ArticleProceedings of the National Academy of Sciences of the United States of America2020
Algal neurotoxin biosynthesis repurposes the terpene cyclase structural fold into an
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Divergent Lineage of Terpene Synthases Establishes Terpenoid Biosynthesis in Brown Macroalgae.Journal of the American Chemical Society · 2026Article
- Article
- Acquisition and evolution of the neurotoxin domoic acid biosynthesis gene cluster in Pseudo-nitzschia species.Communications biology · 2024Article
- Molecular forecasting of domoic acid during a pervasive toxic diatom bloom.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Expression, purification, and biochemical characterization of micro- and macroalgal kainoid synthases.Methods in enzymology · 2024Article
- Domoic acid biosynthesis in the red algaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Alternative metabolic pathways and strategies to high-titre terpenoid production inNatural product reports · 2022Review
- Toxicity of the Diatom GenusToxins · 2022Article
- A roadmap for metagenomic enzyme discovery.Natural product reports · 2021Review
- Recent trends in biocatalysis.Chemical Society reviews · 2021Review
- Bacterial diterpene synthases prenylate small molecules.ACS catalysis · 2021Article
- Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids.Journal of industrial microbiology & biotechnology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prenylation is a common biological reaction in all domains of life wherein prenyl diphosphate donors transfer prenyl groups onto small molecules as well as large proteins. The enzymes that catalyze these reactions are structurally distinct from ubiquitous terpene cyclases that, instead, assemble terpenes via intramolecular rearrangements of a single substrate. Herein, we report the structure and molecular details of a new family of prenyltransferases from marine algae that repurposes the terpene cyclase structural fold for the
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.