id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-321834-n5w88l23	Huang, Cheng-Yang	Inhibition of a Putative Dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by Flavonoids and Substrates of Cyclic Amidohydrolases	2015-05-19		.txt	text/plain	5231	297	47	Although the inhibitory effects of these flavonoids on dihydropyrimidinase were substrate-dependent, dihydromyricetin significantly inhibited dihydropyrimidinase with IC(50) values of 48 and 40 μM for the substrates dihydrouracil and 5-propyl-hydantoin, respectively. In this study, we investigated the effects of the substrates and inhibitors of allantoinase and dihydroorotase, including the flavonols myricetin, quercetin, kaempferol, and galangin, on inhibiting the catalytic activity of a putative dihydropyrimidinase from P. Although dihydromyricetin and myricetin were docked Inhibition of Dihydropyrimidinase by Flavonoids into the active site pocket of dihydropyrimidinase, their binding modes differed. In this study, we showed that dihydromyricetin, a flavonol, significantly inhibited the catalytic activities of dihydropyrimidinase toward both the natural substrate dihydrouracil and xenobiotic substrate 5-propyl-hydantoin (Fig 3) . For example, as shown in Fig 3, the inhibitory effect of kaempferol on the activity of dihydropyrimidinase was significant only with dihydrouracil as a substrate (with IC 50 value of 50 ± 2 μM), but not with 5-propyl-hydantoin.	./cache/cord-321834-n5w88l23.txt	./txt/cord-321834-n5w88l23.txt