Structure-action relationships of histidine decarboxylase inhibitors.
Substituted phenols were found to be more potent inhibitors of histidine decarboxylase than were the correspondingly-substituted benzoic acids. Regression analysis, though indicating that potent inhibitors of histamine formation are unlikely to be found among simple, substituted phenols, enables tentative conclusions to be drawn regarding the nature of the interaction between these compounds and the enzyme.
D000818:Animals; D001565:Benzoates / Q000494:pharmacology; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors*; D006640:Histidine Decarboxylase / Q000037:antagonists & inhibitors*; D010636:Phenols / Q000494:pharmacology*; D051381:Rats; D012044:Regression Analysis; D013270:Stomach / Q000201:enzymology; D013329:Structure-Activity Relationship
D001565:Benzoates; D010636:Phenols; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase