Research paperInhibition in vitro of the enzymes of the oxidative pathway of tryptophan metabolism and of nicotinamide nucleotide synthesis by benserazide, carbidopa and isoniazid
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Kynurenine pathway and human systems
2020, Experimental GerontologyCitation Excerpt :This is most likely due to upregulation of TDO, as well as of KAT and down-regulation of KMO, thus increasing the availability of the Kyn substrate (for references, see Badawy and Guillemin, 2019). 3-HAAO is the most active of the KP enzymes (Nishizuka and Hayaishi, 1963; Bender, 1980), which may explain the rapid conversion of 3-HAA to QA. While 3-HAAO inhibition is desirable to limit QA production, it can result in 3-HAA accumulation with potential proinflammatory effects.
Hypothesis kynurenic and quinolinic acids: The main players of the kynurenine pathway and opponents in inflammatory disease
2018, Medical HypothesesCitation Excerpt :As shown in Table 1, normal human plasma [3-HAA] is in the low nM range. This could be explained by 3-HAAO being the most active KP enzyme, as demonstrated in rat [53] and mouse [54] liver. The lowest effective [3-HAA] (10 µM) used by Fallarino et al. [52] is 377–1297-fold larger than the normal control plasma values in Table 1, whereas a 100 µM [3-HAA] is a further 10-fold higher.
Tryptophan availability for kynurenine pathway metabolism across the life span: Control mechanisms and focus on aging, exercise, diet and nutritional supplements
2017, NeuropharmacologyCitation Excerpt :However, transamination is enhanced by K or Trp loading or if K hydroxylase or kynureninase activity is inhibited. Because 3-HAA oxidase activity is the highest of all KP enzymes (Nishizuka and Hayaishi, 1963; Bender, 1980), 3-HAA is rapidly converted to quinolinic acid (QA) by non-enzymic cyclization of acroleyl aminofumarate. This latter intermediate is at the cross point of the pathway, which favours QA and hence production of nicotinamide and NAD+.
Schistosoma mansoni: Effects on tryptophan metabolism in mice
1990, Experimental Parasitology