Peptidoglycan tripeptide content and cross-linking are altered in Enterobacter cloacae induced to produce AmpC beta-lactamase by glycine and D-amino acids.

Induction of AmpC beta-lactamase in Enterobacter cloacae ATCC 13047 by D-methionine, glycine, or D-tryptophan was accompanied by alterations in peptidoglycan composition and structure; in the case of D-methionine, it was also accompanied by morphologic changes. A decrease in peptidoglycan tripeptides was seen. With glycine, there was an increase in the proportion of diaminopimelic-diaminopimelic cross-links. The possible implications of these changes for beta-lactamase induction are discussed.