Peptidoglycan is a polysaccharide made of two glucose derivatives, N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM), alternated in long chains. The chains are cross-linked to one another by a tetrapeptide that extends off the NAM sugar unit, allowing a lattice-like structure to form. The four amino acids that compose the tetrapeptide are: L-alanine, D-glutamine, L-lysine or meso-diaminopimelic acid (DPA), and D-alanine. Typically only the L-isomeric form of amino acids are utilized by cells but the use of the mirror image D-amino acids provides protection from proteases that might compromise the integrity of the cell wall by attacking the peptidoglycan. The tetrapeptides can be directly cross-linked to one another, with the D-alanine on one tetrapeptide binding to the L-lysine/ DPA on another tetrapeptide. In many gram positive bacteria there is a cross-bridge of five amino acids such as glycine (peptide interbridge) that serves to connect one tetrapeptide to another. In either case the cross-linking serves to increase the strength of the overall structure, with more strength derived from complete cross-linking, where every tetrapeptide is bound in some way to a tetrapeptide on another NAG-NAM chain.
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The mechanism of glycine action in growth inhibition was studied on eight different species of bacteria of various genera representing the four most common peptidoglycan types.