Asparenomycins A, B and C, new carbapenem antibiotics. V. Inhibition of .BETA.-lactamases.
- 1 January 1982
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 35 (1) , 39-45
- https://doi.org/10.7164/antibiotics.35.39
Abstract
Asparenomycins (ASM) A, B and C inhibited a wide range of .beta.-lactamases, including cephalosporinases and penicillinases, usually at concentrations < 3 .mu.M. On studying the mechanism of inhibition of .beta.-lactamases produced by gram-negative bacteria by ASM A, it was concluded that ASM A inhibited the .beta.-lactamases by acylating the enzymes. The inhibition was progressive with time. The inhibitor formed stable complexes with the enzyme. Before completing inhibition of 1 molecule of the enzyme, 1.8 molecules of the inhibitor were hydrolyzed.This publication has 2 references indexed in Scilit:
- PS-5, a new .BETA.-lactam antibiotic. III. Synergistic effects and inhibitory activity against a .BETA.-lactamase.The Journal of Antibiotics, 1979
- Clavulanic Acid: a Beta-Lactamase-Inhibiting Beta-Lactam from Streptomyces clavuligerusAntimicrobial Agents and Chemotherapy, 1977