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Aspartimide Modification in RiPP Natural Products.

Angela Zhu1, A James Link1,2,3,4,5

  • 1Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, United States.

Biochemistry
|March 6, 2026
PubMed
Summary
This summary is machine-generated.

Researchers explored the aspartimide modification in ribosomally synthesized and post-translationally modified peptides (RiPPs). A new RiPP class, imiditides, was discovered, expanding the understanding of this unique post-translational modification.

Keywords:
RiPPsaspartimidegraspetidelanthipeptidelasso peptide

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Peptide Chemistry

Background:

  • Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a diverse class of natural products.
  • An enigmatic functional group, the aspartimide, is found in multiple RiPP classes.
  • Enzymes related to protein isoaspartyl methyltransferase (PIMT) catalyze aspartimide formation.

Purpose of the Study:

  • To elucidate the biochemical details of aspartimidylation in known RiPP classes.
  • To discover and characterize novel RiPPs featuring aspartimide modification.
  • To identify knowledge gaps and suggest future research directions in RiPP modification.

Main Methods:

  • Biochemical characterization of aspartimidylation pathways.
  • Enzyme assays and kinetic studies.
  • Bioinformatic analysis and discovery of new RiPPs.

Main Results:

  • Detailed biochemical mechanisms of aspartimidylation were described for lanthipeptides, lasso peptides, and graspetides.
  • A novel class of RiPPs, termed imiditides (or type I pamtides), was discovered.
  • Aspartimide was identified as the defining post-translational modification for imiditides.

Conclusions:

  • RiPP-associated PIMTs exhibit distinct substrate specificity compared to canonical PIMTs.
  • The discovery of imiditides expands the known diversity of RiPPs and their modifications.
  • Further research is needed to fully understand the biological roles and catalytic mechanisms of aspartimidylating enzymes.