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.
Ottolenghi
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AC
Department of Medical Microbiology and Immunology, Ohio State University College of Medicine, Columbus 43210.
Caparrós
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M
de Pedro
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MA
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D001426:Bacterial Proteins; D002851:Chromatography, High Pressure Liquid; D016972:Enterobacter cloacae / Q000201:enzymology* / Q000648:ultrastructure; D004790:Enzyme Induction; D005998:Glycine / Q000378:metabolism; D007700:Kinetics; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism*; D001618:beta-Lactamases / Q000096:biosynthesis / Q000378:metabolism*
D000596:Amino Acids; D001426:Bacterial Proteins; D010457:Peptidoglycan; C048795:AmpC beta-lactamases; D001618:beta-Lactamases; D005998:Glycine