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.

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

ECTree

     1 Oxidoreductases

         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

             1.13.11 With incorporation of two atoms of oxygen

                1.13.11.11 tryptophan 2,3-dioxygenase

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Results	in table
2	Activating Compound
9810	AA Sequence
2	Application
14	Cloned(Commentary)
18	Cofactor
4	Crystallization (Commentary)
1191	Disease/ Diagnostics
4	Expression
54	General Information
4	General Stability
135	IC50 Value
146	Inhibitors
26	KM Value [mM]
1	Localization
4	Metals/Ions
3	Molecular Weight [Da]
39	Natural Substrates/ Products (Substrates)
55	Organism
9	Pathway
85	PDB ID
9	pH Optimum
3	Posttranslational Modification
24	Protein Variants
5	Purification (Commentary)
3	Reaction
45	Reference
63	Source Tissue
60	Substrates and Products (Substrate)
9	Subunits
64	Synonyms
1	Systematic Name
13	Temperature Optimum [°C]
8	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.13.11.11 - tryptophan 2,3-dioxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified enzyme in a ternary complex with the substrates L-Trp and O2 and in a binary complex with the product N-formylkynurenine, under-oil microbatch method under anaerobic conditions, mixing of 0.003 ml of 45 mg/ml protein in 50 mM Tris, pH 8.0, containing 150 mM NaCl and 10 mM L-Trp, and reduced with 2-fold molar excess of sodium dithionite, with 0.003-0.006 ml of precipitannt solution containing 50 mM sodium citrate, pH 5.6, 5% w/v PEG 3350, and 2% w/v Tacsimate, pH 5.0, X-ray diffraction structure determination and analysis at 2.5 A and 2.44 A resolution, respectively. Crystals of the Trp-bound binary complex are soaked in an O2-saturated precipitant solution supplemented with 20% v/v ethylene glycol at room temperature

Homo sapiens

P48775

743821

purified full-length and truncated enzyme variants without heme cofactor, hanging drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 100 mM Tris–HCl, pH 8.0, with 0.001 ml of reservoir solution containing 0.1 M sodium cacodylate, pH 6.0-6.5, 6-10% w/v MPEG 5000, and 10% v/v 2-propanol, addition of hexammine cobalt(III) chloride improves the diffraction significantly, 16°C, X-ray diffraction structure determination and analysis at 2.90 A resolution

Homo sapiens

P48775

743760

crystal structure of the enzyme in complex with L-kynurenine

2 entries

crystal structure of the enzyme in complex with L-kynurenine

Xanthomonas campestris

-

765204

crystal structure of the enzyme in complex with L-kynurenine

Xanthomonas campestris pv. campestris

Q8PDA8

765204