The cell wall, consisting of the crosslinked peptidoglycan (PG), is critical for bacterial viability. Over 50% of the PG is turned over during bacterial growth and division, and its constituents are recycled. The cell wall is broken down in the periplasm by the action of lytic transglycosylases, the reaction products of which are internalized by the permease AmpG. Once in the cytoplasm, the metabolites are processed sequentially by a series of six enzymes to generate a key metabolite on its way to de novo biosynthesis of the peptidoglycan. This work describes the preparations of AmpD, NagZ, AnmK, MupP, AmgK and MurU from Pseudomonas aeruginosa (PAO1). Mass spectrometric assays for each of these enzymes were developed to document the sequential events as a set up to define the metabolic flux for the recycling process. Furthermore, these enzymes would appear to interact with each other in complexes, as defined by surface-plasmon resonance. We will describe these efforts in defining the cytoplasmic events of bacterial cell-wall recycling.

Reconstitution of cytoplasmic events of cell-wall recycling from Pseudomonas aeruginosa

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ACS Fall 2022

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