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IMPDH1
Identifiers
Aliases	IMPDH1, IMPD, IMPD1, IMPDH-I, LCA11, RP10, sWSS2608, IMP (inosine 5'-monophosphate) dehydrogenase 1, inosine monophosphate dehydrogenase 1
External IDs	OMIM: 146690; MGI: 96567; GeneCards: IMPDH1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1JCN
Enzyme activity
Gene location (Human)
Chr.	Chromosome 7 (human)
End	128,410,252 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	29,216,363 bp
RNA expression pattern
	Top expressed in
	granulocyte; ; monocyte; ; body of stomach; ; stromal cell of endometrium; ; blood; ; spleen; ; gastric mucosa; ; apex of heart; ; tibial nerve; ; upper lobe of left lung;
	Top expressed in
	neural layer of retina; ; olfactory epithelium; ; thymus; ; retinal pigment epithelium; ; morula; ; superior frontal gyrus; ; lumbar spinal ganglion; ; dentate gyrus of hippocampal formation granule cell; ; primary visual cortex; ; embryo;
	More reference expression data
	n/a
Gene ontology
Molecular function	metal ion binding; catalytic activity; RNA binding; nucleic acid binding; oxidoreductase activity; DNA binding; IMP dehydrogenase activity; nucleotide binding;
Cellular component	cytoplasm; nucleus; extracellular region; cytosol; secretory granule lumen; azurophil granule lumen; ficolin-1-rich granule lumen;
Biological process	purine nucleotide biosynthetic process; purine ribonucleoside monophosphate biosynthetic process; lymphocyte proliferation; GMP biosynthetic process; GTP biosynthetic process; neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	3614
	23917
	ENSG00000106348
	ENSMUSG00000003500
	P20839
	P50096
NM_000883; NM_001102605; NM_001142573; NM_001142574; NM_001142575;
	NM_001142576; NM_001304521; NM_183243
	NM_011829; NM_001302933; NM_001302934
NP_000874; NP_001096075; NP_001136045; NP_001136046; NP_001136047;
	NP_001136048; NP_001291450; NP_899066
	NP_001289862; NP_001289863; NP_035959
	Wikidata
View/Edit Human	View/Edit Mouse

Inosine-5'-monophosphate dehydrogenase 1, also known as IMP dehydrogenase 1, is an enzyme that in humans is encoded by the IMPDH1 gene.^[5]^[6]

Function

IMP dehydrogenase 1 acts as a homotetramer to regulate cell growth. IMPDH1 is an enzyme that catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5'-monophosphate (IMP). This is the rate-limiting step in the de novo synthesis of guanine nucleotides.^[5]

Clinical significance

Defects in the IMPDH1 gene are a cause of retinitis pigmentosa type 10 (RP10).^[5]^[7]^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000106348 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000003500 – 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 1".
^ 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.
^ Kennan A, Aherne A, Palfi A, Humphries M, McKee A, Stitt A, Simpson DA, Demtroder K, Orntoft T, Ayuso C, Kenna PF, Farrar GJ, Humphries P (March 2002). "Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice". Hum. Mol. Genet. 11 (5): 547–57. doi:10.1093/hmg/11.5.547. PMID 11875049.
^ Bowne SJ, Sullivan LS, Blanton SH, Cepko CL, Blackshaw S, Birch DG, Hughbanks-Wheaton D, Heckenlively JR, Daiger SP (March 2002). "Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa". Hum. Mol. Genet. 11 (5): 559–68. doi:10.1093/hmg/11.5.559. PMC 2585828. PMID 11875050.

