Carbenicillin-hydrolyzing penicillinases of Proteus mirabilis and the PSE-type penicillinases of Pseudomonas aeruginosa.
Three carbenicillin-hydrolyzing penicillinases were found in Proteus mirabilis strains, N-3, N-29, and GN79. The former two strains were isolated in 1978, but strain GN79 was one of our stock cultures isolated in 1965. These penicillinases closely resembled each other, and the PSE-1 and PSE-4 enzymes produced by Pseudomonas aeruginosa, in their substrate profiles and kinetic properties for hydrolyzing various beta-lactams. However, differences were found in their molecular weights and isoelectric points which ranged from 22,000 to 27,000 and from 6.0 to 6.9, respectively. The antiserum against the purified penicillinase of N-29 cross-reacted with the enzyme of N-3 and inhibited its activity by more than 80%. The antiserum also reacted with the PSE-1 and PSE-4 enzymes. The antiserum did not react with the penicillinase from strain GN79 and the PSE-2 and PSE-3 enzymes of P. aeruginosa. Enzyme production in N-3 and N-29 was mediated by R plasmids.
D000818:Animals; D004587:Electrophoresis, Agar Gel; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D010403:Penicillin Resistance; D010405:Penicillinase / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D011513:Proteus mirabilis / Q000201:enzymology* / Q000235:genetics; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics; D011815:R Factors; D011817:Rabbits
D010405:Penicillinase