PMID: 6976340Nov 1, 1981Paper

Properties of cephalosporinase from Proteus morganii

The Journal of Antibiotics
M TodaS Mitsuhashi

Abstract

The cephalosporin beta-lactamase (cephalosporinase) was purified from a strain of Proteus morganii which showed resistance to cephalosporins. The optimal pH was about 8.5, and the optimal temperature was 40 degrees C. The isoelectric point was 8.7 and the molecular weight was estimated to be about 41,000 from sodium dodecyl sulfate-acrylamide gel electrophoresis. The enzyme activity was inhibited by cloxacillin, ampicillin, carbenicillin, cefuroxime, cefotaxime, ceftizoxime (FK749), cefmenoxime (SCE-1365), cefoxitin, cefmetazole, YM09330 and moxalactam (6059-S), but not by clavulanic acid or CP-45899. The beta-lactamase also hydrolyzed cephaloridine, cefazolin, cephalothin, cephalexin, cefotiam, cefamandole and benzylpenicillin. These results suggest the possibility that the properties of beta-lactamases may be characterized by measuring the kinetic parameters of the enzyme toward newly-introduced beta-lactam antibiotics and beta-lactamase inhibitors.

Citations

Jan 1, 1985·Biotechnology & Genetic Engineering Reviews·A Coulson
Feb 24, 2006·Antimicrobial Agents and Chemotherapy·Pablo PowerGabriel Gutkind
Aug 4, 1998·Antimicrobial Agents and Chemotherapy·F TessierC Quentin
Sep 1, 1988·Antimicrobial Agents and Chemotherapy·A TamuraS Mitsuhashi
Aug 1, 1982·Antimicrobial Agents and Chemotherapy·K KatsuS Mitsuhashi
Jun 1, 1995·Antimicrobial Agents and Chemotherapy·K BushA A Medeiros
Jul 1, 1987·Antimicrobial Agents and Chemotherapy·Y UtsuiS Mitsuhashi

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