The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases

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.

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch

Erschienen in
The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases ; day:28 ; month:12 ; year:2022 ; extent:8
ChemBioChem ; (28.12.2022) (gesamt 8)

Urheber
Löhr, Nikolai A.
Urban, Maximilian C.
Eisen, Frederic
Platz, Lukas
Hüttel, Wolfgang
Greßler, Markus
Müller, Michael
Hoffmeister, Dirk

DOI
10.1002/cbic.202200649
URN
urn:nbn:de:101:1-2022122914053188475873
Rechteinformation
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Letzte Aktualisierung
15.08.2025, 07:26 MESZ

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