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Polyether Cyclization Cascade Alterations in Response to Monensin Polyketide Synthase Mutations.

Sascha Heinrich1, Marius Grote1, Sonja Sievers2

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Summary

Researchers explored how enzymes process modified polyketide chains, revealing significant flexibility in post-polyketide synthases (PKS) during monensin biosynthesis. This flexibility allows for the creation of novel polyether structures from altered polyketide backbones.

Keywords:
biosynthesisconfiguration determinationmass spectrometrynatural productsprotein engineering

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Natural Product Biosynthesis

Background:

  • Targeted manipulation of polyketide synthases (PKS) generates novel polyketides.
  • The enzymatic processing of manipulated polyketide backbones by post-PKS enzymes is not well understood, especially for complex pathways like ionophore biosynthesis.

Purpose of the Study:

  • To investigate the substrate promiscuity of polyether cyclization cascade enzymes in monensin biosynthesis.
  • To understand how these enzymes process redox derivatives of the nascent polyketide chain.

Main Methods:

  • Liquid chromatography-high resolution mass spectrometry/mass spectrometry (LC-HRMS/MS^2) based studies.
  • Characterization of a novel monensin derivative using 2D-NMR spectroscopy, crystallography, and bioactivity assays.

Main Results:

  • Post-PKS enzymes demonstrated remarkable flexibility in processing derivatized polyketide backbones.
  • Enzymes acted on polyketide backbones with three different redox states across two modules.
  • An altered polyether structure was generated, and one derivative was successfully isolated and characterized.

Conclusions:

  • The post-PKS enzymes involved in monensin biosynthesis exhibit significant substrate promiscuity.
  • This flexibility enables the generation of novel polyether structures by acting on modified polyketide precursors.
  • The findings contribute to understanding polyketide biosynthesis and engineering new natural products.