ReviewThe Journal of biological chemistry2019
How structural subtleties lead to molecular diversity for the type III polyketide synthases.
Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 73 citations in OpenAlex.
- A case study of evolutionary variability and determinism among type III polyketide synthases.Nature communications · 2026Article
- Integrative structural and physicochemical characterization of chalcone synthase enzymes from medicinal plants using AlphaFold, molecular docking, and molecular dynamics.Scientific reports · 2026Article
- Molecular basis of very-long-chain fatty acid elongation by the CER6-GL2 enzyme complex in plant wax biosynthesis.Science advances · 2025Article
- Elucidating the Iterative Elongation Mechanism in a Type III Polyketide Synthase.Journal of the American Chemical Society · 2025Article
- Comparison of the Blood-Brain Barrier Penetration Ability and Anti-Neuroinflammatory Activity of Chromones in Two Types of Agarwood.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Characterization and functional analysis of type III polyketide synthases in Selaginella moellendorffii.Planta · 2025Article
- Methyltransferase Domain-Focused Genome Mining for Fungal Polyketide Synthases.Small methods · 2024Article
- Structural insights into type III polyketide synthase CylI from cylindrocyclophane biosynthesis.Protein science : a publication of the Protein Society · 2024Article
- Evaluating the Metabolomic Profile and Anti-Pathogenic Properties ofMetabolites · 2024Review
- Chalcone-Synthase-EncodingMolecules (Basel, Switzerland) · 2024Article
- Complete biosynthesis of the potent vaccine adjuvant QS-21.Nature chemical biology · 2024Article
- Cloning of threeHeliyon · 2024Article
- Identification of a diarylpentanoid-producing polyketide synthase in the biosynthesis of 2-(2-phenylethyl)chromones in agarwood.Journal of natural medicines · 2023Review
- Reshaping the 2-Pyrone Synthase Active Site for Chemoselective Biosynthesis of Polyketides.Angewandte Chemie (International ed. in English) · 2023Article
- Evolution and function of red pigmentation in land plants.Annals of botany · 2022Review
- Scale-up of an amoeba-based process for the production of the cannabinoid precursor olivetolic acid.Microbial cell factories · 2022Article
- Polyketide reductases in defense-related parasorboside biosynthesis in Gerbera hybrida share processing strategies with microbial polyketide synthase systems.The New phytologist · 2022Article
- Intrinsic Ability of the β-Oxidation Pathway To Produce Bioactive Styrylpyrones.Angewandte Chemie (International ed. in English) · 2022Article
- Engineering the amoeba Dictyostelium discoideum for biosynthesis of a cannabinoid precursor and other polyketides.Nature biotechnology · 2022Article
- Engineered biosynthesis of plant polyketides by type III polyketide synthases in microorganisms.Frontiers in bioengineering and biotechnology · 2022Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type III polyketide synthases (PKSs) produce an incredibly diverse group of plant specialized metabolites with medical importance despite their structural simplicity compared with the modular type I and II PKS systems. The type III PKSs use homodimeric proteins to construct the molecular scaffolds of plant polyketides by iterative condensations of starter and extender CoA thioesters. Ever since the structure of chalcone synthase (CHS) was disclosed in 1999, crystallographic and mutational studies of the type III PKSs have explored the intimate structural features of these enzyme reactions, revealing that seemingly minor alterations in the active site can drastically change the catalytic functions and product profiles. New structures described in this review further build on this knowledge, elucidating the detailed catalytic mechanism of enzymes that make curcuminoids, use extender substrates without the canonical CoA activator, and use noncanonical starter substrates, among others. These insights have been critical in identifying structural features that can serve as a platform for enzyme engineering via structure-guided and precursor-directed engineered biosynthesis of plant polyketides. In addition, we describe the unique properties of the recently discovered "second-generation" type III PKSs that catalyzes the one-pot formation of complex molecular scaffolds from three distinct CoA thioesters or from "CoA-free" substrates, which are also providing exciting new opportunities for synthetic biology approaches. Finally, we consider post-type III PKS tailoring enzymes, which can also serve as useful tools for combinatorial biosynthesis of further unnatural novel molecules. Recent progress in the field has led to an exciting time of understanding and manipulating these fascinating enzymes.
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