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Literature summary for 1.13.11.52 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
Search for more literature for 1.13.11.52

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
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

Localization Comment Organism GeneOntology No. Textmining

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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

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
-
 ?

Synonyms

Synonyms Comment Organism
IDO
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme
-
 Homo sapiens