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Showing content from https://en.wikipedia.org/wiki/IMPDH2 below:

IMPDH2 - Wikipedia

From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

1B3O, 1NF7, 1NFB

• left ovary


• body of pancreas


• cartilage tissue


• right ovary


• right uterine tube


• gingival epithelium


• ventricular zone


• canal of the cervix


• skin of leg


• vulva

• morula


• epiblast


• uterus


• ventricular zone


• embryo


• embryo


• blastocyst


• spermatid


• yolk sac


• ovary

• DNA binding
• metal ion binding
• catalytic activity
• protein binding
• RNA binding
• oxidoreductase activity
• nucleotide binding
• IMP dehydrogenase activity

• cytoplasm
• membrane
• peroxisomal membrane
• extracellular exosome
• nucleus
• extracellular region
• cytosol
• secretory granule lumen
• ficolin-1-rich granule lumen

• cellular response to interleukin-4
• purine nucleotide biosynthetic process
• retina development in camera-type eye
• purine ribonucleoside monophosphate biosynthetic process
• lymphocyte proliferation
• GMP biosynthetic process
• protein homotetramerization
• GTP biosynthetic process
• neutrophil degranulation
• circadian rhythm

3615

23918

ENSG00000178035

ENSMUSG00000062867

P12268

P24547

NM_000884

NM_011830
NM_001378921

NP_000875

NP_035960
NP_001365850

Inosine-5'-monophosphate dehydrogenase 2, also known as IMP dehydrogenase 2, is an enzyme that in humans is encoded by the IMPDH2 gene.^[5][6][7]

IMP dehydrogenase 2 is the rate-limiting enzyme in the de novo guanine nucleotide biosynthesis. It is thus involved in maintaining cellular guanine deoxy- and ribonucleotide pools needed for DNA and RNA synthesis. IMPDH2 catalyzes the NAD-dependent oxidation of inosine-5'-monophosphate into xanthine-5'-monophosphate, which is then converted into guanosine-5'-monophosphate.^[5] IMPDH2 has been identified as an intracellular target of the natural product sanglifehrin A.^[8]

This gene is up-regulated in some neoplasms, suggesting it may play a role in malignant transformation.^[5]

• IMP dehydrogenase

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000178035 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000062867 – 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.
5. ^ ^{a b c} "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 2". Archived from the original on 2024-04-22. Retrieved 2017-10-29.
6. ^ Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March 1990). "Two distinct cDNAs for human IMP dehydrogenase". J. Biol. Chem. 265 (9): 5292–5. doi:10.1016/S0021-9258(19)34120-1. PMID 1969416.
7. ^ Kost-Alimova MV, Glesne DA, Huberman E, Zelenin AV (1998). "Assignment1 of inosine '-monophosphate dehydrogenase type 2 (IMPDH2) to human chromosome band 3p21.2 by in situ hybridization". Cytogenet. Cell Genet. 82 (3–4): 145–6. doi:10.1159/000015088. PMID 9858805. S2CID 46764436. Archived from the original on 2024-04-22. Retrieved 2019-07-05.
8. ^ Pua KH, Stiles DT, Sowa ME, Verdine GL (10 January 2017). "IMPDH2 Is an Intracellular Target of the Cyclophilin A and Sanglifehrin A Complex". Cell Rep. 18 (2): 432–442. doi:10.1016/j.celrep.2016.12.030. PMID 28076787.

