PMID: 6991465Mar 1, 1980Paper

PS-5 inhibition of a beta-lactamase from Proteus vulgaris

The Journal of Antibiotics
K OkamuraT Ishikura

Abstract

Inhibition of Proteus vulgaris beta-lactamase by a new beta-lactam antibiotic, PS-5 was studied kinetically. There were two stages of inhibition. In the early stage, PS-5 inhibited the beta-lactamase by formation of a Michaelis-complex, and showed a competitive inhibition pattern with Ki-value of 0.22 microM (substrate, cephaloridine). After the formation of a Michaelis-complex between PS-5 and the enzyme, PS-5 showed a characteristic progressive inhibition pattern with time. Maximum inactivation was obtained after several minutes of preincubation of the enzyme with PS-5; as hydrolysis of PS-5 progressed, the enzyme activity was gradually recovered. Reactivation by an excess of substrate (cephaloridine) was not substantially realized in the presence of PS-5. PS-5 was very slowly hydrolyzed by the enzyme, showing a triphasic pattern in its reaction curve.

Citations

Apr 1, 2014·Applied Microbiology and Biotechnology·Veličković DušanDimitrijević Aleksandra
Oct 1, 1983·Medicinal Research Reviews·S J Cartwright, S G Waley
Jan 1, 1988·Clinical Microbiology Reviews·K Bush
Jan 1, 1984·Antimicrobial Agents and Chemotherapy·T HashizumeT Sawai
Mar 1, 1984·Antimicrobial Agents and Chemotherapy·A YamaguchiT Sawai

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