Literature summary extracted from
Huang, W.; Gong, Z.; Li, J.; Ding, J.
Crystal structure of Drosophila melanogaster tryptophan 2,3-dioxygenase reveals insights into substrate recognition and catalytic mechanism (2013), J. Struct. Biol., 181, 291-299.
Application
EC Number |
Application |
Comment |
Organism |
---|
1.13.11.52 |
medicine |
tryptophan 2,3-dioxygenase is considered as a drug target for cancer immunotherapy |
Drosophila melanogaster |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.13.11.52 |
expression of His6-tagged TDO in Escherichia coli strain BL21 (DE3) |
Drosophila melanogaster |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.13.11.52 |
purified His6-tagged recombinant enzyme in complex with heme, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM Tris, pH 8.0, and 200 mM NaCl, with reservoir solution containing 0.1 M HEPES, pH 7.0, and 1.1 M sodium malonate, at equal volumes, 20°C, X-ray diffraction structure determination and analysis at 2.7 A resolution |
Drosophila melanogaster |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.13.11.52 |
Fe2+ |
heme-scontaining enzyme |
Drosophila melanogaster |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.13.11.52 |
L-tryptophan + O2 |
Drosophila melanogaster |
- |
N-formyl-L-kynurenine |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.13.11.52 |
Drosophila melanogaster |
P20351 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.13.11.52 |
recombinant His6-tagged TDO from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration to homogeneity |
Drosophila melanogaster |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
1.13.11.52 |
L-tryptophan + O2 = N-formyl-L-kynurenine |
substrate recognition and catalytic mechanism, overview |
Drosophila melanogaster |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.13.11.52 |
L-tryptophan + O2 |
- |
Drosophila melanogaster |
N-formyl-L-kynurenine |
- |
? |
|
1.13.11.52 |
L-tryptophan + O2 |
enzyme shows induced-fit mechanism to bind L-Trp, two conserved but flexible loops undergo conformational changes, converting the active site from an open conformation to a closed conformation, key residues involved in recognition and binding of the heme and the substrate, Molecular modeling and dynamics simulation, overview |
Drosophila melanogaster |
N-formyl-L-kynurenine |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.13.11.52 |
tetramer |
the enzme consists of an N-terminal segment, a large domain and a small domain, and assumes a tetrameric architecture. DmTDO contains two major insertion sequences: one forms part of the heme-binding site and the other forms a large portion of the small domain |
Drosophila melanogaster |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.13.11.52 |
TDO |
- |
Drosophila melanogaster |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.13.11.52 |
heme |
DmTDO contains two major insertion sequences: one forms part of the heme-binding site and the other forms a large portion of the small domain, bindig structure, overview |
Drosophila melanogaster |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.13.11.52 |
metabolism |
tryptophan 2,3-dioxygenase catalyzes the oxidative cleavage of the indole ring of L-tryptophan to N-formylkynurenine in the kynurenine pathway |
Drosophila melanogaster |