Enzyme engineering lets us play with new building blocks in non-ribosomal peptide synthesis

Minuri S Ratnayake; Mathias H Hansen; Max J Cryle

doi:10.1016/j.str.2024.04.003

Enzyme engineering lets us play with new building blocks in non-ribosomal peptide synthesis

Structure. 2024 May 2;32(5):520-522. doi: 10.1016/j.str.2024.04.003.

Authors

Minuri S Ratnayake¹, Mathias H Hansen¹, Max J Cryle²

Affiliations

¹ The Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia; EMBL Australia, Monash University, Clayton, VIC 3800, Australia; ARC Centre of Excellence for Innovations in Peptide and Protein Science, Clayton, VIC 3800, Australia.
² The Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia; EMBL Australia, Monash University, Clayton, VIC 3800, Australia; ARC Centre of Excellence for Innovations in Peptide and Protein Science, Clayton, VIC 3800, Australia. Electronic address: max.cryle@monash.edu.

PMID: 38701750
DOI: 10.1016/j.str.2024.04.003

Abstract

In a recent issue of Nature Chemical Biology, Folger et al. demonstrated a high-throughput approach for engineering peptide bond forming domains from non-ribosomal peptide synthesis. A non-ribosomal peptide synthetase module from surfactin biosynthesis was reprogrammed to accept a fatty acid substrate into peptide biosynthesis, thus illustrating the potential of this approach for generating novel bioactive peptides.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Peptide Synthases* / chemistry
Peptide Synthases* / genetics
Peptide Synthases* / metabolism
Peptides / chemistry
Peptides / metabolism
Protein Engineering* / methods

Substances

Peptide Synthases
non-ribosomal peptide synthase
Peptides