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Dissecting Bottromycin Biosynthesis Using Comparative Untargeted Metabolomics.

William J K Crone1, Natalia M Vior2, Javier Santos-Aberturas2

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.

Angewandte Chemie (International Ed. in English)
|July 5, 2016
PubMed
Summary

Researchers elucidated the biosynthesis of bottromycin A2, a unique antibacterial peptide. Key enzymes, including a YcaO domain protein, were identified, revealing the mechanism for its unprecedented macrocyclization.

Keywords:
biosynthesisbottromycinmass spectrometrynatural productspeptides

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Product Biosynthesis

Background:

  • Bottromycin A2 is a ribosomally synthesized and post-translationally modified peptide (RiPP) with potent activity against multidrug-resistant bacteria.
  • Its unique structure features a macrocyclic amidine and beta-methylated amino acids, but its biosynthetic pathway was largely unknown.

Purpose of the Study:

  • To elucidate the key enzymatic transformations in the bottromycin A2 biosynthetic pathway.
  • To identify the enzymes responsible for the unprecedented macrocyclization step.

Main Methods:

  • Utilized an untargeted metabolomic approach combined with mass spectral networking.
  • Analyzed the metabolomes of various bottromycin biosynthetic pathway mutants.

Main Results:

  • Identified the functions of previously uncharacterized biosynthetic enzymes within the btm gene cluster.
  • Determined that a YcaO domain protein and its partner protein collaborate to catalyze the macrocyclization of bottromycin A2.

Conclusions:

  • The study provides a detailed understanding of the bottromycin A2 biosynthetic pathway.
  • The identified enzymes, particularly the YcaO-partner complex, are crucial for the formation of this unique antibacterial compound.