Unknown

Dataset Information

0

Aestuaramides, a natural library of cyanobactin cyclic peptides resulting from isoprene-derived Claisen rearrangements.


ABSTRACT: We report 12 cyanobactin cyclic peptides, the aestuaramides, from the cultivated cyanobacterium Lyngbya aestuarii. We show that aestuaramides are synthesized enzymatically as reverse O-prenylated tyrosine ethers that subsequently undergo a Claisen rearrangement to produce forward C-prenylated tyrosine. These results reveal that a nonenzymatic Claisen rearrangement dictates isoprene regiochemistry in a natural system. They also reveal one of the mechanisms that organisms use to generate structurally diverse compound libraries starting from simple ribosomal peptide pathways (RiPPs).

SUBMITTER: McIntosh JA 

PROVIDER: S-EPMC3657307 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Aestuaramides, a natural library of cyanobactin cyclic peptides resulting from isoprene-derived Claisen rearrangements.

McIntosh John A JA   Lin Zhenjian Z   Tianero Ma Diarey B MD   Schmidt Eric W EW  

ACS chemical biology 20130222 5


We report 12 cyanobactin cyclic peptides, the aestuaramides, from the cultivated cyanobacterium Lyngbya aestuarii. We show that aestuaramides are synthesized enzymatically as reverse O-prenylated tyrosine ethers that subsequently undergo a Claisen rearrangement to produce forward C-prenylated tyrosine. These results reveal that a nonenzymatic Claisen rearrangement dictates isoprene regiochemistry in a natural system. They also reveal one of the mechanisms that organisms use to generate structura  ...[more]

Similar Datasets

| S-EPMC8286818 | biostudies-literature
| S-EPMC4356197 | biostudies-literature
| S-EPMC4482617 | biostudies-literature
| S-EPMC2547484 | biostudies-literature
| S-EPMC5764894 | biostudies-literature
2023-06-01 | GSE202764 | GEO
| S-EPMC3119926 | biostudies-literature