IMPDH2

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Identifiers
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External IDs	GeneCards: [1]
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	Wikidata
View/Edit Human

Inosine-5'-monophosphate dehydrogenase 2, also known as IMP dehydrogenase 2, is an enzyme that in humans is encoded by the IMPDH2 gene.^[1]^[2]^[3]

Function

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.^[1] IMPDH2 has been identified as an intracellular target of the natural product sanglifehrin A^[4]

Clinical significance

This gene is up-regulated in some neoplasms, suggesting it may play a role in malignant transformation.^[1]

References

↑ ^1.0 ^1.1 ^1.2 "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 2".
↑ 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. PMID 1969416.
↑ 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.
↑ 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.
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.
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.
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): HASH(0x2dc9fd0). 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.
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.
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.
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.
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. 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.
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. 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.

This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it.

[entrez-1] 1.0 ^1.1 ^1.2 "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 2".

[pmid1969416-2] 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. PMID 1969416.

[pmid9858805-3] 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.

[sanglifehrin-4] 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.

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v t e Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

IMPDH2

Contents

Function

Clinical significance

See also

References

Further reading

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