title: 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).
authors: John A
authors: JA
authors: McIntosh
authors: Zhenjian
authors: Z
authors: Lin
authors: Ma Diarey B
authors: MD
authors: Tianero
authors: Eric W
authors: EW
authors: Schmidt
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D002070:Butadienes / Q000737:chemistry*; D000458:Cyanobacteria / Q000378:metabolism*; D045782:Hemiterpenes / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010420:Pentanes / Q000737:chemistry*; D019151:Peptide Library; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000302:isolation & purification; D054876:Prenylation
chemical_list: D001426:Bacterial Proteins; D002070:Butadienes; D045782:Hemiterpenes; D010420:Pentanes; D019151:Peptide Library; D010456:Peptides, Cyclic; C005059:isoprene