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
-
immunotherapy
- heme
- serotonin
-
checkpoint
- l-trp
- n-formylkynurenine
-
quinolinic
-
tolerogenic
-
3-monooxygenase
-
3,4-dioxygenase
-
heme-containing
-
2,3-dioxygenase-1
-
tryptophan-degrading
- 3-hydroxyanthranilate
- indoleamine-2,3-dioxygenase
-
picolinic
-
tryptophan-catabolizing
-
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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Subunits
Subunits on EC 1.13.11.11 - tryptophan 2,3-dioxygenase
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tetramer
additional information
tetramer
holo-hTDO, dimer of dimers, in which the two C-shape dimers (AB and CD) are clamped perpendicularly to each other to form a tight tetramer
tetramer
4 * 48000, high tryptophan levels stabilize the active tetrameric conformation of the enzyme through binding noncatalytic exosites. The lack of tryptophan binding in the exosites destabilizes the tetramer into inactive monomers and dimers
hTDO must form an oligomer to exhibit activity. Active site structure, overview
additional information
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hTDO must form an oligomer to exhibit activity. Active site structure, overview