Comparison of the substrate specificities of the  -lactamases from Klebsiella aerogenes 1082E and Enterobacter cloacae P99.
A potent beta-lactamase (EC 3.5.2.6) produced by a strain of Klebsiella aerogenes (K. pneumoniae), 1082E, isolated from a hospital patient, has been examined. Its properties were different from those of most gram-negative beta-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 from Enterobacter cloacae (Aerobacter cloacae) P99. The K. aerogenes enzyme, although predominantly a penicillinase, had a wide range of specificity. In addition to hydrolyzing the cephalosporins, it attacked the normally beta-lactamaseresistant compounds methicillin and cloxacillin as well as cephalosporin analogues with the same acyl substituents. The results obtained with the E. cloacae enzyme confirmed its cephalosporinase activity and showed that, unlike the enzyme from K. aerogenes, it was relatively inactive against the penicillins.
D000667:Ampicillin; D002506:Cephalexin; D002509:Cephaloridine / Q000378:metabolism; D002511:Cephalosporins; D002512:Cephalothin; D055598:Chemical Phenomena; D002621:Chemistry; D003023:Cloxacillin; D003470:Culture Media; D004589:Electrophoresis, Disc; D004754:Enterobacter / Q000201:enzymology*; D006868:Hydrolysis; D007202:Indicators and Reagents; D007455:Iodine; D007709:Klebsiella / Q000201:enzymology*; D007711:Klebsiella pneumoniae / Q000201:enzymology; D008712:Methicillin; D010400:Penicillin G; D010405:Penicillinase / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D010406:Penicillins; D013045:Species Specificity; D013997:Time Factors
D002511:Cephalosporins; D003470:Culture Media; D007202:Indicators and Reagents; D010406:Penicillins; D000667:Ampicillin; D007455:Iodine; D010405:Penicillinase; D002509:Cephaloridine; D003023:Cloxacillin; D002506:Cephalexin; D010400:Penicillin G; D008712:Methicillin; D002512:Cephalothin