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

BRENDA support

Literature summary extracted from

  • Alvarez, L.; Lewis-Ballester, A.; Roitberg, A.; Estrin, D.A.; Yeh, S.R.; Marti, M.A.; Capece, L.
    Structural study of a flexible active site loop in human indoleamine 2,3-dioxygenase and its functional implications (2016), Biochemistry, 55, 2785-2793 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.52 R231L site-directed mutagenesis, altered structure compared to wild-type, inactive mutant Homo sapiens
1.13.11.52 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.52 0.023
-
 L-tryptophan recombinant wild-type enzyme, pH 7.4, 25°C Homo sapiens
1.13.11.52 0.112
-
 L-tryptophan recombinant mutant T379A, pH 7.4, 25°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.52 Fe2+ ferric heme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.52 D-tryptophan + O2 Homo sapiens
-
 N-formyl-D-kynurenine
-
 ?
1.13.11.52 L-tryptophan + O2 Homo sapiens
-
 N-formyl-L-kynurenine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.52 Homo sapiens P14902
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.52 D-tryptophan + O2
-
 Homo sapiens N-formyl-D-kynurenine
-
 ?
1.13.11.52 L-tryptophan + O2
-
 Homo sapiens N-formyl-L-kynurenine
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.52 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.52 25
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.52 0.87
-
 L-tryptophan recombinant mutant T379A, pH 7.4, 25°C Homo sapiens
1.13.11.52 4.3
-
 L-tryptophan recombinant wild-type enzyme, pH 7.4, 25°C Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.52 7.4
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.52 heme ferric heme Homo sapiens

General Information

EC Number General Information Comment Organism
1.13.11.52 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