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Inosine-5′-monophosphate dehydrogenase

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into the newly unoccupied NAD binding site. The arginine residue is thought to act as the general base that activates a water molecule for the hydrolysis reaction. Alternatively, molecular mechanics simulations suggest that in conditions where the arginine residue is protonated, the threonine residue
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nucleotide synthesis. IMPDH has also been shown to bind nucleic acids, and this function can be impaired by mutations that are located in the Bateman domain. The Bateman domain has also been implicated in mediating IMPDH association with polyribosomes, which suggests a potential
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Guanine nucleotide synthesis is essential for maintaining normal cell function and growth, and is also important for the maintenance of cell proliferation and immune responses. IMPDH expression is found to be upregulated in some tumor tissues and cell lines. B and T
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residue attacks the 2-position of the purine ring. A hydride ion is then transferred from the C2 position to NAD and the E-XMP* intermediate is formed. NADH dissociates from the enzyme and a mobile active-site flap element moves a conserved catalytic dyad of
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Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC (September 1997). "Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex".
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Gan L, Seyedsayamdost MR, Shuto S, Matsuda A, Petsko GA, Hedstrom L (February 2003). "The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase".
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reaction involving a hydride transfer to NAD which generates NADH and an enzyme-bound XMP intermediate (E-XMP*) and (2) a hydrolysis step that releases XMP from the enzyme. IMP binds to the active site and a conserved
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Wang J, Yang JW, Zeevi A, Webber SA, Girnita DM, Selby R, Fu J, Shah T, Pravica V, Hutchinson IV, Burckart GJ (May 2008). "IMPDH1 gene polymorphisms and association with acute rejection in renal transplant patients".
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Visual representation of the active site with IMP (green) and NAD (purple) bound. Key residues (white) of the protein and the catalytic cysteine (cyan) are shown. Dashed lines represent polar contacts.
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Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR (April 1999). "Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase".
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Nimmesgern E, Black J, Futer O, Fulghum JR, Chambers SP, Brummel CL, Raybuck SA, Sintchak MD (November 1999). "Biochemical analysis of the modular enzyme inosine 5'-monophosphate dehydrogenase".
353:, IMPDH have been identified as a plasminogen-binding protein. Drosophila IMPDH has been demonstrated to act as a sequence-specific transcriptional repressor that can reduce the expression of 315:
that are inserted within the dehydrogenase sequence. Monovalent cations have been shown to activate most IMPDH enzymes and may serve to stabilize the conformation of the active-site loop.
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Gedeon, Antoine; Ayoub, Nour; Brûlé, Sébastien; Raynal, Bertrand; Karimova, Gouzel; Gelin, Muriel; Mechaly, Ariel; Haouz, Ahmed; Labesse, Gilles; Munier-Lehmann, Hélène (August 2023).
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Both isozymes contain 514 residues, have an 84% similarity in peptide sequence, and have similar kinetic properties. Both isozymes are constitutively expressed in most tissues, but
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Jonsson CA, Carlsten H (January 2003). "Mycophenolic acid inhibits inosine 5'-monophosphate dehydrogenase and suppresses immunoglobulin and cytokine production of B cells".
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Labesse, Gilles; Alexandre, Thomas; Vaupré, Laurène; Salard-Arnaud, Isabelle; Him, Joséphine Lai Kee; Raynal, Bertrand; Bron, Patrick; Munier-Lehmann, Hélène (2013-06-04).
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display a dependence on IMPDH for normal activation and function, and demonstrate upregulated IMPDH expression. Therefore, IMPDH has been addressed as a drug target for
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Aherne A, Kennan A, Kenna PF, McNally N, Lloyd DG, Alberts IL, Kiang AS, Humphries MM, Ayuso C, Engel PC, Gu JJ, Mitchell BS, Farrar GJ, Humphries P (March 2004).
