The flavonoid galangin inhibits the L1 metallo-β-lactamase from Stenotrophomonas maltophilia

Abstract The flavonoid galangin inhibits the partially purified metallo-β-lactamase from Stenotrophomonas maltophilia. The effect was not reversed by the addition of ZnCl2 suggesting that the inhibitory effect is not related to metal chelation. The flavonoid quercetin also has some inhibitory effect...

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Bibliographic Details
Published in:FEMS microbiology letters 2002-02, Vol.208 (1), p.21-24
Main Authors: Denny, Brian J, Lambert, Peter A, West, Patrick W.J.
Format: Article
Language:English
Subjects:
Chelation
Crystal structure
Enzymes
Flavonoid
Flavonoids
Galangin
Metallo-β-lactamase
Metallography
Microbiology
Molecular modelling
Molecular structure
Quercetin
Stenotrophomonas maltophilia
Zinc chloride
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Summary:Abstract The flavonoid galangin inhibits the partially purified metallo-β-lactamase from Stenotrophomonas maltophilia. The effect was not reversed by the addition of ZnCl2 suggesting that the inhibitory effect is not related to metal chelation. The flavonoid quercetin also has some inhibitory effect against the enzyme. Using the crystal structure of the enzyme, a molecular modelling study predicts a possible orientation of galangin at the active site of the enzyme.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2002.tb11054.x