The flavonoid galangin inhibits the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
The flavonoid galangin inhibits the partially purified metallo-beta-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.
Denny
Brian J
BJ
Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Kuwait University, Kuwait, Kuwait. denny@hsc.kuniv.edu.kw
Lambert
Peter A
PA
West
Patrick W J
PW
D004791:Enzyme Inhibitors / Q000494:pharmacology; D005419:Flavonoids / Q000737:chemistry / Q000494:pharmacology*; D008958:Models, Molecular; D011794:Quercetin / Q000737:chemistry / Q000494:pharmacology; D020615:Stenotrophomonas maltophilia / Q000201:enzymology*; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000737:chemistry / Q000378:metabolism
D004791:Enzyme Inhibitors; D005419:Flavonoids; D065093:beta-Lactamase Inhibitors; C037032:galangin; D011794:Quercetin; C088032:beta-lactamase L1; D001618:beta-Lactamases