{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lohr NA"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["e202200649"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10108026"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(3)"],"pubmed_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."],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases."],"pmcid":["PMC10108026"],"funding_grant_id":["HO2515/8-1"],"pubmed_authors":["Eisen F","Muller M","Gressler M","Hoffmeister D","Lohr NA","Huttel W","Urban MC","Platz L"],"additional_accession":[]},"is_claimable":false,"name":"The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases.","description":"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.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2025-07-10T03:08:15.415Z","creation":"2025-04-06T11:22:11.583Z"},"accession":"S-EPMC10108026","cross_references":{"pubmed":["36507600"],"doi":["10.1002/cbic.202200649"]}}