Penetration of moxalactam into its target proteins in Escherichia coli K-12: comparison of a highly moxalactam resistant mutant with its parent strain.
An eschericia coli K-12 mutant highly resistant to moxalactam but only slightly resistant to other beta-lactam antibiotics was obtained by mutagen treatment. The affinity of moxalactam for its target penicillin-binding proteins was unchanged, as was the level of beta-lactamase activity. The penetration of [14C] moxalactam, however, was markedly reduced in the mutant. Electrophoretic analysis revealed alterations of the outer membrane proteins. A reduction in the amount of one of the pore-forming proteins (porins) was especially noteworthy. These data suggest that moxalactam resistance is the result of an alteration in the outer membrane structure.
D001426:Bacterial Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002511:Cephalosporins / Q000378:metabolism*; D002513:Cephamycins / Q000378:metabolism*; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D009070:Moxalactam; D009154:Mutation; D011485:Protein Binding; D001618:beta-Lactamases / Q000378:metabolism
D001426:Bacterial Proteins; D002511:Cephalosporins; D002513:Cephamycins; D001618:beta-Lactamases; D009070:Moxalactam