{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Folger IB"],"funding":["ETH Zürich","Swiss National Science Foundation","Gouvernement du Canada | Canadian Institutes of Health Research","Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada)"],"pagination":["761-769"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11142918"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(6)"],"pubmed_abstract":["Engineered biosynthetic assembly lines could revolutionize the sustainable production of bioactive natural product analogs. Although yeast display is a proven, powerful tool for altering the substrate specificity of gatekeeper adenylation domains in nonribosomal peptide synthetases (NRPSs), comparable strategies for other components of these megaenzymes have not been described. Here we report a high-throughput approach for engineering condensation (C) domains responsible for peptide elongation. We show that a 120-kDa NRPS module, displayed in functional form on yeast, can productively interact with an upstream module, provided in solution, to produce amide products tethered to the yeast surface. Using this system to screen a large C-domain library, we reprogrammed a surfactin synthetase mo"],"journal":["Nature chemical biology"],"pubmed_title":["High-throughput reprogramming of an NRPS condensation domain."],"pmcid":["PMC11142918"],"funding_grant_id":["PJT-178084"],"pubmed_authors":["Folger IB","Frota NF","Pistofidis A","Niquille DL","Hansen DA","Hilvert D","Schmeing TM"],"additional_accession":[]},"is_claimable":false,"name":"High-throughput reprogramming of an NRPS condensation domain.","description":"Engineered biosynthetic assembly lines could revolutionize the sustainable production of bioactive natural product analogs. Although yeast display is a proven, powerful tool for altering the substrate specificity of gatekeeper adenylation domains in nonribosomal peptide synthetases (NRPSs), comparable strategies for other components of these megaenzymes have not been described. Here we report a high-throughput approach for engineering condensation (C) domains responsible for peptide elongation. We show that a 120-kDa NRPS module, displayed in functional form on yeast, can productively interact with an upstream module, provided in solution, to produce amide products tethered to the yeast surface. Using this system to screen a large C-domain library, we reprogrammed a surfactin synthetase mo","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-04-29T14:12:28.351Z","creation":"2026-04-14T03:06:55.67Z"},"accession":"S-EPMC11142918","cross_references":{"pubmed":["38308044"],"doi":["10.1038/s41589-023-01532-x"]}}