Nonribosomal peptides (NRPs) have gained attention due to their diverse biological activities and potential applications in medicine and agriculture. The natural diversity of NRPs is a result of evolutionary processes that have occurred over millions of years. Recent studies have shed light on the mechanisms by which nonribosomal peptide synthetases (NRPSs) evolve, including gene duplication, recombination, and horizontal transfer. Mimicking natural evolution could be a useful strategy for engineering NRPSs to produce novel compounds with desired properties. Furthermore, the emergence of antibiotic-resistant bacteria has highlighted the urgent need for new drugs, and NRPs represent a promising avenue for drug discovery. This review discusses the engineering potential of NRPSs in light of their evolutionary history.
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Cover Image
Cover Image
The image shows two immune cells from a Xenopus embryo squeezing through dense tissue network and making extensive contacts with surrounding cells. At their leading fronts, they show a constriction, suggesting that these cells are encountering physical confinements as they migrate. In green/blue is Phalloidin staining for actin, in magenta is DAPI for nuclei. The small blue circles are yolk platelets, a characteristic trait of Xenopus cells. For further information, see the review in this issue by Le and Mayor, pages 1731–1243. Image provided by Hoang Anh Le.
Biomimetic engineering of nonribosomal peptide synthesis
Kexin Zhang, Hajo Kries; Biomimetic engineering of nonribosomal peptide synthesis. Biochem Soc Trans 31 August 2023; 51 (4): 1521–1532. doi: https://doi.org/10.1042/BST20221264
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