ArticleAngewandte Chemie (International ed. in English)2016
Structure and Function of a "Head-to-Middle" Prenyltransferase: Lavandulyl Diphosphate Synthase.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
- Biosynthesis of irregular monoterpene lavandulol inSynthetic and systems biotechnology · 2025Article
- Plant (di)terpenoid evolution: from pigments to hormones and beyond.Natural product reports · 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
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 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
- Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.Natural product reports · 2020Review
- Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Catalytic Role of Conserved Asparagine, Glutamine, Serine, and Tyrosine Residues in Isoprenoid Biosynthesis Enzymes.ACS catalysis · 2018Article
- Structural and Chemical Biology of Terpenoid Cyclases.Chemical reviews · 2017Review
- Head-to-Head Prenyl Synthases in Pathogenic Bacteria.Chembiochem : a European journal of chemical biology · 2017Article
- cis-Prenyltransferase: New Insights into Protein Glycosylation, Rubber Synthesis, and Human Diseases.The Journal of biological chemistry · 2016Review
- A versatile cis-prenyltransferase from Methanosarcina mazei catalyzes both C- and O-prenylations.The Journal of biological chemistryArticle
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Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
Abstract
We report the first X-ray structure of the unique "head-to-middle" monoterpene synthase, lavandulyl diphosphate synthase (LPPS). LPPS catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to the fragrance lavandulol. The structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase (UPPS), and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DMAPP nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 (Asn in UPPS) is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product. The results are of interest since they provide the first structure and structure-based mechanism of this unusual prenyl synthase.
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