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A potent β-lactamase (EC 3.5.2.6) produced by a strain ofKlebsiella aerogenes (K. pneumoniae ), 1082E, isolated from a hospital patient, has been examined. Its properties were different from those of most gram-negative β-lactamases previously reported. The enzyme has been partly purified, and its activity against a range of substrates has been compared with that of the enzyme fromEnterobacter cloacae (Aerobacter cloacae ) P99. TheK. aerogenes enzyme, although predominantly a penicillinase, had a wide range of specificity. In addition to hydrolyzing the cephalosporins, it attacked the normally β-lactamaseresistant compounds methicillin and cloxacillin as well as cephalosporin analogues with the same acyl substituents. The results obtained with theE. cloacae enzyme confirmed its cephalosporinase activity and showed that, unlike the enzyme fromK. aerogenes , it was relatively inactive against the penicillins.

Comparison of the Substrate Specificities of the β-Lactamases from Klebsiella aerogenes 1082E and Enterobacter cloacae P99