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Interaction of Cefpirome and a Cephalosporinase from Citrobacter Freundii GN7391

Overview
Journal Antimicrob Agents Chemother
Publisher American Society for Microbiology
Specialty Pharmacology
Date 1989 Mar 1
PMID 2658787
Citations 4
Authors
S Satake
M Hiraoka
S Mitsuhashi
Affiliations
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Abstract

The interaction of cefpirome and a cephalosporinase from Citrobacter freundii, including hydrolysis and inhibition, was studied in comparison with those of cefotiam, cefotaxime, and ceftazidime. Cefpirome was hydrolyzed by the enzyme more rapidly at Vmax than were cefotaxime and ceftazidime. However, the low affinity of the enzyme for cefpirome caused a reduction in the hydrolytic rate of cefpirome at a low drug concentration (0.1 microM). The high stability of cefpirome at a low concentration explains the high antimicrobial activity of the agent against cephalosporinase-producing bacteria.

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PMID: 8655212 DOI: 10.1007/BF01713572.

A functional classification scheme for beta-lactamases and its correlation with molecular structure.

Bush K, Jacoby G, Medeiros A Antimicrob Agents Chemother. 1995; 39(6):1211-33.

PMID: 7574506 PMC: 162717. DOI: 10.1128/AAC.39.6.1211.

Interaction of E1040 with cephalosporinase from Citrobacter freundii GN7391.

Inoue E, Mitsuhashi S Antimicrob Agents Chemother. 1989; 33(12):2157-9.

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Effects of beta-lactamases and omp mutation on susceptibility to beta-lactam antibiotics in Escherichia coli.

Hiraoka M, Okamoto R, Inoue M, Mitsuhashi S Antimicrob Agents Chemother. 1989; 33(3):382-6.

PMID: 2658786 PMC: 171497. DOI: 10.1128/AAC.33.3.382.

References
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