Mortimer SE, Xu D, McGrew D, et al. (2008). "IMP dehydrogenase type 1 associates with polyribosomes translating rhodopsin mRNA". J. Biol. Chem. 283 (52): 36354–60. doi:10.1074/jbc.M806143200. PMC 2605994. PMID 18974094.
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.
Grover S, Fishman GA, Stone EM (2004). "A novel IMPDH1 mutation (Arg231Pro) in a family with a severe form of autosomal dominant retinitis pigmentosa". Ophthalmology. 111 (10): 1910–6. doi:10.1016/j.ophtha.2004.03.039. PMID 15465556.
Bowne SJ, Liu Q, Sullivan LS, et al. (2006). "Why do mutations in the ubiquitously expressed housekeeping gene IMPDH1 cause retina-specific photoreceptor degeneration?". Invest. Ophthalmol. Vis. Sci. 47 (9): 3754–65. doi:10.1167/iovs.06-0207. PMC 2581456. PMID 16936083.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Schatz P, Ponjavic V, Andréasson S, et al. (2005). "Clinical phenotype in a Swedish family with a mutation in the IMPDH1 gene". Ophthalmic Genet. 26 (3): 119–24. doi:10.1080/13816810500229090. PMID 16272056. S2CID 33839722.
Wada Y, Tada A, Itabashi T, et al. (2005). "Screening for mutations in the IMPDH1 gene in Japanese patients with autosomal dominant retinitis pigmentosa". Am. J. Ophthalmol. 140 (1): 163–5. doi:10.1016/j.ajo.2005.01.017. PMID 16038673.
Wang J, Yang JW, Zeevi A, et al. (2008). "IMPDH1 gene polymorphisms and association with acute rejection in renal transplant patients". Clin. Pharmacol. Ther. 83 (5): 711–7. doi:10.1038/sj.clpt.6100347. PMID 17851563. S2CID 12718828.
Gandra M, Anandula V, Authiappan V, et al. (2008). "Retinitis pigmentosa: mutation analysis of RHO, PRPF31, RP1, and IMPDH1 genes in patients from India". Mol. Vis. 14: 1105–13. PMC 2426732. PMID 18552984.
Bowne SJ, Sullivan LS, Mortimer SE, et al. (2006). "Spectrum and frequency of mutations in IMPDH1 associated with autosomal dominant retinitis pigmentosa and leber congenital amaurosis". Invest. Ophthalmol. Vis. Sci. 47 (1): 34–42. doi:10.1167/iovs.05-0868. PMC 2581444. PMID 16384941.
Xu D, Cobb G, Spellicy CJ, et al. (2008). "Retinal isoforms of inosine 5'-monophosphate dehydrogenase type 1 are poor nucleic acid binding proteins". Arch. Biochem. Biophys. 472 (2): 100–4. doi:10.1016/j.abb.2008.02.012. PMC 2366119. PMID 18295591.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Kozma P, Hughbanks-Wheaton DK, Locke KG, et al. (2005). "Phenotypic characterization of a large family with RP10 autosomal-dominant retinitis pigmentosa: an Asp226Asn mutation in the IMPDH1 gene". Am. J. Ophthalmol. 140 (5): 858–867. doi:10.1016/j.ajo.2005.05.027. PMC 2771559. PMID 16214101.
Wada Y, Sandberg MA, McGee TL, et al. (2005). "Screen of the IMPDH1 gene among patients with dominant retinitis pigmentosa and clinical features associated with the most common mutation, Asp226Asn". Invest. Ophthalmol. Vis. Sci. 46 (5): 1735–41. doi:10.1167/iovs.04-1197. PMID 15851576.
Jin P, Fu GK, Wilson AD, et al. (2004). "PCR isolation and cloning of novel splice variant mRNAs from known drug target genes". Genomics. 83 (4): 566–71. doi:10.1016/j.ygeno.2003.09.023. PMID 15028279.
Roberts RL, Gearry RB, Barclay ML, Kennedy MA (2007). "IMPDH1 promoter mutations in a patient exhibiting azathioprine resistance". Pharmacogenomics J. 7 (5): 312–7. doi:10.1038/sj.tpj.6500421. PMID 17001353. S2CID 11257472.
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.

External links

GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview
Overview of all the structural information available in the PDB for UniProt: P20839 (Inosine-5'-monophosphate dehydrogenase 1) at the PDBe-KB.

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 7 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000106348 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000003500 – 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.

[entrez-5] "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 1".

[pmid1969416-6] 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.

[pmid11875049-7] Kennan A, Aherne A, Palfi A, Humphries M, McKee A, Stitt A, Simpson DA, Demtroder K, Orntoft T, Ayuso C, Kenna PF, Farrar GJ, Humphries P (March 2002). "Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice". Hum. Mol. Genet. 11 (5): 547–57. doi:10.1093/hmg/11.5.547. PMID 11875049.

[pmid11875050-8] Bowne SJ, Sullivan LS, Blanton SH, Cepko CL, Blackshaw S, Birch DG, Hughbanks-Wheaton D, Heckenlively JR, Daiger SP (March 2002). "Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa". Hum. Mol. Genet. 11 (5): 559–68. doi:10.1093/hmg/11.5.559. PMC 2585828. PMID 11875050.

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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 6-Phosphogluconate 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+) 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	Alcohol oxidase Glucose oxidase L-gulonolactone oxidase L-lactate 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 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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IMPDH1

Function

Clinical significance

See also

References

Further reading

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