Quinoline and quninaldine as naturally occurring inhibitors specific for type A monoamine oxidase.
Type A monoamine oxidase (MAO-A) in human placental mitochondria was competitively inhibited by naturally occurring substances, quinoline and quinaldine, using kynuramine as substrate. Quinoline had a higher affinity for MAO than kynuramine. MAO-A in human brain synaptosomal mitochondria was also competitively inhibited by quinoline, while type B MAO (MAO-B) was reversibly and non-competitively inhibited by quinoline. Quinoline inhibited MAO-A much more potently than MAO-B. Of several compounds structurally similar to quinoline, isoquinoline noncompetitively inhibited MAO-A and -B activity.
D001667:Binding, Competitive; D001921:Brain / Q000201:enzymology; D005260:Female; D006801:Humans; D007735:Kynuramine / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D008995:Monoamine Oxidase / Q000378:metabolism; D008996:Monoamine Oxidase Inhibitors / Q000494:pharmacology*; D010920:Placenta / Q000201:enzymology; D011247:Pregnancy; D011798:Quinaldines / Q000494:pharmacology*; D011804:Quinolines / Q000494:pharmacology*; D013574:Synaptosomes / Q000201:enzymology
D008996:Monoamine Oxidase Inhibitors; D011798:Quinaldines; D011804:Quinolines; D007735:Kynuramine; C037073:2-methylquinoline; C037219:quinoline; D008995:Monoamine Oxidase