1) ThuS catalyzes both S-glycosylation of the thiol of cysteine and O-glycosylation of the hydroxyl group of serine in peptide substrates in vitro. 2) ThuS catalyzed S-glycosylation is more efficient than O-glycosylation. 3) The biosynthesis of the putative products of the thuS gene cluster were reconstituted in vitro and the resulting S glycosylated peptides thurandacin A and thurandacin B and it exhibits highly selective antimicrobial activity towards B. thuringiensis.
Howard Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign , 600 South Mathews Avenue, Urbana, Illinois 61801, United States.
