PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31870154-2 2020 This 2,3-dioxygenative cleavage of the indole ring of tryptophan with dioxygen is mediated by two heme enzymes, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO), during its conversion to N-formylkynurenine in the first and rate-limiting step of kynurenine pathway. Oxygen 9-17 tryptophan 2,3-dioxygenase Homo sapiens 112-138 33615851-7 2022 The NIR-based device used in this study estimates effective changes in TO in terms of oxy-, deoxy-, total hemoglobin, and oxygen saturation. Oxygen 122-128 tryptophan 2,3-dioxygenase Homo sapiens 71-73 31870154-2 2020 This 2,3-dioxygenative cleavage of the indole ring of tryptophan with dioxygen is mediated by two heme enzymes, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO), during its conversion to N-formylkynurenine in the first and rate-limiting step of kynurenine pathway. Oxygen 9-17 tryptophan 2,3-dioxygenase Homo sapiens 140-143 27909919-1 2017 It is well established that there are two different classes of enzymes-tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO)-that catalyse the O2-dependent oxidation of L-tryptophan to N-formylkynurenine. Oxygen 160-162 tryptophan 2,3-dioxygenase Homo sapiens 63-97 28715185-1 2017 The human heme enzyme tryptophan 2,3-dioxygenase (hTDO) catalyzes the insertion of dioxygen into its cognate substrate, l-tryptophan (l-Trp). Oxygen 37-45 tryptophan 2,3-dioxygenase Homo sapiens 50-54 27909919-1 2017 It is well established that there are two different classes of enzymes-tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO)-that catalyse the O2-dependent oxidation of L-tryptophan to N-formylkynurenine. Oxygen 160-162 tryptophan 2,3-dioxygenase Homo sapiens 99-102 27801576-5 2016 Complexes 1 and 2 decompose in the presence of O2 to yield the corresponding sulfinic acid (RSO2H) products, thereby emulating the reactivity of the TDO enzymes and related complexes. Oxygen 47-49 tryptophan 2,3-dioxygenase Homo sapiens 149-152 27951658-1 2016 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of l-tryptophan (l-Trp) in biological systems. Oxygen 117-119 tryptophan 2,3-dioxygenase Homo sapiens 38-64 27951658-1 2016 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of l-tryptophan (l-Trp) in biological systems. Oxygen 117-119 tryptophan 2,3-dioxygenase Homo sapiens 66-69 27801576-7 2016 Treatment of the TDO models with nitric oxide (NO)-a well-established surrogate of O2-led to a mixture of high-spin and low-spin {FeNO}7 species at low temperature (-70 C), as indicated by electron paramagnetic resonance (EPR) spectroscopy. Oxygen 83-85 tryptophan 2,3-dioxygenase Homo sapiens 17-20 26511316-3 2015 This is an O2-dependent process and catalyzed by indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase. Oxygen 11-13 tryptophan 2,3-dioxygenase Homo sapiens 81-107 27762317-2 2016 Here we report the crystal structure of human TDO (hTDO) in a ternary complex with the substrates L-Trp and O2 and in a binary complex with the product N-formylkynurenine (NFK), defining for the first time the binding modes of both substrates and the product of this enzyme. Oxygen 108-110 tryptophan 2,3-dioxygenase Homo sapiens 46-49 27762317-2 2016 Here we report the crystal structure of human TDO (hTDO) in a ternary complex with the substrates L-Trp and O2 and in a binary complex with the product N-formylkynurenine (NFK), defining for the first time the binding modes of both substrates and the product of this enzyme. Oxygen 108-110 tryptophan 2,3-dioxygenase Homo sapiens 51-55 27072164-1 2016 Tryptophan-2, 3-dioxygenase (TDO) is a heme-containing protein catalyzing the first reaction in the kynurenine pathway, which incorporates oxygen into the indole moiety of tryptophan and catalyzes it into kynurenine (KYN). Oxygen 18-24 tryptophan 2,3-dioxygenase Homo sapiens 29-32 25996254-1 2015 L-Tryptophan 2,3-dioxygenase (TDO) is a protoheme-containing enzyme that catalyzes the production of N-formylkynurenine by inserting O2 into the pyrrole ring of L-tryptophan. Oxygen 133-135 tryptophan 2,3-dioxygenase Homo sapiens 0-28 25996254-1 2015 L-Tryptophan 2,3-dioxygenase (TDO) is a protoheme-containing enzyme that catalyzes the production of N-formylkynurenine by inserting O2 into the pyrrole ring of L-tryptophan. Oxygen 133-135 tryptophan 2,3-dioxygenase Homo sapiens 30-33 25996254-3 2015 In this study, the O2 insertion reaction catalyzed by Pseudomonas TDO (PaTDO) was examined using a heme-modification approach, which allowed us to draw a quantitative correlation between the inductive electronic effects of the heme substituents and the substituent-induced changes in the functional behaviors of the ferrous-oxy form. Oxygen 19-21 tryptophan 2,3-dioxygenase Homo sapiens 66-69 22616860-7 2012 In the present mini-review, recent developments in our understanding of how the TDO class of enzymes use activated molecular oxygen to break the indole ring are discussed. Oxygen 125-131 tryptophan 2,3-dioxygenase Homo sapiens 80-83 20361220-3 2010 Previous studies suggested that the first step of the dioxygenase reaction involves the deprotonation of the indoleamine group of the substrate by an evolutionarily conserved distal histidine residue in TDO and the heme-bound dioxygen in IDO. Oxygen 54-62 tryptophan 2,3-dioxygenase Homo sapiens 203-206 20361220-9 2010 The results reveal the subtle differences between the TDO and IDO reactions and highlight the importance of protein matrix in modulating stereoelectronic factors for oxygen activation and the stabilization of both transition and intermediate states. Oxygen 166-172 tryptophan 2,3-dioxygenase Homo sapiens 54-57 19275153-1 2009 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme enzymes that catalyze the O(2)-dependent oxidation of L-tryptophan to N-formyl-kynurenine. Oxygen 106-110 tryptophan 2,3-dioxygenase Homo sapiens 38-64 19275153-1 2009 Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme enzymes that catalyze the O(2)-dependent oxidation of L-tryptophan to N-formyl-kynurenine. Oxygen 106-110 tryptophan 2,3-dioxygenase Homo sapiens 66-69 19250632-1 2009 It is well established that ozone as well as oxygen activated by tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase cleave the 2,3-C=C bond of the indole ring of tryptophan to produce N-formylkynurenine. Oxygen 45-51 tryptophan 2,3-dioxygenase Homo sapiens 65-91 19021508-1 2008 The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathway. Oxygen 38-46 tryptophan 2,3-dioxygenase Homo sapiens 18-21 19021508-2 2008 Recent crystallographic and biochemical analyses of TDO and IDO have greatly aided our understanding of the mechanisms employed by these enzymes in the binding and activation of dioxygen and tryptophan. Oxygen 178-186 tryptophan 2,3-dioxygenase Homo sapiens 52-55