The inhibitory activity of six groups of flavonoids against yeast and rat small intestinal alpha-glucosidases and porcine pancreatic alpha-amylase was compared, and chemical structures of flavonoids responsible for the inhibitory activity were evaluated. Yeast alpha-glucosidase was potently inhibited by the anthocyanidin, isoflavone and flavonol groups with the IC50 values less than 15 microM. The following structures enhanced the inhibitory activity: the unsaturated C ring, 3-OH, 4-CO, the linkage of the B ring at the 3 position, and the hydroxyl substitution on the B ring. Rat small intestinal alpha-glucosidase was weakly inhibited by many flavonoids, and slightly by the anthocyanidin and isoflavone groups. 3-OH and the hydroxyl substitution on the B ring increased the inhibitory activity. In porcine pancreatic alpha-amylase, luteolin, myricetin and quercetin were potent inhibitors with the IC50 values less than 500 microM. The 2,3-double bond, 5-OH, the linkage of the B ring at the 3 position, and the hydroxyl substitution on the B ring enhanced the inhibitory activity, while 3-OH reduced it.
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Evidence ID | Analyze ID | Gene/Complex | Systematic Name/Complex Accession | Qualifier | Gene Ontology Term ID | Gene Ontology Term | Aspect | Annotation Extension | Evidence | Method | Source | Assigned On | Reference |
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Complement ID | Locus ID | Gene | Species | Gene ID | Strain background | Direction | Details | Source | Reference |
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Evidence ID | Analyze ID | Dataset | Description | Keywords | Number of Conditions | Reference |
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