PMID: 6978132Oct 1, 1981Paper

Interactions between non-classical beta-lactam compounds and the beta-lactamases of Actinomadura R39 and Streptomyces albus G

The Biochemical Journal
J A KellyJ M Ghuysen

Abstract

6-Aminopenicillanic acid, 7-aminocephalosporanic acid, mecillinam and quinacillin have varying substrate activities for both the R39 beta-lactamase (excreted by Actinomadura R39) and the G beta-lactamase (excreted by Streptomyces albus G). Cefoxitin and quinacillin sulphone are not recognized by the G beta-lactamase and are weak inactivators of the R39 beta-lactamase. N-Formimidoylthienamycin is a poor substrate for the G beta-lactamase and a potent inactivator of the R39 beta-lactamase. The high value of the bimolecular rate constant for enzyme inactivation is mainly due to a very low dissociation constant (1 microM). Clavulanate is an inactivator of both G and R39 beta-lactamases. The reaction with this latter enzyme is a branched pathway where normal turnover and permanent enzyme inactivation occur concomitantly. Between 28 and 43 molecules of clavulanate are hydrolysed before one of them has the opportunity to inactivate one molecule of enzyme.

Citations

Jan 1, 1985·Journal of Enzyme Inhibition·M V Lenzini, J M Frère
Jan 1, 1985·Biotechnology & Genetic Engineering Reviews·A Coulson
Jan 1, 1985·Critical Reviews in Microbiology·J M Frère, B Joris
Jan 4, 1982·Biochimica Et Biophysica Acta·C DuezL Dierickx
Jun 1, 1995·Antimicrobial Agents and Chemotherapy·K BushA A Medeiros

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