Keywords :
Bacillus cereus/enzymology; Bacterial Proteins; Binding Sites; Combinatorial Chemistry Techniques; Cysteine; Dipeptides/chemical synthesis/pharmacology; Enzyme Inhibitors/pharmacology; Hydrogen-Ion Concentration; Kinetics; Structure-Activity Relationship; Zinc; beta-Lactamase Inhibitors; beta-Lactamases/chemistry
Abstract :
[en] Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-beta-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site.
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