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.
Wang, H., Oman, T. J., Zhang, R., Garcia De Gonzalo, C. V., Zhang, Q., & Van Der Donk, W. A.
Research groups
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.
Corresponding Author
Van Der Donk, W. A.
Contacts
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.
