ArticleACS catalysis2021
Bacterial diterpene synthases prenylate small molecules.
Article in ACS catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Stereoselective Prenylation of Aryl- and Heteroaryl Halides: γ-Selective Suzuki-Miyaura Coupling as a Tool for Asymmetric CspThe Journal of organic chemistry · 2026Article
- Post-translational modifications in ferroptosis: mechanisms and therapeutic potential.International journal of biological sciences · 2026Review
- Structure-Activity Relationship of an All-α-helical Prenyltransferase Reveals the Mechanism of Indole Prenylation.Biochemistry · 2025Article
- Discovery of bacterial terpenoids by genome mining.Methods in enzymology · 2025Article
- Boswellianols A-I, Structurally Diverse Diterpenoids from the Oleo-Gum Resin ofPlants (Basel, Switzerland) · 2024Article
- Molecular insights into the catalytic promiscuity of a bacterial diterpene synthase.Nature communications · 2023Article
- FirstChem · 2023Article
- Mutation of the eunicellane synthase Bnd4 alters its product profile and expands its prenylation ability.Organic & biomolecular chemistry · 2022Article
- Thermoadaptation in an Ancestral Diterpene Cyclase by Altered Loop Stability.The journal of physical chemistry. B · 2022Article
- Identification of the new prenyltransferase Ubi-297 from marine bacteria and elucidation of its substrate specificity.Beilstein journal of organic chemistry · 2022Article
- Mechanistic Insights into the Formation of the 6,10-Bicyclic Eunicellane Skeleton by the Bacterial Diterpene Synthase Bnd4.Angewandte Chemie (International ed. in English) · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The biosynthesis of terpenoid natural products begins with a carbocation-based cyclization or prenylation reaction. While these reactions are mechanistically similar, there are several families of enzymes, namely terpene synthases and prenyltransferases, that have evolved to specifically catalyze terpene cyclization or prenylation reactions. Here, we report that bacterial diterpene synthases, enzymes that are traditionally considered to be specific for cyclization, are capable of efficiently catalyzing both diterpene cyclization and the prenylation of small molecules. We investigated this unique dual reactivity of terpene synthases through a series of kinetic, biocatalytic, structural, and bioinformatics studies. Overall, this study unveils the ability of terpene synthases to catalyze
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