• Garat A, Cauffiez C, Hamdan-Khalil R, et al. (2009). "IMPDH2 genetic polymorphism: a promoter single-nucleotide polymorphism disrupts a cyclic adenosine monophosphate responsive element". Genet Test Mol Biomarkers. 13 (6): 841–7. doi:10.1089/gtmb.2009.0096. PMID 19810816.
• Wang J, Zeevi A, Webber S, et al. (2007). "A novel variant L263F in human inosine 5'-monophosphate dehydrogenase 2 is associated with diminished enzyme activity". Pharmacogenet. Genomics. 17 (4): 283–90. doi:10.1097/FPC.0b013e328012b8cf. PMID 17496727. S2CID 21301713.
• So HC, Fong PY, Chen RY, et al. (2010). "Identification of neuroglycan C and interacting partners as potential susceptibility genes for schizophrenia in a Southern Chinese population". Am. J. Med. Genet. B Neuropsychiatr. Genet. 153B (1): 103–13. doi:10.1002/ajmg.b.30961. PMID 19367581. S2CID 20522961. Archived from the original on 2019-09-28. Retrieved 2019-09-28.
• Grinyó J, Vanrenterghem Y, Nashan B, et al. (2008). "Association of four DNA polymorphisms with acute rejection after kidney transplantation". Transpl. Int. 21 (9): 879–91. doi:10.1111/j.1432-2277.2008.00679.x. PMID 18444945. S2CID 42432512.
• Ohmann EL, Burckart GJ, Brooks MM, et al. (2010). "Genetic polymorphisms influence mycophenolate mofetil-related adverse events in pediatric heart transplant patients". The Journal of Heart and Lung Transplantation. 29 (5): 509–516. doi:10.1016/j.healun.2009.11.602. PMID 20061166.
• Sombogaard F, van Schaik RH, Mathot RA, et al. (2009). "Interpatient variability in IMPDH activity in MMF-treated renal transplant patients is correlated with IMPDH type II 3757T > C polymorphism". Pharmacogenet. Genomics. 19 (8): 626–34. doi:10.1097/FPC.0b013e32832f5f1b. PMID 19617864. S2CID 41882586.
• Fellenberg J, Bernd L, Delling G, et al. (2007). "Prognostic significance of drug-regulated genes in high-grade osteosarcoma". Mod. Pathol. 20 (10): 1085–94. doi:10.1038/modpathol.3800937. PMID 17660802.
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
• He Y, Mou Z, Li W, et al. (2009). "Identification of IMPDH2 as a tumor-associated antigen in colorectal cancer using immunoproteomics analysis". Int J Colorectal Dis. 24 (11): 1271–9. doi:10.1007/s00384-009-0759-2. PMID 19597826. S2CID 24143679.
• Peñuelas S, Noé V, Ciudad CJ (2005). "Modulation of IMPDH2, survivin, topoisomerase I and vimentin increases sensitivity to methotrexate in HT29 human colon cancer cells". FEBS J. 272 (3): 696–710. doi:10.1111/j.1742-4658.2004.04504.x. PMID 15670151. S2CID 43226077.
• Winnicki W, Weigel G, Sunder-Plassmann G, et al. (2010). "An inosine 5'-monophosphate dehydrogenase 2 single-nucleotide polymorphism impairs the effect of mycophenolic acid". Pharmacogenomics J. 10 (1): 70–6. doi:10.1038/tpj.2009.43. PMID 19770842.
• Patel CG, Richman K, Yang D, et al. (2007). "Effect of diabetes mellitus on mycophenolate sodium pharmacokinetics and inosine monophosphate dehydrogenase activity in stable kidney transplant recipients". Ther Drug Monit. 29 (6): 735–42. doi:10.1097/FTD.0b013e31815d8ace. PMC 4082794. PMID 18043470.
• Sanquer S, Maison P, Tomkiewicz C, et al. (2008). "Expression of inosine monophosphate dehydrogenase type I and type II after mycophenolate mofetil treatment: a 2-year follow-up in kidney transplantation". Clin. Pharmacol. Ther. 83 (2): 328–35. doi:10.1038/sj.clpt.6100300. PMID 17713475. S2CID 44919245.
• Mohamed MF, Frye RF, Langaee TY (2008). "Interpopulation variation frequency of human inosine 5'-monophosphate dehydrogenase type II (IMPDH2) genetic polymorphisms". Genet. Test. 12 (4): 513–6. doi:10.1089/gte.2008.0049. PMID 18976158.
• Mannava S, Grachtchouk V, Wheeler LJ, et al. (2008). "Direct role of nucleotide metabolism in C-MYC-dependent proliferation of melanoma cells". Cell Cycle. 7 (15): 2392–400. doi:10.4161/cc.6390. PMC 3744895. PMID 18677108.
• Chen L, Petrelli R, Olesiak M, et al. (2008). "Bis(sulfonamide) isosters of mycophenolic adenine dinucleotide analogues: inhibition of inosine monophosphate dehydrogenase". Bioorg. Med. Chem. 16 (15): 7462–9. doi:10.1016/j.bmc.2008.06.003. PMID 18583139.
• Guo D, Han J, Adam BL, et al. (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.
• Kudo M, Saito Y, Sasaki T, et al. (2009). "Genetic variations in the HGPRT, ITPA, IMPDH1, IMPDH2, and GMPS genes in Japanese individuals". Drug Metab. Pharmacokinet. 24 (6): 557–64. doi:10.2133/dmpk.24.557. PMID 20045992.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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

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PDB gallery

• 1b3o: TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE

• 1jr1: Crystal structure of Inosine Monophosphate Dehydrogenase in complex with Mycophenolic Acid

• 1nfb: Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with 6Cl-IMP and NAD

• 1nf7: Ternary complex of the human type II Inosine Monophosphate Dedhydrogenase with Ribavirin Monophosphate and C2-Mycophenolic Adenine Dinucleotide

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