Conformational adaptation of RTEM beta-lactamase to cefoxitin

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Cefoxitin, a semisynthetic cephamycin antibiotic: resistance to beta-lactamase inactivation.

Cefoxitin is a new, cephalosporin-like antibiotic which is highly resistant to hydrolysis by beta-lactamase. Ninety-one cultures were selected either for their general resistance to cephalosporin antibiotics or for their ability to produce beta-lactamase. Some of these cultures were resistant to cefoxitin. The capacity of each of the 91 strains to hydrolyze cefoxitin with beta-lactamase was det...

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beta-lactamase stability of HR 756, a novel cephalosporin, compared to that of cefuroxime and cefoxitin.

The stability to beta-lactamase hydrolysis of HR 756, a new cephalosporin antibiotic, was compared to the beta-lactamase stability of cefoxitin and cefuroxime. HR 756, cefoxitin, and cefuroxime were not hydrolyzed by Richmond type I, III, IV, and V beta-lactamases. Antibacterial activity of HR 756 correlated well with resistance to beta-lactamase hydrolysis except against Pseudomonas aeruginosa...

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Role of a cefoxitin-inducible beta-lactamase in a case of breakthrough bacteremia.

Development of resistance during therapy with cefamandole contributes to treatment failure. A simple cefoxitin disk test was recently described which detects a cefamandole-active inducible beta-lactamase not otherwise detectable with cefamandole as the inducer. A case of breakthrough Enterobacter bacteremia due to selection of a resistant subpopulation is reported in an immunocompromised patie...

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The comparative beta-lactamase resistance and inhibitory activity of 1-oxa cephalosporin, cefoxitin and cefotaxime.

The beta-lactamase stability and inhibitory activity of 1-oxa cephalosporin, (6R,7R)-7-[[carboxy(4-hydroxyphenyl)acetyl]amino]-7-methoxy-3-[[(1-methyl-1H-tetrazol-5-yl)thio]methyl]-8-oxo-5-oxa-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, was investigated and compared to that of cefoxitin and cefotaxime. There was no detectable beta-lactamase hydrolysis of 1-oxa cephalosporin, cefotaxime and ...

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Altering enzymatic activity: recruitment of carboxypeptidase activity into an RTEM beta-lactamase/penicillin-binding protein 5 chimera.

The D-Ala-D-Ala carboxypeptidases/transpeptidases (penicillin-binding proteins, PBPs) share considerable structural homology with class A beta-lactamases (EC 3.5.2.6), although these beta-lactamases have no observable D-Ala-D-Ala carboxypeptidase activity. With the objective of recruiting such activity into a beta-lactamase background, we have prepared a chimeric protein by inserting a 28-amino...

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ژورنال

عنوان ژورنال: European Journal of Biochemistry

سال: 1984

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1984.tb08468.x