IMPDH2

IMPDH2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1B3O, 1NF7, 1NFB

Identifiers

Aliases

IMPDH2, IMPD2, IMPDH-II, IMP (inosine 5'-monophosphate) dehydrogenase 2, inosine monophosphate dehydrogenase 2

External IDs

OMIM: 146691 MGI: 109367 HomoloGene: 48919 GeneCards: IMPDH2

Gene location (Human)

Chr.	Chromosome 3 (human)^[1]

Band	3p21.31	Start	49,024,325 bp^[1]
Band	3p21.31	End	49,029,447 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 9 (mouse)^[2]

Band	9\|9 F2	Start	108,437,485 bp^[2]
Band	9\|9 F2	End	108,442,783 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

body of pancreas

right uterine tube

canal of the cervix

vulva

skin of abdomen

embryo

nipple

ganglionic eminence

gastrocnemius muscle

human penis

Top expressed in

morula

uterus

spermatid

yolk sac

ovary

spleen

ganglionic eminence

thymus

limb

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	DNA binding metal ion binding catalytic activity protein binding RNA binding oxidoreductase activity nucleotide binding IMP dehydrogenase activity
Cellular component	cytoplasm membrane peroxisomal membrane extracellular exosome nucleus extracellular region cytosol secretory granule lumen ficolin-1-rich granule lumen
Biological process	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
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


3615


23918

Ensembl


ENSG00000178035


ENSMUSG00000062867

UniProt


P12268


P24547

RefSeq (mRNA)


NM_000884


NM_011830 NM_001378921

RefSeq (protein)


NP_000875


NP_035960 NP_001365850

Location (UCSC)

Chr 3: 49.02 – 49.03 Mb

Chr 9: 108.44 – 108.44 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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]

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.^[5] IMPDH2 has been identified as an intracellular target of the natural product sanglifehrin A.^[8]

Clinical significance

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

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000178035 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000062867 – 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.
^ ^a ^b ^c "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 2". Archived from the original on 2024-04-22. Retrieved 2017-10-29.
^ 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.
^ 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.
^ 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.

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

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 Alcohol 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 Diffusion-limited enzyme 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) EC7 Translocases (list)

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This page was last edited on 22 April 2024, at 06:54

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Function

Clinical significance

See also

References

Further reading