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Bowne SJ, Sullivan LS, Mortimer SE, Hedstrom L, Zhu J, Spellicy CJ, Gire AI, Hughbanks-Wheaton D, Birch DG, Lewis RA, Heckenlively JR, Daiger SP (January 2006).
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domain with an active site located in the loops at the C-terminal end of the barrel, and a subdomain, named the Bateman domain, and consisting of two, repeated
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The canonic monomeric form of IMPDH has a molecular masse of approximately 55 kDa and generally consists of 400-500 residues. IMPDHs have been described as
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Buey, Rubén M.; Ledesma-Amaro, Rodrigo; Velázquez-Campoy, Adrián; Balsera, Mónica; Chagoyen, Mónica; de Pereda, José M.; Revuelta, José L. (2015-11-12).
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mice demonstrate a mild retinopathy in which a slow, progressive form of retinal degeneration gradually weakens visual transduction, while homozygous
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The Bateman domain is not required for catalytic activity. Mutations within the Bateman domain or a complete deletion of the domain do not impair the
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monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism".
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nucleotides from IMP. IMPDH is a regulator of the intracellular guanine nucleotide pool, and is therefore important for DNA and RNA synthesis,
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Bojkova, Denisa; Klann, Kevin; Koch, Benjamin; Widera, Marek; Krause, David; Ciesek, Sandra; Cinatl, Jindrich; Münch, Christian (2020-05-14).
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for "Study to Evaluate the Safety and Efficacy of VIRAZOLE® in Hospitalized Adult Participants With Respiratory Distress Due to COVID-19" at
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PDB ID: 1NFB, Risal, D., Strickler M,D., Goldstein, B.M.,The Conformation of NAD Bound to Human Inosine Monophosphate Dehydrogenase Type II.
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Nimmesgern, E.; Black, J.; Futer, O.; Fulghum, J. R.; Chambers, S. P.; Brummel, C. L.; Raybuck, S. A.; Sintchak, M. D. (November 1999).
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Sintchak MD, Nimmesgern E (May 2000). "The structure of inosine 5'-monophosphate dehydrogenase and the design of novel inhibitors".
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Senda M, Natsumeda Y (1994). "Tissue-differential expression of two distinct genes for human IMP dehydrogenase (E.C.1.1.1.205)".
1444:"Autosomal dominant retinitis pigmentosa mutations in inosine 5'-monophosphate dehydrogenase type I disrupt nucleic acid binding" 675: 497: 3854: 3150: 3000: 2933: 2880: 2302:
Inosine-5'-monophosphate dehydrogenase: regulation of expression and role in cellular proliferation and T lymphocyte activation
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is also capable of activating water by accepting a proton from water while transferring its own proton to a nearby residue.
3045: 2735: 3315: 2958: 3448: 3212: 1528:"Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases" 381:
General mechanism used by the enzyme IMPDH to convert IMP to XMP. Only the purine portion of each molecule is shown.
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catalytic activity of some IMPDH . Other deletion examples of the Bateman domain in IMPDH have shown an enhanced
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Kozhevnikova EN, van der Knaap JA, Pindyurin AV, Ozgur Z, van Ijcken WF, Moshkin YM, Verrijzer CP (July 2012).
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Min D, Josephine HR, Li H, Lakner C, MacPherson IS, Naylor GJ, Swofford D, Hedstrom L, Yang W (August 2008).
2087:"Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs" 1995: 3591: 3415: 3222: 3060: 2804: 2763: 2632: 3307: 3120: 2779: 2258:"Increased inosine-5'-phosphate dehydrogenase gene expression in solid tumor tissues and tumor cell lines" 1189: 229: 680: 502: 406: 137: 3612: 3531: 3500: 3262: 3160: 3014: 2909: 389: 257: 3684: 1358:"Enzymes essential for the biosynthesis of nucleic acid guanine; inosine 5'-phosphate dehydrogenase of 3277: 3272: 3232: 3055: 2528: 881: 878: 864: 745: 567: 346: 72: 3085: 1194: 165: 3648: 3165: 3032: 3005: 2875: 1943:
Mortimer SE, Xu D, McGrew D, Hamaguchi N, Lim HC, Bowne SJ, Daiger SP, Hedstrom L (December 2008).
