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Protein-coding gene in the species Homo sapiens
Indoleamine 2,3-dioxygenase 2 (IDO2) is a protein that in humans is encoded by the IDO2 gene .[ 5]
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 IDO1 and IDO2 being closely related enzymes originating by gene duplication and sharing high level (43%) of sequence homology,[ 6] [ 7] [ 8] [ 9] [ 10] Treg differentiation in vitro ,[ 11] [ 12]
^ a b c GRCh38: Ensembl release 89: ENSG00000188676 – Ensembl , May 2017^ a b c 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 . PMC 11030193 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 .
This article incorporates text from the United States National Library of Medicine , which is in the public domain .
