Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

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.
    View publication on PubMed

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