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5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
D-tryptophan + O2
N-formyl-D-kynurenine
L-Trp + O2
L-formylkynurenine
L-tryptophan + O2
N-formyl-L-kynurenine
L-tryptophan + O2-
N-formyl-L-kynurenine
additional information
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5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
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5-hydroxy-L-tryptophan + O2
N-formyl-5-hydroxy-L-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
IDO displays a similar kcat for D- and L-tryptophan, but D-tryptophan has 173folds higher Km
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D-tryptophan + O2
N-formyl-D-kynurenine
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L-Trp is a better substrate for IDO than D-Trp
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D-tryptophan + O2
N-formyl-D-kynurenine
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IDO1
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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IDO1
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
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D-tryptophan + O2
N-formyl-D-kynurenine
while L and D-tryptophan have similar affinities (Km values), the kcat is 10times lower for D-tryptophan
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L-Trp + O2
L-formylkynurenine
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regulation of enzyme activity
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L-Trp + O2
L-formylkynurenine
during larval life the enzyme controls the level of potentially harmful free Trp in the hemolymph by converting it to kynurenine, and during adult development the enzyme catalyzes the first step of brown eye pigment biosynthesis
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L-Trp + O2
L-formylkynurenine
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lipopolysaccharide and muramyl tripeptide upregulate enzyme induction through a mechanism independent of interleukin 1alpha
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L-Trp + O2
L-formylkynurenine
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interleukin-4 inhibits expression of the enzyme in monocytes
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L-Trp + O2
L-formylkynurenine
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initial enzyme of tryptophan degradation pathway
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L-Trp + O2
L-formylkynurenine
induction by interferongamma
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L-Trp + O2
L-formylkynurenine
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activity is increased in important biological processes, such as protection of the fetus from rejection during pregnancy and possibly T cell death in HIV-infected patients
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L-Trp + O2
L-formylkynurenine
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Trp degradation by the enzyme regulates lymphocyte proliferation
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L-Trp + O2
L-formylkynurenine
rate-limiting enzyme in the catabolism of tryptophan
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L-Trp + O2
L-formylkynurenine
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IDO is the first enzyme in UV-filter pathway. UV-filter biosynthesis is active even in aged lenses
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L-Trp + O2
L-formylkynurenine
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the enzyme inhibits tumor cell proliferation by tryptophan depletion. IDO-induced suppression of antitumoral immune response in both adenocarcinoma and squamous cell carcinoma
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L-Trp + O2
L-formylkynurenine
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indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase catalyze the rate-limiting step in the kynurenine pathway from Trp to quinolinic acid
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L-Trp + O2
L-formylkynurenine
induction by interferongamma
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L-Trp + O2
L-formylkynurenine
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enzyme contributes to tumor cell evasion of T cell-mediated rejection
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L-Trp + O2
L-formylkynurenine
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expression of indoleamine 2,3-dioxygenase is an inducible feature of specific subsets of dendritic cells, and provides a potential mechanistic explanation for their T cell regulatory properties
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L-Trp + O2
L-formylkynurenine
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tryptophan-derived catabolites are responsible for inhibition of T cell and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase
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L-Trp + O2
L-formylkynurenine
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regulatory control
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L-Trp + O2
L-formylkynurenine
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a dramatic and specific induction of the pulmonary enzyme by virus and lipopolysaccharide is mediated by interferon. The enzyme may play an important role in the inflammatory processes, immune responses, and/or the mode of action of interferon
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L-Trp + O2
L-formylkynurenine
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influenza virus infection and tumor transplantation induce the enzyme
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L-Trp + O2
L-formylkynurenine
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regulatory control
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L-Trp + O2
L-formylkynurenine
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regulation of enzyme activity
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L-Trp + O2
L-formylkynurenine
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indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase catalyze the rate-limiting step in the kynurenine pathway from Trp to quinolinic acid
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L-Trp + O2
L-formylkynurenine
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enzyme controls the physiological flux of Trp into both the serotonergic and kynureninic pathways
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L-Trp + O2
L-formylkynurenine
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key enzyme of tryptophan catabolism, importance as regulator of whole-body tryptophan catabolism and brain levels of tryptophan and serotonin
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L-Trp + O2
L-formylkynurenine
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the skin enzyme may play an important role in the initiation or suppression of rat hair growth
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L-Trp + O2
L-formylkynurenine
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regulatory control
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L-Trp + O2
L-formylkynurenine
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key regulatory enzyme, though irreversible degradation, controls the flux of tryptophan through physiologically relevant pathways
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L-tryptophan + O2
N-formyl-L-kynurenine
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tryptophan 2,3-dioxygenase is the only enzyme able to initiate L-tryptophan degradation through the kynurenine pathway
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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the enzyme is involved in tryptophan catabolism and in quinolinate biosynthesis
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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395469, 657496, 660498, 664443, 665164, 666239, 666378, 666763, 666895, 687116, 711247, 711422, 711580, 711776, 711952, 712112, 712172, 712173, 712230, 712250, 712647, 712820, 712832, 712945, 712947, 713489, 724912 -
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan that contributes to immune suppression and tolerance
