A rapid-kinetic study of the class C beta-lactamase of Enterobacter cloacae 908R.
The individual rate constants for acylation and deacylation (k2 and k3, respectively) of the class C beta-lactamase of Enterobacter cloacae 908R by ampicillin and carbenicillin have been determined. For several other beta-lactams, the value of k2 was too high to be determined and the k2/k3 ratio could be larger than 10,000. Branched pathways were also shown to occur with several penicillins and cephalosporins.
Monnaie
D
D
Laboratoire d'enzymologie, Université de Liège, Belgium.
Virden
R
R
Frère
J M
JM
D016972:Enterobacter cloacae / Q000201:enzymology*; D007700:Kinetics; D013379:Substrate Specificity; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000378:metabolism*
D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases