Co-existence of beta-lactamase and penicillin acylase in bacteria; detection and quantitative determination of enzyme activities.
Twenty-six bacteria were examined for the presence of penicillin acylase and beta-lactamase. A copper reducing assay, which was sensitive in the analytical range 2-20 micrograms/ml, was used for determination of penicilloates and a fluorescamine assay was used to determine 6-aminopenicillanic acid concentrations when both substances were produced by the action of the enzymes on a single substrate. Seventeen bacteria contained beta-lactamases, six contained penicillin acylases and four contained both enzymes. Two bacteria contained a Type 1 penicillin acylase and four bacteria contained a Type II enzyme. No ampicillin acylases were detected. All beta-lactamases were constitutive enzymes in those organisms where both enzymes co-existed. Bacillus subtilis and B. cereus produced inducible and extracellular beta-lactamases. Acinetobacter calcoaceticus ATCC 21288 produced a constitutive beta-lactamase which was detected extracellularly.
Baker
W L
WL
Swinburne Institute of Technology, Hawthorn, Victoria, Australia.
D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D003300:Copper / Q000378:metabolism; D004790:Enzyme Induction; D005470:Fluorometry / Q000379:methods; D010084:Oxidation-Reduction; D010399:Penicillin Amidase / Q000032:analysis*; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000032:analysis* / Q000378:metabolism; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D047090:beta-Lactams; D003300:Copper; D010399:Penicillin Amidase; D001618:beta-Lactamases