1689:"A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis" 273: 89: 67: 17: 1740:"The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover" 3581: 2846: 2705: 2669: 2620: 2578: 3849: 3252: 3247: 2885: 2815: 2687: 2612: 2554: 2546: 2497: 2448: 2413: 2364: 2323: 2313: 2279: 2235: 2200: 2159: 2108: 2067: 2023: 2015: 1976: 1925: 1873: 1865: 1826: 1777: 1759: 1720: 1669: 1651: 1612: 1604: 1565: 1547: 1508: 1473: 1424: 1403:"Monovalent cation activation and kinetic mechanism of inosine 5'-monophosphate dehydrogenase" 1383: 1329: 1321: 1282: 1243: 1207: 1162: 1106: 1071: 1053: 1012: 994: 955: 913: 847: 156: 1994:
Mölkänen, Tomi; Tyynelä, Jaana; Helin, Jari; Kalkkinen, Nisse; Kuusela, Pentti (2002-04-24).
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The mechanism of IMPDH involves a sequence of two different chemical reactions: (1) a fast
3674: 3658: 3571: 3425: 3410: 2468:"Inhibition of T lymphocyte activation in mice heterozygous for loss of the IMPDH II gene" 769: 591: 101: 60: 2532: 2466:
Gu JJ, Stegmann S, Gathy K, Murray R, Laliberte J, Ayscue L, Mitchell BS (August 2000).
1664: 1631: 1066: 1031: 377: 39: 3823: 3712: 3653: 3116: 3050: 2980: 2943: 2384:"Targeted disruption of the inosine 5'-monophosphate dehydrogenase type I gene in mice" 2154: 2127: 1971: 1944: 1920: 1895: 1821: 1796: 1772: 1739: 1715: 1688: 1560: 1527: 1468: 1443: 1157: 1132: 1007: 974: 295: 200: 2492: 2467: 2444: 2408: 2383: 2343:"On the molecular pathology of neurodegeneration in IMPDH1-based retinitis pigmentosa" 2309: 2195: 2178: 2103: 2086: 2011: 1861: 1378: 1357: 1278: 1102: 180: 3833: 3617: 3576: 2895: 2830: 2789: 2709: 2399: 2231: 1996:"Enhanced activation of bound plasminogen on Staphylococcus aureus by staphylokinase" 1755: 1032:"A journey into the regulatory secrets of the de novo purine nucleotide biosynthesis" 860: 826: 175: 2624: 1795:
McLean JE, Hamaguchi N, Belenky P, Mortimer SE, Stanton M, Hedstrom L (April 2004).
3566: 2046:"Metabolic enzyme IMPDH is also a transcription factor regulated by cellular state" 1945:"IMP dehydrogenase type 1 associates with polyribosomes translating rhodopsin mRNA" 1585:"Biochemical analysis of the modular enzyme inosine 5'-monophosphate dehydrogenase" 854: 822:
is generally upregulated in proliferating cells and neoplastic tissues. Homozygous
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is predominately expressed in the spleen, retina, and peripheral blood leukocytes.
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catalytic activity in comparison with the corresponding wild-type counterpart. An
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synthesis, as well as other process that are involved in cellular proliferation.
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Gu JJ, Tolin AK, Jain J, Huang H, Santiago L, Mitchell BS (September 2003).
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Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March 1990).
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Cornuel, Jean-François; Moraillon, Anne; Guéron, Maurice (April 2002).
