1.13.11.11: tryptophan 2,3-dioxygenase
This is an abbreviated version!
For detailed information about tryptophan 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.11
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1.13.11.11
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indoleamine
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kynurenine
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immunotherapy
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heme
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serotonin
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checkpoint
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l-trp
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n-formylkynurenine
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quinolinic
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tolerogenic
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3-monooxygenase
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3,4-dioxygenase
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heme-containing
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2,3-dioxygenase-1
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tryptophan-degrading
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3-hydroxyanthranilate
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indoleamine-2,3-dioxygenase
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picolinic
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tryptophan-catabolizing
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pyrrolase
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3-hydroxykynurenine
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medicine
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drug development
- 1.13.11.11
- indoleamine
- kynurenine
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immunotherapy
- heme
- serotonin
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checkpoint
- l-trp
- n-formylkynurenine
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quinolinic
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tolerogenic
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3-monooxygenase
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3,4-dioxygenase
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heme-containing
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2,3-dioxygenase-1
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tryptophan-degrading
- 3-hydroxyanthranilate
- indoleamine-2,3-dioxygenase
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picolinic
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tryptophan-catabolizing
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pyrrolase
- 3-hydroxykynurenine
- medicine
- drug development
Reaction
Synonyms
33737, BRAFLDRAFT_210874, C28H8.11, EC 1.11.1.4, hTDO, IDO-1, IDO-2, IDO1, IDO2, indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2, TDO, TDO2, TDOa, tryptophan 2,3-dioxygenase, tryptophan 2,3-dioxygenase 2, tryptophan 2,3-dioxygenase-2, tryptophan-2,3-dioxygenase, v1g157887, vCG5163, XcTDO
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Substrates Products
Substrates Products on EC 1.13.11.11 - tryptophan 2,3-dioxygenase
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REACTION DIAGRAM
L-tryptophan + O2
3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid
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5-fluoro-L-tryptophan + O2
5-fluoro-N-formyl-L-kynurenine
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5-fluoro-L-tryptophan + O2
5-fluoro-N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
kinetic and spectroscopic characterization of the catalytic ternary complex of tryptophan 2,3-dioxygenase
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L-tryptophan + O2
N-formyl-L-kynurenine
kinetic and spectroscopic characterization of the catalytic ternary complex of tryptophan 2,3-dioxygenase
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L-tryptophan + O2
N-formyl-L-kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
cleavage of the C2-C3 bond in the indole moiety of L-Trp and incorporation of one oxygen molecule
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L-tryptophan + O2
N-formyl-L-kynurenine
the enzyme has broad substrate specificity for various indoleamines such as L-tryptophan and serotonin. It catalyzes the oxidation of the pyrrole ring of tryptophan to form N-formylkynurenine, which is later metabolized to formic acid and kynurenine
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L-tryptophan + O2
N-formyl-L-kynurenine
the enzyme has broad substrate specificity for various indoleamines such as L-tryptophan and serotonin. It catalyzes the oxidation of the pyrrole ring of tryptophan to form N-formylkynurenine, which is later metabolized to formic acid and 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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enzyme TDO is highly substrate-specific for L-Trp and the related derivatives 6-fluoro-Trp and 5-fluoro-Trp
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additional information
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enzyme TDO is highly substrate-specific for L-Trp and the related derivatives 6-fluoro-Trp and 5-fluoro-Trp
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additional information
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no activity with D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
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additional information
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substrate recognition and binding structures, overview. The EG segment in hTDO plays a critical role in promoting NFK release, thereby allowing Trp binding during multiple turnover
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additional information
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substrate recognition and binding structures, overview. The EG segment in hTDO plays a critical role in promoting NFK release, thereby allowing Trp binding during multiple turnover
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additional information
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in mouse liver homogenate, TDO activity is five times lower for D-Trp than that for L-Trp. L-Trp is the preferred substrate for nicotinamide synthesis because L-Trp metabolism is more efficient than D-Trp in mice
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additional information
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the kcat of tryptophan-2,3-dioxygenase (TDO) is 10 times lower for D-Trp than that for L-Trp in vitro
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additional information
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in mouse liver homogenate, TDO activity is five times lower for D-Trp than that for L-Trp. L-Trp is the preferred substrate for nicotinamide synthesis because L-Trp metabolism is more efficient than D-Trp in mice
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additional information
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the kcat of tryptophan-2,3-dioxygenase (TDO) is 10 times lower for D-Trp than that for L-Trp in vitro
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additional information
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no activity witth D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
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additional information
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no activity witth D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
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