ArticleCommunications chemistry2022
Structure-guided product determination of the bacterial type II diterpene synthase Tpn2.
Article in Communications chemistry, 2022. 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.
- Dimerization-Dependent Trans-Domain Coupling Enables Intermediate Transfer in Fungal Haloacid Dehalogenase-Like Terpene Cyclases.Journal of the American Chemical Society · 2026Article
- Investigating conserved aromatic residues in ent-copalyl pyrophosphate synthases required for gibberellin phytohormone biosynthesis.Phytochemistry · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.Biochemistry · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.bioRxiv : the preprint server for biology · 2025Article
- The Evolutionary History and Modern Diversity of Triterpenoid Cyclases.Molecular biology and evolution · 2025Article
- The evolutionary history and modern diversity of triterpenoid cyclases.bioRxiv : the preprint server for biology · 2025Article
- Discovery of bacterial terpenoids by genome mining.Methods in enzymology · 2025Article
- Discovery of bifunctional diterpene cyclases/synthases in bacteria supports a bacterial origin for the plant terpene synthase gene family.Horticulture research · 2024Article
- Class II terpene cyclases: structures, mechanisms, and engineering.Natural product reports · 2024Review
- Extending the Structural Diversity of Labdane Diterpenoids from Marine-Derived FungusMarine drugs · 2023Article
- Discovery, Structure, and Mechanism of a Class II Sesquiterpene Cyclase.Journal of the American Chemical Society · 2022Article
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Authors and funding
5 authors.
Funding
Abstract
A grand challenge in terpene synthase (TS) enzymology is the ability to predict function from protein sequence. Given the limited number of characterized bacterial TSs and significant sequence diversities between them and their eukaryotic counterparts, this is currently impossible. To contribute towards understanding the sequence-structure-function relationships of type II bacterial TSs, we determined the structure of the terpentedienyl diphosphate synthase Tpn2 from Kitasatospora sp. CB02891 by X-ray crystallography and made structure-guided mutants to probe its mechanism. Substitution of a glycine into a basic residue changed the product preference from the clerodane skeleton to a syn-labdane skeleton, resulting in the first syn-labdane identified from a bacterial TS. Understanding how a single residue can dictate the cyclization pattern in Tpn2, along with detailed bioinformatics analysis of bacterial type II TSs, sets the stage for the investigation of the functional scope of bacterial type II TSs and the discovery of novel bacterial terpenoids.
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Registered trials
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