Role of catechol structure in the inhibitory effects of D-isomers of amino acids on the decarboxylation of L-5-hydroxytryptophan.
D-3,4-dihydroxyphenylalanine, D-threo-3,4-dihydroxyphenylserine and pyrocatechol competitively inhibited aromatic L-amino acid decarboxylase, whereas no inhibition occurred with l-norepinephrine, l-epinephrine, dopamine or some other amino acids without catechol side chains.
D006916:5-Hydroxytryptophan / Q000037:antagonists & inhibitors*; D000818:Animals; D001667:Binding, Competitive; D001921:Brain / Q000201:enzymology; D002396:Catechols / Q000494:pharmacology*; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives / Q000494:pharmacology; D004296:Dopa Decarboxylase / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008297:Male; D051381:Rats; D013379:Substrate Specificity
D002396:Catechols; D004295:Dihydroxyphenylalanine; D006916:5-Hydroxytryptophan; D004296:Dopa Decarboxylase