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Literature summary extracted from

  • Lu, C.; Lin, Y.; Yeh, S.R.
    Spectroscopic studies of ligand and substrate binding to human indoleamine 2,3-dioxygenase (2010), Biochemistry, 49, 5028-5034.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.52
-
 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.52 cyanide prebinding of cyanide to the enzyme facilitates L-Trp binding by 22fold but retards its dissociation by 2fold, indicating that cyanide binding to the heme iron introduces structural changes to the protein matrix allowing faster access of the substrate to the active site and slower dissociation from it. Prebinding of L-Trp to the enzyme retards cyanide binding by about 13fold Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.52
-
 Homo sapiens

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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.52 IDO
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.52 heme
-
 Homo sapiens