ArticleActa crystallographica. Section D, Structural biology2017
Molecular architectures of benzoic acid-specific type III polyketide synthases.
Article in Acta crystallographica. Section D, Structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 15 citations in OpenAlex.
- Elucidating the Iterative Elongation Mechanism in a Type III Polyketide Synthase.Journal of the American Chemical Society · 2025Article
- Characterization and functional analysis of type III polyketide synthases in Selaginella moellendorffii.Planta · 2025Article
- Structural and Interactional Analysis of the Flavonoid Pathway Proteins: Chalcone Synthase, Chalcone Isomerase and Chalcone Isomerase-like Protein.International journal of molecular sciences · 2024Article
- Xanthone Biosynthetic Pathway in Plants: A Review.Frontiers in plant science · 2022Review
- Construction of an Artificial Biosynthetic Pathway for the Styrylpyrone Compound 11-Methoxy-Bisnoryangonin Produced in EngineeredFrontiers in microbiology · 2021Article
- An Overview of the Medicinally Important Plant Type III PKS Derived Polyketides.Frontiers in plant science · 2021Review
- The crystal structure of benzophenone synthase from Garcinia mangostana L. pericarps reveals the basis for substrate specificity and catalysis.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Benzoate-CoA ligase contributes to the biosynthesis of biphenyl phytoalexins in elicitor-treated pear cell cultures.Plant cell reports · 2020Article
- Article
- How structural subtleties lead to molecular diversity for the type III polyketide synthases.The Journal of biological chemistry · 2019Review
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
Biphenyl synthase and benzophenone synthase constitute an evolutionarily distinct clade of type III polyketide synthases (PKSs) that use benzoic acid-derived substrates to produce defense metabolites in plants. The use of benzoyl-CoA as an endogenous substrate is unusual for type III PKSs. Moreover, sequence analyses indicate that the residues responsible for the functional diversification of type III PKSs are mutated in benzoic acid-specific type III PKSs. In order to gain a better understanding of structure-function relationships within the type III PKS family, the crystal structures of biphenyl synthase from Malus × domestica and benzophenone synthase from Hypericum androsaemum were compared with the structure of an archetypal type III PKS: chalcone synthase from Malus × domestica. Both biphenyl synthase and benzophenone synthase contain mutations that reshape their active-site cavities to prevent the binding of 4-coumaroyl-CoA and to favor the binding of small hydrophobic substrates. The active-site cavities of biphenyl synthase and benzophenone synthase also contain a novel pocket associated with their chain-elongation and cyclization reactions. Collectively, these results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants.
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