Interaction of clavulanate with class C beta-lactamases.
The interactions between clavulanate and three class C enzymes have been studied in detail. In all cases, the reactions followed branched pathways where 25-150 turnovers occurred before inactivation was completed. Reactivation rates were quite low. The poor efficiency of clavulanate as a class C inactivator appeared to rest upon a very slow acylation of the protein, and of a relatively high turnover rate.
Monnaie
D
D
Centre d'Ingénierie des Protéines and Laboratorie d'enzymologie, Université de Liège, Belgium.
Frere
J M
JM
D019818:Clavulanic Acid; D002969:Clavulanic Acids / Q000378:metabolism*; D016972:Enterobacter cloacae / Q000201:enzymology; D007700:Kinetics; D012706:Serratia marcescens / Q000201:enzymology; D013211:Staphylococcus aureus / Q000201:enzymology; D013302:Streptomyces / Q000201:enzymology; D065093:beta-Lactamase Inhibitors
D002969:Clavulanic Acids; D065093:beta-Lactamase Inhibitors; D019818:Clavulanic Acid