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.
An overview of the kinetic parameters of class B β-lactamases
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A Felici, G Amicosante, A Oratore, R Strom, P Ledent, B Joris, L Fanuel, J M Frère; An overview of the kinetic parameters of class B β-lactamases. Biochem J 1 April 1993; 291 (1): 151–155. doi: https://doi.org/10.1042/bj2910151
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