Biosynthesis and engineering of the nonribosomal peptides with a C-terminal putrescine.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
19 10 2023
19 10 2023
Historique:
received:
05
01
2023
accepted:
09
10
2023
medline:
23
10
2023
pubmed:
20
10
2023
entrez:
19
10
2023
Statut:
epublish
Résumé
The broad bioactivities of nonribosomal peptides rely on increasing structural diversity. Genome mining of the Burkholderiales strain Schlegelella brevitalea DSM 7029 leads to the identification of a class of dodecapeptides, glidonins, that feature diverse N-terminal modifications and a uniform putrescine moiety at the C-terminus. The N-terminal diversity originates from the wide substrate selectivity of the initiation module. The C-terminal putrescine moiety is introduced by the unusual termination module 13, the condensation domain directly catalyzes the assembly of putrescine into the peptidyl backbone, and other domains are essential for stabilizing the protein structure. Swapping of this module to another two nonribosomal peptide synthetases leads to the addition of a putrescine to the C-terminus of related nonribosomal peptides, improving their hydrophilicity and bioactivity. This study elucidates the mechanism for putrescine addition and provides further insights to generate diverse and improved nonribosomal peptides by introducing a C-terminal putrescine.
Identifiants
pubmed: 37857663
doi: 10.1038/s41467-023-42387-z
pii: 10.1038/s41467-023-42387-z
pmc: PMC10587159
doi:
Substances chimiques
Putrescine
V10TVZ52E4
Peptides
0
Peptide Synthases
EC 6.3.2.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6619Informations de copyright
© 2023. Springer Nature Limited.
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