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. 1993 Apr 1;291(Pt 1):151–155. doi: 10.1042/bj2910151

An overview of the kinetic parameters of class B beta-lactamases.

A Felici 1, G Amicosante 1, A Oratore 1, R Strom 1, P Ledent 1, B Joris 1, L Fanuel 1, J M Frère 1
PMCID: PMC1132494  PMID: 8471035

Abstract

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.

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Selected References

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