Protein Variants | Comment | Organism |
---|---|---|
R231L | site-directed mutagenesis, altered structure compared to wild-type, inactive mutant | Homo sapiens |
T379A | site-directed mutagenesis, altered structure compared to wild-type revealing a weaker A379-Trp interaction and altered active site conformation, overview. The T379A mutation results in a 25fold reduction in the activity toward L-Trp, as evidenced by the 5fold reduction in kcat, compared to the wild-type enzyme | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.023 | - |
L-tryptophan | recombinant wild-type enzyme, pH 7.4, 25°C | Homo sapiens | |
0.112 | - |
L-tryptophan | recombinant mutant T379A, pH 7.4, 25°C | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | ferric heme | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-tryptophan + O2 | Homo sapiens | - |
N-formyl-D-kynurenine | - |
? | |
L-tryptophan + O2 | Homo sapiens | - |
N-formyl-L-kynurenine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P14902 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-tryptophan + O2 | - |
Homo sapiens | N-formyl-D-kynurenine | - |
? | |
L-tryptophan + O2 | - |
Homo sapiens | N-formyl-L-kynurenine | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | conformational dynamics in three-dimensional structure of hIDO, and structure-function analysis, modeling using structures PDB IDs 2D0T, 2NW8, and 2X67, overview. Flexible active site loop in human indoleamine 2,3-dioxygenase | Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.87 | - |
L-tryptophan | recombinant mutant T379A, pH 7.4, 25°C | Homo sapiens | |
4.3 | - |
L-tryptophan | recombinant wild-type enzyme, pH 7.4, 25°C | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | ferric heme | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | conformational dynamics in three-dimensional structure of hIDO, and structure-function analysis, modeling using structures PDB IDs 2D0T, 2NW8, and 2X67, overview. Flexible active site loop in human indoleamine 2,3-dioxygenase | Homo sapiens |