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Literature summary extracted from

  • Paglino, A.; Lombardo, F.; Arca, B.; Rizzi, M.; Rossi, F.
    Purification and biochemical characterization of a recombinant Anopheles gambiae tryptophan 2,3-dioxygenase expressed in Escherichia coli (2008), Insect Biochem. Mol. Biol., 38, 871-876.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.52 expression of Ag-HisTDO in Escherichia coli Anopheles gambiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.52 3-hydroxykynurenine 0.1 mM, 89.8% inhibition Anopheles gambiae
1.13.11.52 5-hydroxyindole acetic acid 1 mM, 61.5% inhibition Anopheles gambiae
1.13.11.52 5-hydroxytryptamine 1 mM, 82.3% inhibition Anopheles gambiae
1.13.11.52 5-hydroxytryptophan 1 mM, 78.6% inhibition Anopheles gambiae
1.13.11.52 Kynurenic acid 0.1 mM, 57.2% inhibition. 1 mM, 99.4% inhibition Anopheles gambiae
1.13.11.52 L-kynurenine 0.1 mM, 17.7% inhibition. 1 mM, 93.6% inhibition Anopheles gambiae
1.13.11.52 NADH 0.1 mM, 51.3% inhibition Anopheles gambiae
1.13.11.52 xanthurenic acid 0.1 mM, 50.6% inhibition. 1 mM, 96.2% inhibition Anopheles gambiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.52 0.6
-
L-tryptophan
-
Anopheles gambiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.52 47900
-
x * 47900, SDS-PAGE Anopheles gambiae

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 Anopheles gambiae tryptophan 2,3-dioxygenase is the only enzyme able to initiate L-tryptophan degradation through the kynurenine pathway N-formyl-L-kynurenine
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.52 Anopheles gambiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.52
-
Anopheles gambiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.11.52 1.43
-
-
Anopheles gambiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.52 L-tryptophan + O2
-
Anopheles gambiae N-formyl-L-kynurenine
-
?
1.13.11.52 L-tryptophan + O2 tryptophan 2,3-dioxygenase is the only enzyme able to initiate L-tryptophan degradation through the kynurenine pathway Anopheles gambiae N-formyl-L-kynurenine
-
?

Subunits

EC Number Subunits Comment Organism
1.13.11.52 ? x * 47900, SDS-PAGE Anopheles gambiae

Synonyms

EC Number Synonyms Comment Organism
1.13.11.52 TDO
-
Anopheles gambiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.52 2.03
-
L-tryptophan
-
Anopheles gambiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.52 8
-
-
Anopheles gambiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.13.11.52 6.5 9 pH 6.5: about 50% of maximal activity, pH 9.0: about 70% of maximal activity Anopheles gambiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.52 heme Ag-HisTDO is purified in its heme-ferric form. The prosthetic group can be fully converted into the heme-ferrous form by treatment with sodium dithionite Anopheles gambiae