Enzymatic studies on the mechanism of action of cefoxitin. Correlation between the affinities of cefoxitin to penicillin-binding proteins and its rates of inhibition of the respective penicillin-sensitive reactions in E. coli.
The affinities of cefoxitin, a cephamycin antibiotic, to penicillin-binding proteins of Escherichia coli were reexamined using a recently developed method for separating penicillin-binding proteins. The inhibitions by this antibiotic of four measurable penicillin-sensitive enzymatic reactions, the reactions of D-alanine carboxypeptidases IA and IB, cross-bridge formation and concomitant release of D-alanine, were also measured. An approximate correlation was found between the affinities of cefoxitin to the penicillin-binding proteins responsible for these reactions and its rates of inhibition of the respective penicillin-sensitive reactions.
D001426:Bacterial Proteins / Q000378:metabolism*; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000378:metabolism*; D002440:Cefoxitin / Q000378:metabolism / Q000494:pharmacology*; D002511:Cephalosporins / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects* / Q000378:metabolism; D010400:Penicillin G / Q000378:metabolism; D010406:Penicillins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011485:Protein Binding
D001426:Bacterial Proteins; D002352:Carrier Proteins; D002511:Cephalosporins; D010406:Penicillins; D002440:Cefoxitin; D010400:Penicillin G