ArticleChembiochem : a European journal of chemical biology2023
The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases.
Article in Chembiochem : a European journal of chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 14 citations in OpenAlex.
- Haplotype-Phased Chromosome-Level Genome Assembly ofJournal of fungi (Basel, Switzerland) · 2025Article
- Methyltransferase Domain-Focused Genome Mining for Fungal Polyketide Synthases.Small methods · 2024Article
- Combinatorial biosynthesis for the engineering of novel fungal natural products.Communications chemistry · 2024Review
- Basidiomycete non-reducing polyketide synthases function independently of SAT domains.Fungal biology and biotechnology · 2023Article
- The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases.Chembiochem : a European journal of chemical biology · 2023Article
- Domain Truncation in Hispidin Synthase Orthologs from Non-Bioluminescent Fungi Does Not Lead to Hispidin Biosynthesis.International journal of molecular sciences · 2023Article
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Authors and funding
8 authors at 2 institutions in 1 country.
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Abstract
The nonreducing iterative type I polyketide synthases (NR-PKSs) CoPKS1 and CoPKS4 of the webcap mushroom Cortinarius odorifer share 88 % identical amino acids. CoPKS1 almost exclusively produces a tricyclic octaketide product, atrochrysone carboxylic acid, whereas CoPKS4 shows simultaneous hepta- and octaketide synthase activity and also produces the bicyclic heptaketide 6-hydroxymusizin. To identify the region(s) controlling chain length, four chimeric enzyme variants were constructed and assayed for activity in Aspergillus niger as heterologous expression platform. We provide evidence that the β-ketoacyl synthase (KS) domain determines chain length in these mushroom NR-PKSs, even though their KS domains differ in only ten amino acids. A unique proline-rich linker connecting the acyl carrier protein with the thioesterase domain varies most between these two enzymes but is not involved in chain length control.
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