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A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.

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Researchers elucidated daptide biosynthesis, a unique peptide modification. They discovered enzymes that enable engineering new C-termini for peptides and proteins, expanding synthetic biology applications.

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Enzymology

Background:

  • Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a diverse class of natural products.
  • Daptides, a subclass of RiPPs, are characterized by a C-terminal amine instead of a carboxylic acid.
  • The biosynthetic pathways and engineering potential of daptides are not fully understood.

Purpose of the Study:

  • To establish the diversity, enzymatic requirements, and engineering potential of daptide biosynthesis.
  • To reconstitute and characterize the key enzymatic steps in daptide formation.
  • To explore the substrate tolerance and engineering capabilities of the daptide biosynthetic machinery.

Main Methods:

  • Reconstitution of daptide biosynthesis in vitro using gene clusters from Thermobifida fusca and Streptomyces azureus.
  • In vitro and in vivo characterization of YcaO enzymes in converting amine intermediates to C-terminal imidazolines.
  • Demonstration of enzymatic activity on modified and non-native peptide substrates.

Main Results:

  • The study identified sequential enzymatic requirements for daptide biosynthesis: oxidative decarboxylation, transamination, and N,N-dimethylation.
  • A family of YcaO enzymes was shown to catalyze the final conversion of a secondary amine to a C-terminal imidazoline.
  • The daptide pathway enzymes exhibited broad substrate tolerance, accepting shortened, leader peptide-free, and non-native core peptides.
  • Engineered daptide pathways successfully installed novel C-termini, including an aminoacetone moiety, onto various peptide and protein substrates.

Conclusions:

  • The enzymatic machinery for daptide biosynthesis has been elucidated, revealing key steps and enzyme families involved.
  • The broad substrate tolerance of daptide pathway enzymes offers significant potential for synthetic biology applications.
  • This work enables the engineering of novel peptide and protein C-termini for applications such as bioconjugation.