoding for a 305-amino acid long protein, was expressed in Escherichia coli, and the recombinant protein was purified by nickel-nitrilotriacetic acid affinity chromatography. The approximately 34.5-kDa bacterially produced protein specifically catalyzed the head-to-middle condensation of two dimethylallyl diphosphate units to LPP in vitro with apparent Km and kcat values of 208 ± 12 μm and 0.1 s(-1), respectively. LiLPPS is a homodimeric enzyme with a sigmoidal saturation curve and Hill coefficient of 2.7, suggesting a positive co-operative interaction among its catalytic sites. LiLPPS could be used to modulate the production of lavandulol and its derivatives in plants through metabolic engineering.
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