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L-tryptophan + O2
N-formyl-L-kynurenine
IDO displays a similar kcat for D- and L-tryptophan, but D-tryptophan has 173folds higher Km
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-Trp is a better substrate for IDO than D-Trp
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L-tryptophan + O2
N-formyl-L-kynurenine
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human TDO displays a major specificity towards L-Trp, structural role of T342 in controlling the substrate stereoselectivity of the enzyme
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L-tryptophan + O2
N-formyl-L-kynurenine
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IDO1 and IDO2
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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no activity with oxygen concentrations below 0.1 mM, maximum activity at 1.15 mM oxygen
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L-tryptophan + O2
N-formyl-L-kynurenine
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first step during biosynthesis of 3-hydroxyquinaldic acid
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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663820, 665204, 666461, 666895, 687116, 710831, 711165, 712112, 712152, 712821, 713412, 713448, 713586 -
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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IDO represents an important immune regulatory enzyme under diverse physiological and pathological conditions in vivo and is of considerable medical importance
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L-tryptophan + O2
N-formyl-L-kynurenine
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indoleamine 2,3-dioxygenase is a rate-limiting enzyme in the L-tryptophan-kynurenine pathway. IFN-gamma-induced expression of IDO expression is inhibited only by JAK inhibitor I. Lipopolysaccharide-induced expression of indoleamine 2,3-dioxygenase is inhibited by LY294002 and SP600125 but not by JAK inhibitor I, SB203580, or U0126. LPS can induce the expression of indoleamine 2,3-dioxygenase via an IFN-gamma-independent mechanism and PI3 kinase and JNK in the LPS-induced pathway leading to IDO expression
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L-tryptophan + O2
N-formyl-L-kynurenine
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IDO1 and IDO2
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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higher affinity at alkaline pH than at acidic pH
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L-tryptophan + O2
N-formyl-L-kynurenine
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the enzyme is involved in the catabolic pathway of L-tryptophan degradation, overview
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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no activity with oxygen concentrations below 0.1 mM, maximum activity at 1.15 mM oxygen
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L-tryptophan + O2
N-formyl-L-kynurenine
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rate-limiting enzyme in L-tryptophan catabolism and thus a key serotonergic determinant
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
while L and D-tryptophan have similar affinities (Km values), the kcat is 10times lower for D-tryptophan
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2-
N-formyl-L-kynurenine
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L-tryptophan + O2-
N-formyl-L-kynurenine
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serotonin + O2
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serotonin + O2
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tryptamine + O2
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tryptamine + O2
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tryptamine + O2
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additional information
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first and rate-limiting enzyme in tryptophan metabolism
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additional information
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first enzyme of the kynurenine pathway of tryptophan metabolism
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additional information
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in the placenta, inhibition of the enzyme leads to spontaneous abortion. By catabolizing extracellular tryptophan the enzyme inhibits local T cell proliferation thereby preventing placental rejection. This mechanism can also be active in suppressing inflammatory responses in the central neurvous system, where inflammation must be tightly regulated to prevent the loss of irreplaceable neurons. Local expression of the enzyme during inflammation is a self-protection mechanism which limits antigen-specific immune responses in the central nervous system
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additional information
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Langerhans cells possess an immunoregulatory function in promoting T cell tolerance by production of IDO
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additional information
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the oxidative metabolism of melatonin is due, in presence of H2O2, to the activities of both myeloperoxidase, EC 1.11.1.7 and indolemanine 2,3-dioxygenase
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additional information
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the enzyme plays an important physiological role in the defense mechanism against a variety of infectious pathogens, in the regulation of T-cell function by macrophages and a subset of dendritic cells, and in the synthesis of UV filters in human lenses. Serious problems arise from the unregulated over-expression of the enzyme, which often results in a deleterious systemic Trp depletion and/or the accumulation of neurotoxin, quinolinic acidn the brain. Enzyme expression in malignant tumors helps them to avoid the immune surveillance through a local Trp depletion. The kynurenilation of the lens protein with UV filters thus appears to be the major cause of age-related cataract
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additional information
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the IDO enzyme is involved in the immune regulation of early atherosclerosis, particularly in young female adults
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additional information
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the enzyme acts as a heme peroxidase that, in the absence of substrates, self-inactivates dioxygenase activity via compound I-initiated protein oxidation. L-Trp protects against dioxygenase inactivation by reacting with compound I and retarding compound II reduction to suppress peroxidase turnover. Catalytic cycle of hemeperoxidase enzymes, and enzyme peroxidase mechanism, overview
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additional information
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the enzyme catalyzes the oxidation of indole by H2O2, with generation of 2- and 3-oxoindole as the major products, in the absence of O2 and reducing agents and is not inhibited by superoxide dismutase or hydroxyl radical scavengers, although it is strongly inhibited by L-Trp. IDO inserts oxygen into indole in a reaction that is mechanistically analogous to the peroxide shunt pathway of cytochrome P450
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additional information
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IDO2 enzyme may be involved in immune evasion by tumours
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additional information
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IDO2 enzyme may be involved in immune evasion by tumours
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additional information
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Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
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additional information
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Trp suppresses 2,3-dioxygenase induction by IFN-gamma at the transcriptional level
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