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Indoleamine 2,3-dioxygenase

Indoleamine-pyrrole 2,3 dioxygenase
PDB rendering based on 2d0t.
Available structures: 2d0t, 2d0u
Symbol(s) INDO; CD107B; IDO
External IDs OMIM: 147435 MGI: 96416 Homologene: 48082
EC number
RNA expression pattern

More reference expression data

Human Mouse
Entrez 3620 15930
Ensembl ENSG00000131203 ENSMUSG00000031551
Uniprot P14902 P28776
Refseq NM_002164 (mRNA)
NP_002155 (protein)
NM_008324 (mRNA)
NP_032350 (protein)
Location Chr 8: 39.89 - 39.91 Mb Chr 8: 26.05 - 26.06 Mb
Pubmed search [1] [2]

Indoleamine-pyrrole 2,3-dioxygenase (IDO or INDO EC is an immunomodulatory enzyme secreted by some alternatively activated macrophages and other immunoregulatory cells (also used as an immune subversion strategy by many tumors).

Gamma-interferon (IFNG; MIM 147570) has an antiproliferative effect on many tumor cells and inhibits intracellular pathogens such as Toxoplasma and Chlamydia, at least partly because of the induction of indoleamine 2,3-dioxygenase (INDO; EC This enzyme catalyzes the degradation of the essential amino acid L-tryptophan to N-formylkynurenine.[supplied by OMIM][1]

IDO is the first and rate limiting enzyme of Tryptophan catabolism through Kynurenine pathway, thus causing depletion of tryptophan which can cause halted growth of microbes as well as T cells.

It catalyzes conversion of L-tryptophan to N-formylkynurenine.


  1. ^ Entrez Gene: INDO indoleamine-pyrrole 2,3 dioxygenase.

Further reading

  • Grohmann U, Fallarino F, Puccetti P (2004). "Tolerance, DCs and tryptophan: much ado about IDO.". Trends Immunol. 24 (5): 242-8. PMID 12738417.
  • Takikawa O (2005). "Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism.". Biochem. Biophys. Res. Commun. 338 (1): 12-9. doi:10.1016/j.bbrc.2005.09.032. PMID 16176799.
  • Puccetti P (2007). "On watching the watchers: IDO and type I/II IFN.". Eur. J. Immunol. 37 (4): 876-9. doi:10.1002/eji.200737184. PMID 17393386.
  • Kadoya A, Tone S, Maeda H, et al. (1992). "Gene structure of human indoleamine 2,3-dioxygenase.". Biochem. Biophys. Res. Commun. 189 (1): 530-6. PMID 1449503.
  • Kamimura S, Eguchi K, Yonezawa M, Sekiba K (1991). "Localization and developmental change of indoleamine 2,3-dioxygenase activity in the human placenta.". Acta Med. Okayama 45 (3): 135-9. PMID 1716396.
  • 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.
  • Tone S, Takikawa O, Habara-Ohkubo A, et al. (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.
  • Werner-Felmayer G, Werner ER, Fuchs D, et al. (1990). "Tumour necrosis factor-alpha and lipopolysaccharide enhance interferon-induced tryptophan degradation and pteridine synthesis in human cells.". Biol. Chem. Hoppe-Seyler 370 (9): 1063-9. PMID 2482041.
  • Carlin JM, Borden EC, Byrne GI (1989). "Interferon-induced indoleamine 2,3-dioxygenase activity inhibits Chlamydia psittaci replication in human macrophages.". J. Interferon Res. 9 (3): 329-37. PMID 2501398.
  • Kobayashi K, Hayashi K, Sono M (1989). "Effects of tryptophan and pH on the kinetics of superoxide radical binding to indoleamine 2,3-dioxygenase studied by pulse radiolysis.". J. Biol. Chem. 264 (26): 15280-3. PMID 2549057.
  • Daley-Yates PT, Powell AP, Smith LL (1989). "Pulmonary indoleamine 2,3-dioxygenase activity and its significance in the response of rats, mice, and rabbits to oxidative stress.". Toxicol. Appl. Pharmacol. 96 (2): 222-32. PMID 2848333.
  • Najfeld V, Menninger J, Muhleman D, et al. (1993). "Localization of indoleamine 2,3-dioxygenase gene (INDO) to chromosome 8p12-->p11 by fluorescent in situ hybridization.". Cytogenet. Cell Genet. 64 (3-4): 231-2. PMID 8404046.
  • Burkin DJ, Kimbro KS, Barr BL, et al. (1993). "Localization of the human indoleamine 2,3-dioxygenase (IDO) gene to the pericentromeric region of human chromosome 8.". Genomics 17 (1): 262-3. PMID 8406467.
  • Malina HZ, Martin XD (1996). "Indoleamine 2,3-dioxygenase: antioxidant enzyme in the human eye.". Graefes Arch. Clin. Exp. Ophthalmol. 234 (7): 457-62. PMID 8817290.
  • Munn DH, Zhou M, Attwood JT, et al. (1998). "Prevention of allogeneic fetal rejection by tryptophan catabolism.". Science 281 (5380): 1191-3. PMID 9712583.
  • Takikawa O, Littlejohn TK, Truscott RJ (2001). "Indoleamine 2,3-dioxygenase in the human lens, the first enzyme in the synthesis of UV filters.". Exp. Eye Res. 72 (3): 271-7. doi:10.1006/exer.2000.0951. PMID 11180976.
  • Kudo Y, Boyd CA (2001). "The role of L-tryptophan transport in L-tryptophan degradation by indoleamine 2,3-dioxygenase in human placental explants.". J. Physiol. (Lond.) 531 (Pt 2): 417-23. PMID 11230514.
  • Terentis AC, Thomas SR, Takikawa O, et al. (2002). "The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions.". J. Biol. Chem. 277 (18): 15788-94. doi:10.1074/jbc.M200457200. PMID 11867636.
  • Kvirkvelia N, Vojnovic I, Warner TD, et al. (2002). "Placentally derived prostaglandin E2 acts via the EP4 receptor to inhibit IL-2-dependent proliferation of CTLL-2 T cells.". Clin. Exp. Immunol. 127 (2): 263-9. PMID 11876748.
  • Sedlmayr P, Blaschitz A, Wintersteiger R, et al. (2002). "Localization of indoleamine 2,3-dioxygenase in human female reproductive organs and the placenta.". Mol. Hum. Reprod. 8 (4): 385-91. PMID 11912287.
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Indoleamine_2,3-dioxygenase". A list of authors is available in Wikipedia.
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