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Purification and some properties of a cephalosporinase from Proteus vulgaris
Antimicrobial Agents and Chemotherapy
|January 1, 1981
Abstract:
The purified cephalosporinase from Proteus vulgaris hydrolyzed a variety of cephalosporins, including cefuroxime, at a high level; its activity was inhibited by clavulanic acid.
Insights
The purified cephalosporinase enzyme from Proteus vulgaris effectively breaks down cephalosporin antibiotics like cefuroxime. Its harmful activity against these drugs is neutralized by clavulanic acid.
Area of Science:
- Microbiology
- Enzymology
- Pharmacology
Background:
- Proteus vulgaris is a bacterium known to produce enzymes that can inactivate antibiotics.
- Cephalosporin antibiotics are crucial for treating bacterial infections, but resistance is a growing concern.
- Cephalosporinases are a class of beta-lactamase enzymes that hydrolyze cephalosporins.
Purpose of the Study:
- To characterize the cephalosporinase enzyme produced by Proteus vulgaris.
- To determine the substrate specificity of the purified enzyme.
- To investigate potential inhibitors of the enzyme's activity.
Main Methods:
- Purification of the cephalosporinase enzyme from Proteus vulgaris.
- Enzymatic assays to measure the hydrolysis of various cephalosporins, including cefuroxime.
- Testing the inhibitory effect of clavulanic acid on enzyme activity.
Main Results:
- The purified Proteus vulgaris cephalosporinase demonstrated high-level hydrolysis of multiple cephalosporins.
- Cefuroxime was significantly hydrolyzed by the enzyme.
- Clavulanic acid effectively inhibited the activity of the cephalosporinase.
Conclusions:
- Proteus vulgaris produces a potent cephalosporinase capable of inactivating important cephalosporin antibiotics.
- The enzyme's activity against cefuroxime highlights a mechanism of resistance.
- Clavulanic acid shows promise as an inhibitor for combating this type of antibiotic resistance.