An overview of the kinetic parameters of class B beta-lactamases.
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.
Felici
A
A
Università degli Studi dell'Aquila, Dipartimento di Scienze e Tecnologie Biomediche e di Biometria, Italy.
Amicosante
G
G
Oratore
A
A
Strom
R
R
Ledent
P
P
Joris
B
B
Fanuel
L
L
Frère
J M
JM
D016980:Aeromonas hydrophila / Q000201:enzymology; D001409:Bacillus cereus / Q000201:enzymology; D002384:Catalysis; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology; D001618:beta-Lactamases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D001618:beta-Lactamases