An overview of the kinetic parameters of class B β-lactamases

• Published in: Biochemical journal 1993-04, Vol.291 (1), p.151-155
• Main Authors: FELICI, A, AMICOSANTE, G, ORATORE, A, STROM, R, LEDENT, P, JORIS, B, FANUEL, L, FRERE, J.-M
• Format: Article
• Language: English
• Subjects: Aeromonas hydrophila; Aeromonas hydrophila - enzymology; Analytical, structural and metabolic biochemistry; Bacillus cereus - enzymology; Bacteroides fragilis; beta-Lactamases - chemistry; beta-Lactamases - isolation & purification; beta-Lactamases - metabolism; beta-Lactamases/chemistry/isolation & purification/metabolism; Biochemistry, biophysics & molecular biology; Biochimie, biophysique & biologie moléculaire; Biological and medical sciences; Catalysis; Electrophoresis, Polyacrylamide Gel; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; Isoelectric Point; Kinetics; Life sciences; Molecular Weight; Pseudomonas - enzymology; Pseudomonas maltophilia; Sciences du vivant
• ISSN: 0264-6021; 1470-8728; 1470-8728
• DOI: 10.1042/bj2910151

The catalytic properties of three class B beta-lactamases (from Pseudomonas maltophilia, Aeromonas hydrophila and Bacillus cereus) were studied and compared with those of the Bacteroides fragilis enzyme. The A. hydrophila beta-lactamase exhibited a unique specificity profile and could be considered as a rather specific 'carbapenemase'. No relationships were found between sequence similarities and catalytic properties. The problem of the repartition of class B beta-lactamases into sub-classes is discussed. Improved purification methods were devised for the P. maltophilia and A. hydrophila beta-lactamases including, for the latter enzyme, a very efficient affinity chromatography step on a Zn(2+)-chelate column.