Abstract
The radical S-adenosylmethionine (SAM) enzyme NosL catalyzes the conversion of l -tryptophan ( l -Trp) into 3-methyl-2-indolic acid (MIA) in the biosynthesis of the thiopeptide antibiotic nosiheptide, and this reaction is initiated by the 5′-deoxyadenosyl (dAdo)-radical-mediated hydrogen-atom abstraction from the l -Trp amino group. NosL also exhibits diverse promiscuous activities on various l -Trp analogues, and remarkably, the canonical dAdo-radical-mediated hydrogen abstraction can be switched to radical addition reactions by using a substrate analogue containing an olefin moiety. These findings highlight the intriguing chemistry and catalytic versatility of the radical SAM superfamily enzymes, offering a promising strategy to produce nucleoside-containing compounds, which could be of pharmaceutical interest.
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