Cefoxitin: Difference between revisions
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<StructureSection load='' size='340' side='right' caption='Caption for this structure' scene='10/1040131/Cv/1'> | <StructureSection load='' size='340' side='right' caption='Caption for this structure' scene='10/1040131/Cv/1'> | ||
Cefoxitin is a second-generation cephamycin antibiotic developed by Merck & Co., Inc. from Cephamycin C in the year following its discovery, 1972. See also [https://en.wikipedia.org/wiki/Cefoxitin Cefoxitin]. | Cefoxitin is a second-generation [[cephamycin]] antibiotic developed by Merck & Co., Inc. from Cephamycin C in the year following its discovery, 1972. See also [https://en.wikipedia.org/wiki/Cefoxitin Cefoxitin]. | ||
Cefoxitin is a beta-lactam antibiotic which binds to penicillin binding proteins, or transpeptidases. By binding to PBPs, cefoxitin prevents the PBPs from forming the cross-linkages between the peptidoglycan layers that make up the bacterial cell wall, thereby interfering with cell wall synthesis. It is a strong beta-lactamase inducer, as are certain other antibiotics (such as imipenem). However, cefoxitin is a better substrate than imipenem for beta-lactamases.<ref name="a10">PMID:8477758</ref> | Cefoxitin is a beta-lactam antibiotic which binds to penicillin binding proteins, or transpeptidases. By binding to PBPs, cefoxitin prevents the PBPs from forming the cross-linkages between the peptidoglycan layers that make up the bacterial cell wall, thereby interfering with cell wall synthesis. It is a strong beta-lactamase inducer, as are certain other antibiotics (such as imipenem). However, cefoxitin is a better substrate than imipenem for beta-lactamases.<ref name="a10">PMID:8477758</ref> | ||
Latest revision as of 09:35, 9 April 2024
Cefoxitin is a second-generation cephamycin antibiotic developed by Merck & Co., Inc. from Cephamycin C in the year following its discovery, 1972. See also Cefoxitin. Cefoxitin is a beta-lactam antibiotic which binds to penicillin binding proteins, or transpeptidases. By binding to PBPs, cefoxitin prevents the PBPs from forming the cross-linkages between the peptidoglycan layers that make up the bacterial cell wall, thereby interfering with cell wall synthesis. It is a strong beta-lactamase inducer, as are certain other antibiotics (such as imipenem). However, cefoxitin is a better substrate than imipenem for beta-lactamases.[1] (7kcx). . |
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ReferencesReferences
- ↑ Phillips I, Shannon K. Importance of beta-lactamase induction. Eur J Clin Microbiol Infect Dis. 1993;12 Suppl 1:S19-26. PMID:8477758 doi:10.1007/BF02389873