|Gene:||INDO||Accession Number: G-11449 (MetaCyc)|
Synonyms: IDO, IDO1
Species: Homo sapiens
The apparent molecular mass of the enzyme was determined by SDS-PAGE [Littlejohn03] . In mammals this monomeric enzyme is present in most tissues with the exception of liver, which contains tryptophan 2,3-dioxygenase. Catalytic differences between these two enzymes have been shown [Basran08]. The enzyme has been reviewed in [Rafice09] and [King07].
Recombinant enzyme has been cloned, expressed in Saccharomyces cerevisiae [Vottero06] and Escherichia coli, [Littlejohn03] and purified. Differences between the recombinant human and mouse enzymes have been studied [Austin09].
The crystal structure of this enzyme has been determined [Sugimoto06].
A third enzyme indoleamine 2,3-dioxygenase-2 has been described in mouse. It is expressed in liver, kidney and in the reproductive system. It differs from this enzyme in its selectivity for some inhibitors. Its biological function remains to be determined [Ball09].
|Map Position: [39,771,328 -> 39,785,950]|
Molecular Weight of Polypeptide: 45.326 kD (from nucleotide sequence), 45.0 kD (experimental)
Unification Links: ArrayExpress:P14902 , Entrez-gene:3620 , Mint:MINT-1414454 , PhosphoSite:P14902 , Pride:P14902 , Protein Model Portal:P14902 , SMR:P14902 , String:9606.ENSP00000253513 , UniProt:P14902
Enzymatic reaction of: indoleamine 2,3-dioxygenase
Synonyms: indoleamine-pyrrole 2,3-dioxygenase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
In Pathways: tryptophan degradation III (eukaryotic) , tryptophan degradation XI (mammalian, via kynurenine) , NAD biosynthesis II (from tryptophan) , tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde
Austin09: Austin CJ, Astelbauer F, Kosim-Satyaputra P, Ball HJ, Willows RD, Jamie JF, Hunt NH (2009). "Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties." Amino Acids 36(1);99-106. PMID: 18274832
Basran08: Basran J, Rafice SA, Chauhan N, Efimov I, Cheesman MR, Ghamsari L, Raven EL (2008). "A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase." Biochemistry 47(16);4752-60. PMID: 18370401
Dai90: Dai W, Gupta SL (1990). "Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA." Biochem Biophys Res Commun 168(1);1-8. PMID: 2109605
Littlejohn03: Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ (2003). "Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase." J Biol Chem 278(32);29525-31. PMID: 12766158
Rafice09: Rafice SA, Chauhan N, Efimov I, Basran J, Raven EL (2009). "Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase." Biochem Soc Trans 37(Pt 2);408-12. PMID: 19290871
Sugimoto06: Sugimoto H, Oda S, Otsuki T, Hino T, Yoshida T, Shiro Y (2006). "Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase." Proc Natl Acad Sci U S A 103(8);2611-6. PMID: 16477023
Tone90: Tone S, Takikawa O, Habara-Ohkubo A, Kadoya A, Yoshida R, Kido R (1990). "Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA." Nucleic Acids Res 18(2);367. PMID: 2326172
Vottero06: Vottero E, Mitchell DA, Page MJ, MacGillivray RT, Sadowski IJ, Roberge M, Mauk AG (2006). "Cytochrome b(5) is a major reductant in vivo of human indoleamine 2,3-dioxygenase expressed in yeast." FEBS Lett 580(9);2265-8. PMID: 16574111
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