Radical Propagation via σ-Cleavage Mediates Radical SAM Catalyzed Sulfur-for-Oxygen Swapping Reaction during the Biosynthesis of Albomycin δ₂.

ABSTRACT: AbmM is a radical S-adenosyl l-methionine (SAM) enzyme that catalyzes a radical initiated sulfur-for-oxygen swapping reaction, transforming the furanose ring of cytidine diphosphate (CDP) to a 4'-hydroxy-4'-thiofuranose product. While the function of AbmM has been demonstrated, the underlying mechanism regarding the formation of the radical intermediates during the reaction pathway remains to be fully established. To gain additional insight into this vital step in the biosynthesis of albomycin δ₂, 2'-deoxy-2'-methylidene CDP was synthesized as a mechanistic probe. Upon incubation with AbmM and dithionite, a C1' radical intermediate is generated from this mechanistic probe in the form of an allylic radical that can be trapped via oxidation to a sulfinate or a sulfenate ver

SUBMITTER: Zheng Z 

PROVIDER: S-EPMC12401566 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature