Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase

Sakina Bounaga, Moreno Galleni, Andrew P. Laws, Michael I. Page

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)


Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-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.

Original languageEnglish
Pages (from-to)503-510
Number of pages8
JournalBioorganic and Medicinal Chemistry
Issue number2
Publication statusPublished - Feb 2001


Dive into the research topics of 'Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase'. Together they form a unique fingerprint.

Cite this