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Mapping the nonribosomal specificity code through promiscuity-guided A-domain engineering.

Aleksa Stanišić1, Carl-Magnus Svensson2, Maximilian Müll1,3

  • 1Biosynthetic Design of Natural Products, Leibniz Institute for Natural Product Research and Infection Biology - Hans-Knöll-Institute (HKI) Beutenbergstraße 11a 07745 Jena Germany.

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

Researchers engineered nonribosomal peptide synthetases (NRPSs) by exploring multispecificity in adenylation domains. This work provides a roadmap for designing novel bioactive peptides through NRPS engineering.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Nonribosomal peptide synthetases (NRPSs) are crucial for assembling diverse bioactive peptides.
  • Predicting NRPS products is possible, but designing specific NRPSs remains challenging due to unknown multispecificity.

Purpose of the Study:

  • To investigate and engineer the specificity of nonribosomal peptide synthetase adenylation domains.
  • To understand the role of multispecificity in NRPS evolution and design.

Main Methods:

  • Utilized a hydroxamate assay (HAMA) to assess multispecificity in mutant libraries of the SrfAC adenylation domain.
  • Employed full randomization of 15 active site residues and computational modeling to analyze specificity divergence.

Main Results:

  • Identified specific mutations with significant impact on NRPS specificity, demonstrating remarkable evolvability.
  • Statistical analysis revealed three key sequence positions influencing specificity, offering a guide for NRPS engineering.
  • Developed a multispecific SrfAC version, showcasing functional flexibility.

Conclusions:

  • Promiscuity in adenylation domains drives neofunctionalization, a process that can be mimicked for laboratory design of valuable peptides.
  • The findings provide a roadmap for engineering NRPS specificity and designing novel peptide therapeutics or industrial compounds.