Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase

Bioorg Med Chem. 2001 Feb;9(2):503-10. doi: 10.1016/s0968-0896(00)00257-1.

Abstract

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.

MeSH terms

  • Bacillus cereus / enzymology*
  • Bacterial Proteins
  • Binding Sites
  • Combinatorial Chemistry Techniques
  • Cysteine*
  • Dipeptides / chemical synthesis
  • Dipeptides / pharmacology*
  • Enzyme Inhibitors / pharmacology*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Structure-Activity Relationship
  • Zinc
  • beta-Lactamase Inhibitors*
  • beta-Lactamases / chemistry

Substances

  • Bacterial Proteins
  • Dipeptides
  • Enzyme Inhibitors
  • beta-Lactamase Inhibitors
  • beta-Lactamases
  • Zinc
  • Cysteine