Reprogramming Promiscuous Nonribosomal Peptide Synthetases for Production of Specific Peptides.
Journal
Organic letters
ISSN: 1523-7052
Titre abrégé: Org Lett
Pays: United States
ID NLM: 100890393
Informations de publication
Date de publication:
05 04 2019
05 04 2019
Historique:
pubmed:
13
3
2019
medline:
20
8
2019
entrez:
13
3
2019
Statut:
ppublish
Résumé
Pairs of docking domains (DDs) mediate the selective interations between adjacent nonribosomal peptide synthetases (NRPSs) to form defined protein-protein interactions resulting in defined peptide sequences. New specific rhabdopeptide/xenortide-like peptides (RXPs) were generated by swapping of either flexible or nonfunctional DD pairs between these monomodular RXP-NRPSs against DDs from collinear NRPSs. The results presented a promising means of engineering RXP-producing NRPSs to obtain desired peptides and further substantiated the decisive role of DDs in the NRP synthesis.
Identifiants
pubmed: 30859835
doi: 10.1021/acs.orglett.9b00395
doi:
Substances chimiques
Peptides
0
Peptide Synthases
EC 6.3.2.-
non-ribosomal peptide synthase
EC 6.3.2.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng