The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases
© 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH..
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.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2023 |
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Erschienen: |
2023 |
Enthalten in: |
Zur Gesamtaufnahme - volume:24 |
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Enthalten in: |
Chembiochem : a European journal of chemical biology - 24(2023), 3 vom: 01. Feb., Seite e202200649 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Löhr, Nikolai A [VerfasserIn] |
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Links: |
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Themen: |
79956-01-7 |
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Anmerkungen: |
Date Completed 03.02.2023 Date Revised 19.04.2023 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1002/cbic.202200649 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM350197857 |
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520 | |a 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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700 | 1 | |a Hüttel, Wolfgang |e verfasserin |4 aut | |
700 | 1 | |a Gressler, Markus |e verfasserin |4 aut | |
700 | 1 | |a Müller, Michael |e verfasserin |4 aut | |
700 | 1 | |a Hoffmeister, Dirk |e verfasserin |4 aut | |
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