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Literature summary for 1.13.11.52 extracted from

  • Sugimoto, H.; Oda, S.; Otsuki, T.; Hino, T.; Yoshida, T.; Shiro, Y.
    Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase (2006), Proc. Natl. Acad. Sci. USA, 103, 2611-2616.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.52

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method, crystal structure of the enzyme complexed with the ligand inhibitor 4-phenylimidazole and cyanide and cyanide at resolutions of 2.3 and 3.4 A respectively Homo sapiens

Protein Variants

Protein Variants Comment Organism
F226A drastically reduced the dioxygenase activity Homo sapiens
F227A drastically reduced the dioxygenase activity Homo sapiens
R231A drastically reduced the dioxygenase activity Homo sapiens
S263A activity is reduced to 15% Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
4-phenylimidazole
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Trp + O2 proposed reaction mechanism involves the proton abstraction by iron-bound dixoygen. The O-O bond is precisely controlled by the heme proximal and distal environment and is not cleaved before the incorporation of both oxygen atoms into the substrate Homo sapiens L-formylkynurenine
-
 ?

Synonyms

Synonyms Comment Organism
IDO
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme none of the polar amino acid residues in the distal heme pocket are essential for activity. The O-O bond is precisely controlled by the heme proximal and distal environment and is not cleaved before the incorporation of both oxygen atoms into the substrate Homo sapiens