Interaction of .BETA.-lactamase of Streptomyces cacaoi. I. Clavulanic acid and PS-5.
- 1 January 1981
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 34 (10) , 1341-1346
- https://doi.org/10.7164/antibiotics.34.1341
Abstract
Inactivation of a .beta.-lactamase of S. cacaoi by clavulanic acid and PS-5 was investigated and compared with that of a .beta.-lactamase of Bacillus cereus. Inhibition of the enzymes induced by clavulanic acid and the .beta.-lactam antibiotic PS-5 was progressive with time, but the degree of inhibition of the .beta.-lactamase from S. cacaoi increased more progressively with time than that of the enzyme from B. cereus. Conformative response constants were determined. As compared with clavulanic acid, over 10 times higher concentrations of PS-5 were necessary to give a similar degree of inhibition. At lower concentrations, clavulanic acid and PS-5 behaved as competitive inhibitors. Ki values calculated from the integrated form of the Lineweaver-Burk type were 1.1 .times. 10-7 M and 7.6 .times. 10-6 M for clavulanic acid and PS-5, respectively.This publication has 1 reference indexed in Scilit:
- Clavulanic Acid: a Beta-Lactamase-Inhibiting Beta-Lactam from Streptomyces clavuligerusAntimicrobial Agents and Chemotherapy, 1977