Article (Scientific journals)
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase.
Bounaga, S.; Galleni, Moreno; Laws, A. P. et al.
2001In Bioorganic and Medicinal Chemistry, 9 (2), p. 503-10
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Keywords :
Bacillus cereus/enzymology; Bacterial Proteins; Binding Sites; Combinatorial Chemistry Techniques; Cysteine; Dipeptides/chemical synthesis/pharmacology; Enzyme Inhibitors/pharmacology; Hydrogen-Ion Concentration; Kinetics; Structure-Activity Relationship; Zinc; beta-Lactamase Inhibitors; beta-Lactamases/chemistry
Abstract :
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Bounaga, S.
Galleni, Moreno ;  Université de Liège - ULiège
Laws, A. P.
Page, M. I.
Language :
English
Title :
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase.
Publication date :
2001
Journal title :
Bioorganic and Medicinal Chemistry
ISSN :
0968-0896
eISSN :
1464-3391
Publisher :
Elsevier, United Kingdom
Volume :
9
Issue :
2
Pages :
503-10
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 08 December 2015

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