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

BRENDA support

Literature summary for 1.13.11.52 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
Search for more literature for 1.13.11.52

Protein Variants

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 [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

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens P14902
-
-

Substrates and Products (Substrate)

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

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

Turnover Number [1/s]

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

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

Cofactor

Cofactor Comment Organism Structure
heme ferric heme Homo sapiens

General Information

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