A ribosomally synthesised and post-translationally modified peptide containing a β-enamino acid and a macrocyclic motif

Shan Wang, Sixing Lin, Qing Fang, Roland Gyampoh, Zhou Lu, Yingli Gao, David J. Clarke, Kewen Wu, Laurent Trembleau, Yi Yu (), Kwaku Kyeremeh (), Bruce F. Milne (), Jioji Tabudravu () and Hai Deng ()
Additional contact information
Shan Wang: University of Aberdeen
Sixing Lin: Wuhan University
Qing Fang: University of Aberdeen
Roland Gyampoh: University of Ghana
Zhou Lu: University of Aberdeen
Yingli Gao: University of Aberdeen
David J. Clarke: University of Edinburgh
Kewen Wu: University of Aberdeen
Laurent Trembleau: University of Aberdeen
Yi Yu: Wuhan University
Kwaku Kyeremeh: University of Ghana
Bruce F. Milne: University of Aberdeen
Jioji Tabudravu: University of Central Lancashire
Hai Deng: University of Aberdeen

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract Ribosomally synthesized and post-translationally modified peptides (RiPPs) are structurally complex natural products with diverse bioactivities. Here we report discovery of a RiPP, kintamdin, for which the structure is determined through spectroscopy, spectrometry and genomic analysis to feature a bis-thioether macrocyclic ring and a β-enamino acid residue. Biosynthetic investigation demonstrated that its pathway relies on four dedicated proteins: phosphotransferase KinD, Lyase KinC, kinase homolog KinH and flavoprotein KinI, which share low homologues to enzymes known in other RiPP biosynthesis. During the posttranslational modifications, KinCD is responsible for the formation of the characteristic dehydroamino acid residues including the β-enamino acid residue, followed by oxidative decarboxylation on the C-terminal Cys and subsequent cyclization to provide the bis-thioether ring moiety mediated by coordinated action of KinH and KinI. Finally, conserved genomic investigation allows further identification of two kintamdin-like peptides among the kin-like BGCs, suggesting the occurrence of RiPPs from actinobacteria.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-022-32774-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32774-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-32774-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().