Beta-Lactamase activity in strains of Bacteroides melaninogenicus and Bacteroides oralis.
beta-Lactamase from strains of Bacteroides melaninogenicus and Bacteroides oralis hydrolyzed penicillin more rapidly than ampicillin or carbenicillin. Cephalothin and a chromogenic cephalosporin (87/312) were also hydrolyzed by the enzyme. Activity was found only in beta-lactam-resistant strains, but there was considerable variation in activity among strains having the same minimal inhibitory concentrations of antibiotic. beta-Lactamase activity was cell bound and appeared to be tightly associated with the cell envelope since detergents were required to elute this activity.
D000581:Amidohydrolases / Q000378:metabolism*; D000667:Ampicillin / Q000378:metabolism; D001439:Bacteroides / Q000201:enzymology*; D002228:Carbenicillin / Q000378:metabolism; D002473:Cell Wall / Q000201:enzymology; D002510:Cephalosporinase / Q000378:metabolism*; D002512:Cephalothin / Q000378:metabolism; D010405:Penicillinase / Q000378:metabolism*; D010406:Penicillins / Q000378:metabolism; D001443:Prevotella melaninogenica / Q000201:enzymology*
D010406:Penicillins; D000667:Ampicillin; D000581:Amidohydrolases; D002510:Cephalosporinase; D010405:Penicillinase; D002228:Carbenicillin; D002512:Cephalothin