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.
Bounaga
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Department of Chemical and Biological Sciences, University of Huddersfield, Queensgate, UK.
Galleni
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Laws
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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