EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.11.52 | expression of Ag-HisTDO in Escherichia coli | Anopheles gambiae |
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 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.52 | 0.6 | - |
L-tryptophan | - |
Anopheles gambiae |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.13.11.52 | 47900 | - |
x * 47900, SDS-PAGE | Anopheles gambiae |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.52 | Anopheles gambiae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.13.11.52 | - |
Anopheles gambiae |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.13.11.52 | 1.43 | - |
- |
Anopheles gambiae |
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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.13.11.52 | ? | x * 47900, SDS-PAGE | Anopheles gambiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.52 | TDO | - |
Anopheles gambiae |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.13.11.52 | 8 | - |
- |
Anopheles gambiae |
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 |
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 |