Affiliation:
1. Research Laboratories, Ciba-Geigy Ltd., CH-4002 Basel, Switzerland
Abstract
Extracellular hydrolases from
Cephalosporium acremonium
were analyzed according to their ability to deacetylate the β-lactam antibiotic cephalosporin C. One out of at least six hydrolases exhibits appreciable cephalosporin C acetylhydrolase (CAH) activity. This enzyme was separated from other hydrolases and purified 220-fold. The purified CAH has a relatively low affinity for cephalosporin C (
K
m
, 20 mM) and is strongly inhibited by diisopropylfluorophosphate and less markedly affected by fluoride. Addition of glucose, maltose, and sucrose to the culture broth suppresses CAH production, whereas glycerol and succinate have no effect. Verrucarin A prevented the enzyme from appearing in the medium, which indicates the necessity of protein synthesis for CAH formation. When 1-thio-
d
-glucose was added to the culture medium, the results suggested that this glucose analogue is able to inhibit CAH synthesis. Our data provide evidence for a regulation of CAH synthesis similar to the catabolite repression system in bacteria.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Cited by
41 articles.
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