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Certain D-amino acids such as D-methionine are directly incorporated into peptidoglycan of Escherichia coli, where they inhibit the binding of lipoprotein to the peptidoglycan.1* This second binding reaction may \>e important in the normal proliferation of E. coli; its inhibition by D-amino acids may enhance the bacteriolytic activities of most /Mactam compounds (penicillins, cephalosporins, and others; ref. 2, and T. Tsuruoka et al., in preparation), a synergistic phenomenon first observed by Lark and Lark.3) Lark, Bradley, and Lark4) observed the incorporation of D-methionine into the cell wall of Alkaligenes, a Gram-negative bacterium, and found that the incorporated amino acid had both the amino and carboxyl groups substituted. The mode of its binding to peptidoglycan was not known. Izaki, Matsuhashi, and Strominger, based on their enzymatic study of the biosynthesis of peptidoglycan,5}

Binding of D-methionine to peptidoglycan in the presence of inhibitors of cell wall synthesis in Escherichia coli.