The catalytic properties of three class B β-lactamases (from Pseudomonas maltophilia Aeromonas hydrophila and Bacillus cereus) were studied and compared with those of the Bacteroides fragilis enzyme. The A. hydrophila β-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 β-lactamases into sub-classes is discussed. Improved purification methods were devised for the P. maltophilia and A. hydrophila β-lactamases including, for the latter enzyme, a very efficient affinity chromatography step on a Zn2+-chelate column.
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