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

BRENDA support

Literature summary for 1.13.11.52 extracted from

  • Thomas, S.R.; Terentis, A.C.; Cai, H.; Takikawa, O.; Levina, A.; Lay, P.A.; Freewan, M.; Stocker, R.
    Post-translational regulation of human indoleamine 2,3-dioxygenase activity by nitric oxide (2007), J. Biol. Chem., 282, 23778-23787.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
COS-7 cells expressing active human IDO Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
NO inhibits activity reversibly by binding to the active site heme to trap the enzyme as an inactive nitrosyl-FeII enzyme adduct with Trp bound and O2 displaced. Reversible inhibition by NO may represent an important mechanism in controlling the immune regulatory actions of IDO Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + O2 Homo sapiens plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan that contributes to immune suppression and tolerance N-formyl-L-kynurenine
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

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 plays an important role in the immune response by catalyzing the oxidative degradation of L-tryptophan that contributes to immune suppression and tolerance Homo sapiens N-formyl-L-kynurenine
-
?

Cofactor

Cofactor Comment Organism Structure
heme
-
Homo sapiens