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Formicamycin biosynthesis involves a unique reductive ring contraction.

Zhiwei Qin1, Rebecca Devine2, Thomas J Booth1

  • 1Department of Molecular Microbiology , John Innes Centre , Norwich Research Park , Norwich , NR4 7UH , UK .

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|October 9, 2020
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This summary is machine-generated.

Fasamycin is converted to formicamycins via a novel pathway involving ring expansion and contraction. Two specific genes, forX and forY, are essential for this transformation, revealing new insights into polyketide biosynthesis.

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Area of Science:

  • Biochemistry
  • Natural Product Biosynthesis
  • Molecular Biology

Background:

  • Fasamycins are biosynthetic precursors to formicamycins, both potent antibacterial polyketide natural products.
  • These compounds possess distinct three-dimensional structures despite their shared biosynthetic origin.

Purpose of the Study:

  • To elucidate the biochemical pathway and identify the gene products responsible for transforming fasamycins into formicamycins.
  • To investigate the enzymatic mechanisms underlying the structural modifications during this biosynthetic process.

Main Methods:

  • Gene deletion studies involving targeted disruption of forX and forY.
  • Analysis of accumulated metabolites using techniques such as mass spectrometry.
  • In vivo cross-feeding experiments and biomimetic semi-synthesis.

Main Results:

  • Deletion of forX (flavin-dependent monooxygenase) blocked formicamycin production, accumulating fasamycin E.
  • Deletion of forY (flavin-dependent oxidoreductase) also blocked production, yielding Baeyer-Villiger oxidation products (lactones).
  • ForX acts as a Baeyer-Villiger monooxygenase, dearomatizing ring C of fasamycins, while ForY catalyzes a reductive ring contraction of lactone intermediates.

Conclusions:

  • The transformation of fasamycins to formicamycins proceeds through a novel two-step pathway involving ring expansion-ring contraction.
  • ForX and ForY are identified as key enzymes, a Baeyer-Villiger monooxygenase and a reductive ring contraction enzyme, respectively.
  • This study reveals unique enzymatic mechanisms in polyketide natural product biosynthesis.