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

• Published in: FEMS microbiology letters Vol. 208; no. 1; pp. 21 - 24
• Main Authors: Denny, Brian J, Lambert, Peter A, West, Patrick W.J
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier B.V 19.02.2002; Blackwell
• Subjects: Bacteriology; beta-Lactamase Inhibitors; beta-Lactamases - chemistry; beta-Lactamases - metabolism; Biological and medical sciences; Enzyme Inhibitors - pharmacology; Flavonoid; Flavonoids - chemistry; Flavonoids - pharmacology; Fundamental and applied biological sciences. Psychology; Galangin; Metabolism. Enzymes; Metallo-β-lactamase; Microbiology; Models, Molecular; Molecular modelling; Quercetin - chemistry; Quercetin - pharmacology; Stenotrophomonas maltophilia; Stenotrophomonas maltophilia - enzymology; Stenotrophomonas maltophilia; Galangin; Metallo-β-lactamase; Molecular modelling; Flavonoid; Pseudomonadales; Resistance; Antibiotic; Lactam; Bacteria; Pseudomonadaceae; Inhibitor
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1016/S0378-1097(01)00580-8

The flavonoid galangin inhibits the partially purified metallo-β-lactamase from Stenotrophomonas maltophilia. The effect was not reversed by the addition of ZnCl 2 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.