Correlation Between Hydrolysis of the β-Lactam Bond of the Cephalosporin Nucleus and Expulsion of the 3-Substituent

Author:

O'Callaghan Cynthia H.1,Kirby Susan M.1,Morris A.1,Waller R. E.1,Duncombe R. E.1

Affiliation:

1. Glaxo Research Ltd., and Glaxo Laboratories Ltd., Greenford, Middlesex, England

Abstract

The hydrolysis of two cephalosporins by three different β-lactamases has been studied. Each enzyme caused a decrease in ultraviolet absorption, a loss of biological activity, and the release of the leaving group from the 3-position. The changes occurred at the same rate and to the same extent with each enzyme, and it is inferred that the loss of the leaving group is a consequence of, and not a prerequisite for, hydrolysis of the β-lactam ring.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference6 articles.

1. Products of aminolysis and enzymic hydrolysis of the cephalosporins;Hamilton-Miller J. M. T.;Biochem. J.,1970

2. A comparative study of eight distinct ,I-lactamases synthesised by gram-negative bacteria;Jack G. W.;J. Gen. Microbiol.,1970

3. Inhibition of f3-lactamase decomposition of cephaloridine and cephalothin by other cephalosporins;O'Callaghan C. H.;Antimicrob. Ag. Chemother.,1967

4. Effects of ,8-lactamase from gram-negative organisms on cephalosporins and penicillins;O'Callaghan C. H.;Antimicrob. Ag. Chemother.,1968

5. Novel method of detection of ,B-lactamases using a chromogenic cephalosporin substrate;O'Callaghan C. H.;Antimicrob. Ag. Chemother.,1972

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