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.

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

AMICOSANTE, Gianfranco;ORATORE, Arduino;
1993-01-01

Abstract

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.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/103134
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 174
  • ???jsp.display-item.citation.isi??? ND
social impact