Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase

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

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

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.

LanguageEnglish
Pages503-510
Number of pages8
JournalBioorganic and Medicinal Chemistry
Volume9
Issue number2
DOIs
Publication statusPublished - Feb 2001

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Bacillus cereus
beta-Lactamases
Zinc
Catalytic Domain
Peptides
Stereochemistry
Sulfhydryl Compounds
Anions
Enzymes
hydroxide ion

Cite this

Bounaga, Sakina ; Galleni, Moreno ; Laws, Andrew P. ; Page, Michael I. / Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase. In: Bioorganic and Medicinal Chemistry. 2001 ; Vol. 9, No. 2. pp. 503-510.
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Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase. / Bounaga, Sakina; Galleni, Moreno; Laws, Andrew P.; Page, Michael I.

In: Bioorganic and Medicinal Chemistry, Vol. 9, No. 2, 02.2001, p. 503-510.

Research output: Contribution to journalArticle

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