Abstract
An inducible cephalosporinase was purified from Pseudomonas maltophilia GN12873. The pI was 8.4, and the molecular weight was ca. 56,000 by gel filtration or 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting that this enzyme had two subunits. The optimal pH and optimal temperature were 7.5 and 45 degrees C, respectively. Enzyme activity was inhibited by clavulanic acid, sulbactam, cephamycin derivatives, carbapenem antibiotics, iodine, HgCl2, and p-chloromercuribenzoate. The enzyme showed a broad substrate profile, hydrolyzing cephaloridine, cefazolin, cefsulodin, penicillin G, ceftizoxime, and ampicillin at a high rate.
MeSH Terms
Anti-Bacterial Agents/pharmacology
Bacterial Proteins/isolation & purification
Cephalosporinase/isolation & purification,metabolism
Chemical Phenomena
Chemistry, Physical
Chromatography, Gel
Enzyme Induction/drug effects
Hydrogen-Ion Concentration
Pseudomonas/enzymology
beta-Lactamase Inhibitors
beta-Lactamases/metabolism
Chemicals
Anti-Bacterial Agents
Bacterial Proteins
beta-Lactamase Inhibitors
Cephalosporinase
beta-Lactamases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Saino Y
Inoue M
Mitsuhashi S
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18 references, click to expand
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