Biochemical properties of a penicillinase from Escherichia coli carrying Rms 298.
We obtained two R plasmids, i.e., Rms195 and Rms298, from a clinical isolate, E. coli GN5503. Penicillin beta-lactamase (PCase) was extracted from ML1410 Rms195+ and Rms298+, and was purified by chromatography. Rms195 PCase was identical to the type I PCase mediated by R-TEM, RI and Rms212. The isoelectric point of Rms298 PCase was 5.9 and its molecular weight was 21,000 +/- 1,000. The substrate profile and physiochemical properties indicate that Rms298 PCase belongs to the type IV PCase mediated by Rms139 isolated from Pseudomonas aeruginosa.
D002511:Cephalosporins / Q000378:metabolism; D003227:Conjugation, Genetic; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007526:Isoelectric Point; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D009566:Nitrates / Q000494:pharmacology; D010405:Penicillinase / Q000235:genetics / Q000378:metabolism; D010406:Penicillins / Q000378:metabolism; D011815:R Factors; D015032:Zinc / Q000494:pharmacology
D002511:Cephalosporins; D009566:Nitrates; D010406:Penicillins; D010405:Penicillinase; D008274:Magnesium; D015032:Zinc