Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase.
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.
Department of Chemical and Biological Sciences, University of Huddersfield, Queensgate, UK.
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D001409:Bacillus cereus / Q000201:enzymology*; D001426:Bacterial Proteins; D001665:Binding Sites; D020650:Combinatorial Chemistry Techniques; D003545:Cysteine; D004151:Dipeptides / Q000138:chemical synthesis / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013329:Structure-Activity Relationship; D015032:Zinc; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000737:chemistry
D001426:Bacterial Proteins; D004151:Dipeptides; D004791:Enzyme Inhibitors; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases; D015032:Zinc; D003545:Cysteine