Indoleamine 2,3-dioxygenase 2

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

IDO2
Identifiers
AliasesIDO2, INDOL1, indoleamine 2,3-dioxygenase 2
External IDsOMIM: 612129; MGI: 2142489; HomoloGene: 48830; GeneCards: IDO2; OMA:IDO2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_194294
NM_001395206

NM_145949

RefSeq (protein)

NP_919270

NP_666061

Location (UCSC)Chr 8: 39.93 – 40.02 MbChr 8: 25.02 – 25.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

edit

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] 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

edit
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000188676Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031549Ensembl, 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.
  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. PMC 11030193. PMID 18418598. S2CID 6199515.

Further reading

edit

This article incorporates text from the United States National Library of Medicine, which is in the public domain.