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A distributive peptide cyclase processes multiple microviridin core peptides within a single polypeptide substrate.

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This study reveals a novel mechanism in ribosomally synthesized and post-translationally modified peptides (RiPPs) biosynthesis where one enzyme processes multiple core peptides. This finding opens avenues for modular production using synthetic biology.

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Area of Science:

  • Biochemistry
  • Natural Products Chemistry
  • Synthetic Biology

Background:

  • Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a diverse class of natural products.
  • RiPP biosynthesis typically involves a leader peptide guiding modifications of a single core peptide.

Purpose of the Study:

  • To investigate the biochemical processing of multiple core peptides within a single precursor peptide in RiPP biosynthesis.
  • To characterize the enzyme AMdnC from a cyanobacterial microviridin pathway responsible for macrolactone installation.

Main Methods:

  • Biochemical assays to study enzyme catalysis and substrate processing.
  • Kinetic studies to determine enzyme properties.
  • Analysis of the microviridin pathway in cyanobacteria.

Main Results:

  • The ATP-grasp ligase AMdnC installs up to two macrolactones on each of the three core peptides within the precursor AMdnA.
  • AMdnC exhibits distributive catalysis with unstrict N-to-C overall directionality but strict order for macrolactonizing each core peptide.
  • AMdnC demonstrates catalytic versatility, processing unnatural substrates with one to four core peptides.

Conclusions:

  • The study reveals a distinct biosynthetic logic for RiPPs involving multiple core peptide processing.
  • Findings suggest potential for modular production of RiPPs through synthetic biology approaches.