Indoleamine 2,3-dioxygenase 2

IDO2
Identifiers
Aliases	IDO2, INDOL1, indoleamine 2,3-dioxygenase 2
External IDs	OMIM: 612129 MGI: 2142489 HomoloGene: 48830 GeneCards: IDO2
Gene location (Human)
Chr.	Chromosome 8 (human)[1]
End	40,016,391 bp[1]
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)[2]
End	24,576,333 bp[2]
Gene ontology
Molecular function	• oxidoreductase activity; • indoleamine 2,3-dioxygenase activity; • tryptophan 2,3-dioxygenase activity; • heme binding; • dioxygenase activity; • metal ion binding;
Cellular component	• cytoplasm; • cytosol;
Biological process	• tryptophan catabolic process; • oxidation-reduction process; • immune system process; • tryptophan catabolic process to kynurenine; • 'de novo' NAD biosynthetic process from tryptophan;
	Sources:Amigo / QuickGO
Orthologs
	169355
	209176
	ENSG00000188676
	ENSMUSG00000031549
	Q6ZQW0
	Q8R0V5
	NM_194294
	NM_145949
	NP_919270
	NP_666061
	Wikidata
View/Edit Human	View/Edit Mouse

Indoleamine 2,3-dioxygenase 2 (IDO2) is a protein that in humans is encoded by the IDO2 gene.[5]

Function

IDO2 (indolamine-2,3-dioxygenase) is an enzyme with protein size of 420 amino acids (47 kDa) that is used for catabolism of tryptophan. In organisms, other enzymes participate in L-tryptophan cleavage, namely IDO1 and TDO. Despite of IDO1 and IDO2 are closely related enzymes originating by gene duplication and sharing high level (43%) of sequence homology,[6][7] they differentiate by their kinetics, function and expression pattern. Genes encoding IDO1 and IDO2 have similar genomic structure and are situated closely to each other on chromosome 8.[8] IDO2 is produced in a very limited type of tissues as kidney, liver or antigen presenting cells.[9] IDO2 is less active on substrates of IDO1, better catabolizing other Trp derivates as 5-methoxytryptophan. There are several isoforms in population that comes from alternative splicing.[10] As well as IDO1, IDO2 has been reported in Treg differentiation in vitro,[11] suggesting a role in tolerance maintenance. Its expression has been found in several cancers, gastric, colon or renal tumors.[12]

References

GRCh38: Ensembl release 89: ENSG00000188676 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000031549 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: Indoleamine 2,3-dioxygenase 2".
Yuasa HJ, Mizuno K, Ball HJ (July 2015). "Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable". The FEBS Journal. 282 (14): 2735–45. doi:10.1111/febs.13316. PMID 25950090. S2CID 25834690.
Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (July 2007). "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice". Gene. 396 (1): 203–13. doi:10.1016/j.gene.2007.04.010. PMID 17499941.
Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (July 2007). "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice". Gene. 396 (1): 203–13. doi:10.1016/j.gene.2007.04.010. PMID 17499941.
Merlo LM, Mandik-Nayak L (2016). "IDO2: A Pathogenic Mediator of Inflammatory Autoimmunity". Clinical Medicine Insights. Pathology. 9 (Suppl 1): 21–28. doi:10.4137/CPath.S39930. PMC 5119657. PMID 27891058.
Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC (August 2007). "Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan". Cancer Research. 67 (15): 7082–7. doi:10.1158/0008-5472.CAN-07-1872. PMID 17671174.
Metz R, Smith C, DuHadaway JB, Chandler P, Baban B, Merlo LM, Pigott E, Keough MP, Rust S, Mellor AL, Mandik-Nayak L, Muller AJ, Prendergast GC (July 2014). "IDO2 is critical for IDO1-mediated T-cell regulation and exerts a non-redundant function in inflammation". International Immunology. 26 (7): 357–67. doi:10.1093/intimm/dxt073. PMC 4432394. PMID 24402311.
Löb S, Königsrainer A, Zieker D, Brücher BL, Rammensee HG, Opelz G, Terness P (January 2009). "IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism". Cancer Immunology, Immunotherapy. 58 (1): 153–7. doi:10.1007/s00262-008-0513-6. PMID 18418598. S2CID 6199515.

Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (July 2007). "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice". Gene. 396 (1): 203–13. doi:10.1016/j.gene.2007.04.010. PMID 17499941.
Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC (August 2007). "Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan". Cancer Research. 67 (15): 7082–7. doi:10.1158/0008-5472.CAN-07-1872. PMID 17671174.
Witkiewicz AK, Costantino CL, Metz R, Muller AJ, Prendergast GC, Yeo CJ, Brody JR (May 2009). "Genotyping and expression analysis of IDO2 in human pancreatic cancer: a novel, active target". Journal of the American College of Surgeons. 208 (5): 781–7, discussion 787-9. doi:10.1016/j.jamcollsurg.2008.12.018. PMC 3176891. PMID 19476837.
Witkiewicz AK, Costantino CL, Metz R, Muller AJ, Prendergast GC, Yeo CJ, Brody JR (May 2009). "Genotyping and expression analysis of IDO2 in human pancreatic cancer: a novel, active target". Journal of the American College of Surgeons. 208 (5): 781–7, discussion 787-9. doi:10.1016/j.jamcollsurg.2008.12.018. PMC 3176891. PMID 19476837.
Huttunen R, Syrjänen J, Aittoniemi J, Oja SS, Raitala A, Laine J, Pertovaara M, Vuento R, Huhtala H, Hurme M (February 2010). "High activity of indoleamine 2,3 dioxygenase enzyme predicts disease severity and case fatality in bacteremic patients". Shock. 33 (2): 149–54. doi:10.1097/SHK.0b013e3181ad3195. PMID 19487973. S2CID 24459411.
Cetindere T, Nambiar S, Santourlidis S, Essmann F, Hassan M (February 2010). "Induction of indoleamine 2, 3-dioxygenase by death receptor activation contributes to apoptosis of melanoma cells via mitochondrial damage-dependent ROS accumulation". Cellular Signalling. 22 (2): 197–211. doi:10.1016/j.cellsig.2009.09.013. PMID 19799997.
Mao R, Zhang J, Jiang D, Cai D, Levy JM, Cuconati A, Block TM, Guo JT, Guo H (January 2011). "Indoleamine 2,3-dioxygenase mediates the antiviral effect of gamma interferon against hepatitis B virus in human hepatocyte-derived cells". Journal of Virology. 85 (2): 1048–57. doi:10.1128/JVI.01998-10. PMC 3019998. PMID 21084489.
Sørensen RB, Køllgaard T, Andersen RS, van den Berg JH, Svane IM, Straten P, Andersen MH (March 2011). "Spontaneous cytotoxic T-Cell reactivity against indoleamine 2,3-dioxygenase-2". Cancer Research. 71 (6): 2038–44. doi:10.1158/0008-5472.CAN-10-3403. PMID 21406395.
Meininger D, Zalameda L, Liu Y, Stepan LP, Borges L, McCarter JD, Sutherland CL (December 2011). "Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814 (12): 1947–54. doi:10.1016/j.bbapap.2011.07.023. PMID 21835273.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000188676 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000031549 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: Indoleamine 2,3-dioxygenase 2".

[6] Yuasa HJ, Mizuno K, Ball HJ (July 2015). "Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable". The FEBS Journal. 282 (14): 2735–45. doi:10.1111/febs.13316. PMID 25950090. S2CID 25834690.

[7] Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (July 2007). "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice". Gene. 396 (1): 203–13. doi:10.1016/j.gene.2007.04.010. PMID 17499941.

[8] Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (July 2007). "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice". Gene. 396 (1): 203–13. doi:10.1016/j.gene.2007.04.010. PMID 17499941.

[9] Merlo LM, Mandik-Nayak L (2016). "IDO2: A Pathogenic Mediator of Inflammatory Autoimmunity". Clinical Medicine Insights. Pathology. 9 (Suppl 1): 21–28. doi:10.4137/CPath.S39930. PMC 5119657. PMID 27891058.

[10] Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC (August 2007). "Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan". Cancer Research. 67 (15): 7082–7. doi:10.1158/0008-5472.CAN-07-1872. PMID 17671174.

[11] Metz R, Smith C, DuHadaway JB, Chandler P, Baban B, Merlo LM, Pigott E, Keough MP, Rust S, Mellor AL, Mandik-Nayak L, Muller AJ, Prendergast GC (July 2014). "IDO2 is critical for IDO1-mediated T-cell regulation and exerts a non-redundant function in inflammation". International Immunology. 26 (7): 357–67. doi:10.1093/intimm/dxt073. PMC 4432394. PMID 24402311.

[12] Löb S, Königsrainer A, Zieker D, Brücher BL, Rammensee HG, Opelz G, Terness P (January 2009). "IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism". Cancer Immunology, Immunotherapy. 58 (1): 153–7. doi:10.1007/s00262-008-0513-6. PMID 18418598. S2CID 6199515.

Indoleamine 2,3-dioxygenase 2

Function

References

Further reading