ArticlePlant physiology2011
Structure and mechanism of an Arabidopsis medium/long-chain-length prenyl pyrophosphate synthase.
Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 76 citations in OpenAlex.
- Review
- The Catalytic Asymmetric Alkylation of Olefins with Alcohol Derivatives.Journal of the American Chemical Society · 2026Article
- Mysterious giants in the world of lipids: long linear isoprenoid functions in plant physiology and reproduction.Journal of experimental botany · 2026Review
- Structural insights into the molecular mechanisms of OsFBN5-induced OsSPS3 catalysis.Nature plants · 2026Article
- Systematic characterization and functional analysis ofFrontiers in plant science · 2025Article
- Genome-wide identification of the geranylgeranyl pyrophosphate synthase (GGPS) gene family involved in chlorophyll synthesis in cotton.BMC genomics · 2023Article
- Molecular characterization of cyanobacterial short-chain prenyltransferases and discovery of a novel GGPP phosphatase.The FEBS journal · 2022Article
- How plants synthesize coenzyme Q.Plant communications · 2022Review
- Article
- Genetic Manipulation of Biosynthetic Pathways in Mint.Frontiers in plant science · 2022Review
- Molecular and Functional Evolution of the Spermatophyte Sesquiterpene Synthases.International journal of molecular sciences · 2021Article
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 2021Review
- Genome-Wide Identification and Functional Characterization of the Trans-Isopentenyl Diphosphate Synthases Gene Family inFrontiers in plant science · 2021Article
- The Predicted Functional Compartmentation of Rice Terpenoid Metabolism byInternational journal of molecular sciences · 2020Article
- Functional Gene Network of Prenyltransferases inMolecules (Basel, Switzerland) · 2019Review
- Discovery of Geranylgeranyl Pyrophosphate Synthase (GGPPS) Paralogs fromMarine drugs · 2019Article
- Isoprenyl diphosphate synthases: the chain length determining step in terpene biosynthesis.Planta · 2019Review
- Functional Analysis of Polyprenyl Diphosphate Synthase Genes Involved in Plastoquinone and Ubiquinone Biosynthesis inFrontiers in plant science · 2019Article
- Terpene Synthases as Metabolic Gatekeepers in the Evolution of Plant Terpenoid Chemical Diversity.Frontiers in plant science · 2019Review
- A homomeric geranyl diphosphate synthase-encoding gene from Camptotheca acuminata and its combinatorial optimization for production of geraniol in Escherichia coli.Journal of industrial microbiology & biotechnology · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prenyltransferases (PTSs) are involved in the biosynthesis of terpenes with diverse functions. Here, a novel PTS from Arabidopsis (Arabidopsis thaliana) is identified as a trans-type polyprenyl pyrophosphate synthase (AtPPPS), which forms a trans-double bond during each homoallylic substrate condensation, rather than a homomeric C10-geranyl pyrophosphate synthase as originally proposed. Biochemical and genetic complementation analyses indicate that AtPPPS synthesizes C25 to C45 medium/long-chain products. Its close relationship to other long-chain PTSs is also uncovered by phylogenetic analysis. A mutant of contiguous surface polar residues was produced by replacing four charged surface amino acids with alanines to facilitate the crystallization of the enzyme. The crystal structures of AtPPPS determined here in apo and ligand-bound forms further reveal an active-site cavity sufficient to accommodate the medium/long-chain products. The two monomers in each dimer adopt different conformations at the entrance of the active site depending on the binding of substrates. Taken together, these results suggest that AtPPPS is endowed with a unique functionality among the known PTSs.
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