Transient state kinetic studies on catalysis and inhibition of staphylococcal beta-lactamase.
The interaction of beta-lactamase with a beta-lactam substrate may, in addition to hydrolysis of the beta-lactam by way of an acylenzyme intermediate, lead to transient or permanent inhibition through one or more branches in the catalytic pathway. The balance between these processes depends on the interplay between the chemical reactivities of interacting groups and on effects on protein conformation and stability but the molecular basis is not fully understood. Examples of physical and kinetic probes of some of the mechanisms are discussed.
Virden
R
R
Department of Biochemistry and Genetics, University of Newcastle upon Tyne, U.K.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D019818:Clavulanic Acid; D002969:Clavulanic Acids / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D010406:Penicillins / Q000494:pharmacology; D013210:Staphylococcus / Q000201:enzymology*; D013997:Time Factors; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D002969:Clavulanic Acids; D010406:Penicillins; D065093:beta-Lactamase Inhibitors; D019818:Clavulanic Acid; C011097:quinacillin; D001618:beta-Lactamases