Annabell Linck

TL;DR: This work reports a new strategy for the modification of NRPSs that uses defined exchange units (XUs) and not modules as functional units and presents the use of internal condensation domains as an alternative to other peptide-chain-releasing domains for the production of cyclic peptides.

TL;DR: A new fusion point inside the condensation domains of NRPSs is described that results in the development of the exchange unit condensation domain (XUC) concept, which enables the efficient production of peptides, even containing non-natural amino acids, in yields up to 280 mg l−1.

TL;DR: NRPminer as discussed by the authors is a modification-tolerant tool for NRP discovery from large (meta)genomic and mass spectrometry datasets, which is able to identify many NRPs from different environments.

TL;DR: The data suggest that overexpression of transaldolase is a more promising strategy than reduction in GAPDH activity to increase the flux through the nonoxidative pentose phosphate pathway.

TL;DR: A new mechanism of natural product biosynthetic variation whereby mRNA may code for shorter NRPS enzymes in addition to full-length proteins, resulting in the production of smaller peptide derivatives is supported.