Catabolism of tryptophan, anthranilate, and 2,3-dihydroxybenzoate in Trichosporon cutaneum.
Trichosporon cutaneum degraded L-tryptophan by a reaction sequence that included L-kynurenine, anthranilate, 2,3-dihydroxybenzoate, catechol, and beta-ketoadipate as catabolites. All of the enzymes of the sequence were induced by both L-tryptophan and salicylate, and those for oxidizing kynurenine and its catabolites were induced by anthranilate but not by benzoate; induction was not coordinate. Molecular weights of 66,100 and 36,500 were determined, respectively, for purified 2,3-dihydroxybenzoate decarboxylase and its single subunit. Substrates for this enzyme were restricted to benzoic acids substituted with hydroxyl groups at C-2 and C-3; no added coenzyme was required for activity. Partially purified anthranilate hydroxylase (deaminating) catalyzed the incorporation of one atom of 18O, derived from either 18O2 or H2(18)O, into 2,3-dihydroxybenzoic acid.
D002262:Carboxy-Lyases / Q000302:isolation & purification / Q000378:metabolism; D002396:Catechols / Q000378:metabolism; D062385:Hydroxybenzoates / Q000378:metabolism*; D007737:Kynurenine / Q000378:metabolism; D003904:Mitosporic Fungi / Q000201:enzymology / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism; D012459:Salicylates / Q000378:metabolism; D014364:Tryptophan / Q000378:metabolism*; D062367:ortho-Aminobenzoates / Q000378:metabolism*
D002396:Catechols; D062385:Hydroxybenzoates; D012459:Salicylates; D062367:ortho-Aminobenzoates; D007737:Kynurenine; C009135:2,3-dihydroxybenzoic acid; D014364:Tryptophan; D006899:Mixed Function Oxygenases; C023440:anthranilate 2,3-dioxygenase(deaminating); D002262:Carboxy-Lyases; C022501:2-pyrocatechuate decarboxylase