Valpromide inhibits human epoxide hydrolase.
The effect of antipileptic drug valpromide (VPM) on the activity of epoxide hydrolase was studied in human adult and foetal liver, kidneys, lungs, intestine and in placenta. The activity of the epoxide hydrolase was measured with both styrene oxide and benzo(a)pyrene-4,5-oxide as substrates. VPM inhibited the epoxide hydrolase obtained from all organs studied. The degree of inhibition was independent of the substrate used. A lowering of the epoxide hydrolase activity by 50% was observed when the concentration of VPM was similar to that of the substrates. VPM competitively inhibited the activity of adult liver epoxide hydrolase with styrene oxide as substrate.
D000328:Adult; D000368:Aged; D000927:Anticonvulsants / Q000494:pharmacology*; D001580:Benzopyrenes; D004851:Epoxide Hydrolases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004852:Epoxy Compounds; D005260:Female; D005333:Fetus / Q000201:enzymology; D006801:Humans; D007422:Intestines / Q000201:enzymology; D007668:Kidney / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D008875:Middle Aged; D014635:Valproic Acid / Q000031:analogs & derivatives / Q000494:pharmacology*
D000927:Anticonvulsants; D001580:Benzopyrenes; D004852:Epoxy Compounds; C006707:benzo(a)pyrene 4,5-epoxide; D014635:Valproic Acid; C013690:styrene oxide; D004851:Epoxide Hydrolases; C004651:dipropylacetamide