Role of Ser216 in the Mechanism of Action of Membrane-bound Lytic Transglycosylase B: Further Evidence for Substrate-assisted Catalysis

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Published by the Federation of European Biochemical Societies in FEBS Letters Volume 581, Issue 25, pages 4988-4992.

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FEBS Letters


Lytic transglycosylases cleave the β-(1 → 4)-glycosidic bond in the bacterial cell wall heteropolymer peptidoglycan between the N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues with the concomitant formation of a 1,6-anhydromuramoyl residue. Based on sequence alignments, Ser216 in Pseudomonas aeruginosa membrane-bound lytic transglycosylase B (MltB) was targeted for replacement with alanine to delineate its role in the enzyme’s mechanism of action.