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

BRENDA support

Literature summary for 1.13.11.52 extracted from

  • Yanagisawa, S.; Kayama, K.; Hara, M.; Sugimoto, H.; Shiro, Y.; Ogura, T.
    UV Resonance Raman characterization of a substrate bound to human indoleamine 2,3-dioxygenase 1 (2019), Biophys. J., 117, 706-716 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.52

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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.
L-tryptophan + O2
-
 Homo sapiens N-formyl-L-kynurenine
-
 ?
L-tryptophan + O2 the reaction involves cleavage of the C2=C3 double bond in the Trp indole ring and insertion of two atomic oxygens from the iron-bound O2 into the indole 2 and 3 position Homo sapiens N-formyl-L-kynurenine
-
 ?

Synonyms

Synonyms Comment Organism
IDO
-
 Homo sapiens
indoleamine 2,3-dioxygenase 1
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme heme enzyme. The presence of the diatomic ligand at the heme sixth coordination site in the ternary complex significantly alters the mobility and electronic structure of Trp, most likely resulting in the C2=C3 double bond cleavage in the enzymatic reaction Homo sapiens