The Promiscuous Activity of the Radical SAM Enzyme NosL toward Two Unnatural Substrates

Main observation and conclusion The radical S‐adenosylmethionine (SAM) enzyme NosL catalyzes the conversion of L ‐tryptophan ( L ‐Trp, 1) to 3‐methyl‐2‐indolic acid (MIA, 2), a key intermediate in the biosynthesis of the peptide antibiotic nosiheptide. Previous study showed that this remarkable recombination reaction starts from the cleavage of the Cα—COO – bond to result in a •CO 2 − radical migration. In contrast to the radical SAM tyrosine...