Pyrroline Ring Assembly via N-Prenylation and Oxidative Carbocyclization during Biosynthesis of Aeruginosin Derivatives

Aeruginosins are linear peptide natural products isolated from cyanobacteria and contain various arginine derivatives at their termini. 1-Amino-2-(<i>N</i>-amidino-3-Δ3-pyrrolinyl)ethane (Aeap) is a structurally unique arginine derivative, as it has an unusual pyrroline ring with two additional carbon atoms of unknown biosynthetic origin. Here, we demonstrate that Aer3, a member of a newly identified subfamily of prenyltransferases, catalyzes selective isopentenylation of the internal N atom of agmatine. Rieske oxygenase AerC then catalyzes both carbocyclization and C-C bond cleavage to construct the pyrroline ring in Aeap. This pyrroline ring formation in Aeap biosynthesis, involving two novel enzymes, represents a unique route for heterocycle formation in nature.

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Publication Details

Journal
Journal of the American Chemical Society
Published
2025-03-13
DOI
https://doi.org/10.1021/jacs.5c01994
Citations
6
Primary Topic
Biochemical Acid Research Studies
Type
article
Field-Weighted Citation Impact
5.56

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article

Pyrroline Ring Assembly via N-Prenylation and Oxidative Carbocyclization during Biosynthesis of Aeruginosin Derivatives

Wenhe Zhang, Ikuro Abe, Richiro Ushimaru, Masahiro Kanaida
6 citations
Journal of the American Chemical Society
Biochemical Acid Research Studies
5.56
article

Pyrroline Ring Assembly via N-Prenylation and Oxidative Carbocyclization during Biosynthesis of Aeruginosin Derivatives

Wenhe Zhang, Ikuro Abe, Richiro Ushimaru, Masahiro Kanaida
article en
6 citations

Abstract

Aeruginosins are linear peptide natural products isolated from cyanobacteria and contain various arginine derivatives at their termini. 1-Amino-2-(<i>N</i>-amidino-3-Δ3-pyrrolinyl)ethane (Aeap) is a structurally unique arginine derivative, as it has an unusual pyrroline ring with two additional carbon atoms of unknown biosynthetic origin. Here, we demonstrate that Aer3, a member of a newly identified subfamily of prenyltransferases, catalyzes selective isopentenylation of the internal N atom of agmatine. Rieske oxygenase AerC then catalyzes both carbocyclization and C-C bond cleavage to construct the pyrroline ring in Aeap. This pyrroline ring formation in Aeap biosynthesis, involving two novel enzymes, represents a unique route for heterocycle formation in nature.

Journal of the American Chemical SocietyVol. 147(13)
Shenyang Pharmaceutical University (CN), Kyushu University (JP), The University of Tokyo (JP), Kumamoto University (JP)
Naito Foundation, Takeda Science Foundation, Asahi Glass Foundation, Institute for Fermentation, Osaka, Sumitomo Foundation, Japan Foundation for Applied Enzymology, Uehara Memorial Foundation, Japan Agency for Medical Research and Development, New Energy and Industrial Technology Development Organization, Yazaki Memorial Foundation for Science and Technology, Senri Life Science Foundation, Lotte Foundation, MSD Life Science Foundation, Public Interest Incorporated Foundation, Japan Society for the Promotion of Science, Japan Science and Technology Agency
Clean water and sanitation
Openalex Percentile: Top 5%
Biochemical Acid Research Studies
5.56
DOISourceOpenAlex
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