記述言語：英語  

DOI： 10.1093/jimb/kuaf024

PubMed

出版者・発行元：Nature Catalysis  

Carbon–sulfur bond-forming reactions in natural product biosynthesis largely involve Lewis acid/base chemistry with relatively few examples catalysed by radical S-adenosyl-l-methionine (SAM) enzymes. The latter have been limited to radical-mediated sulfur insertion into carbon–hydrogen bonds with the sulfur atom originating from a sacrificial auxiliary iron–sulfur cluster. Here we show that the radical SAM enzyme AbmM encoded in the albomycin biosynthetic gene cluster catalyses a sulfur-for-oxygen swapping reaction, transforming the furanose ring of cytidine 5′-diphosphate to a thiofuranose moiety that is essential for the antibacterial activity of albomycin δ<inf>2</inf>. Thus, in addition to its canonical function of mediating the reductive cleavage of SAM, the radical SAM catalytic cluster of AbmM appears to play a role in providing the sulfur introduced during the AbmM-catalysed reaction. These discoveries not only establish the origin of the thiofuranose core in albomycin δ<inf>2</inf> but, more importantly, also emphasize the functional diversity of radical SAM catalysis. (Figure presented.)

DOI： 10.1038/s41929-025-01367-w

Web of Science

Scopus

記述言語：英語   出版者・発行元：Chemical Society Reviews  

Nitrogen-centered radicals have emerged as versatile intermediates in natural product biosynthesis, playing pivotal roles in complex bond-forming and rearrangement reactions—including fragmentations, cyclizations, and dimerizations. These transformations enable the efficient construction of structurally intricate alkaloids, amino acids, cofactors, and other scaffolds that are often inaccessible via classical polar mechanisms. This review provides an overview of the enzymatic systems discovered and characterized over the past decade that harness nitrogen-centered radicals to mediate diverse biological transformations. Emphasis is placed on the enzymatic strategies for generating and precisely controlling these reactive species, with detailed discussions of their underlying mechanisms. These insights underscore the expanding role of nitrogen radical chemistry in biology and highlight its potential in the development of new biocatalytic platforms for synthetically challenging transformations.

DOI： 10.1039/d5cs00342c

Web of Science

Scopus

PubMed

記述言語：英語   出版者・発行元：Journal of the American Chemical Society  

Aeruginosins are linear peptide natural products isolated from cyanobacteria and contain various arginine derivatives at their termini. 1-Amino-2-(N-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.

DOI： 10.1021/jacs.5c01994

Web of Science

Scopus

PubMed

記述言語：英語   出版者・発行元：Nature Publishing Group  

記述言語：日本語  

記述言語：日本語  

記述言語：日本語  

記述言語：日本語   出版者・発行元：(公財)鈴木謙三記念医科学応用研究財団  

記述言語：日本語   出版者・発行元：(一社)日本生薬学会