Abstract 2288 Substrate promiscuity of the radical SAM RiPP maturase SbtM

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a widely distributed class of natural products. The RiPP biosynthetic enzyme SbtM is a member of the radical SAM S-adenosyl-L-methionine (SAM) superfamily of enzymes that perform radical-mediated transformations. SbtM modifies a (seleno)cysteine residue on the SbtMa peptide to install a thio(seleno)oxazole modification. In this poster we demonstrate using Cys-containing analogs at the site of modification that SbtM has a high tolerance for variations in the peptide substrate sequence.