1812: 1543: 1459: 792: 362: 354: 341: 330: 269: 132: 2517:"Proteomics of SARS-CoV-2-infected host cells reveals therapy targets" 1239: 1203: 1148: 990: 951: 3777: 3547: 3505: 3401: 3200: 3195: 3190: 3185: 3175: 2677: 2274: 2128:"An enzymatic atavist revealed in dual pathways for water activation" 1647: 851: 803: 797: 699: 648: 621: 521: 470: 455: 249: 245: 212: 108: 96: 84: 2483: 292:, although further data validated the existence of octameric forms. 1030:
Ayoub, Nour; Gedeon, Antoine; Munier-Lehmann, Hélène (2024-02-20).
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replication in cells and are being tested in clinical trials for
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suggests that the domain can act as a negative transregulator of
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Prosise GL, Luecke H (February 2003). "Crystal structures of
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Collart FR, Chubb CB, Mirkin BL, Huberman E (October 1992).
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Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
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is generally expressed constitutively at low levels, and
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role for IMPDH as a translational regulatory protein. In
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Phosphoribosylaminoimidazolesuccinocarboxamide synthase
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Zimmermann AG, Gu JJ, Laliberté J, Mitchell BS (1998).
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This article incorporates text from the public domain
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and nuclear accumulation is mostly restricted to the
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Most IMPDH monomers contain two domains: a catalytic
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Malate dehydrogenase (oxaloacetate-decarboxylating)
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(April 2008). 863:is an immunosuppressant that is used to prevent 2039: 2037: 1889: 1887: 1401:Xiang B, Taylor JC, Markham GD (January 1996). 2855:Hypoxanthine-guanine phosphoribosyltransferase 2295: 2293: 2251: 2249: 1687:Pimkin M, Pimkina J, Markham GD (March 2009). 1356:Magasanik B, Moyed HS, Gehring LB (May 1957). 1126: 1124: 1122: 1120: 3532: 3101: 2648: 8: 896:IMPDH inhibitors have been shown to prevent 385:The overall reaction catalyzed by IMPDH is: 2731:Phosphoribosylglycinamide formyltransferase 833:knockout mice display embryonic lethality. 313:cystathionine beta synthetase (CBS) domains 3539: 3525: 3517: 3383:D-lactate dehydrogenase (cytochrome c-553) 3108: 3094: 3086: 2921: 2914: 2699: 2692: 2655: 2641: 2633: 757: 579: 191: 38: 2540: 2491: 2407: 2358: 2273: 2194: 2153: 2143: 2102: 2061: 1970: 1960: 1919: 1820: 1771: 1714: 1704: 1663: 1559: 1467: 1418: 1377: 1193: 1156: 1065: 1047: 1006: 408: 3228:D-malate dehydrogenase (decarboxylating) 2741:Phosphoribosylaminoimidazole carboxylase 795:of IMPDH encoded by two distinct genes, 3814: 2085:Collart FR, Huberman E (October 1988). 1442:Mortimer SE, Hedstrom L (August 2005). 929: 634:IMP dehydrogenase 2 homotetramer, Human 3283:Malate dehydrogenase (decarboxylating) 867:and acts through inhibition of IMPDH. 617: 451: 242:Inosine 5′-monophosphate dehydrogenase 33:Inosine 5'-monophosphate dehydrogenase 29: 2472:The Journal of Clinical Investigation 874:are associated with the RP10 form of 7: 3378:D-lactate dehydrogenase (cytochrome) 2964:Orotidine 5'-phosphate decarboxylase 3388:Mannitol dehydrogenase (cytochrome) 2183:The Journal of Biological Chemistry 1949:The Journal of Biological Chemistry 1693:The Journal of Biological Chemistry 1589:Protein Expression and Purification 1493:Protein Expression and Purification 1407:The Journal of Biological Chemistry 870:Mutations in the Bateman domain of 416:{\displaystyle \rightleftharpoons } 18:Inosine monophosphate dehydrogenase 3482:Quinoprotein glucose dehydrogenase 3243:Glycerol-3-phosphate dehydrogenase 3156:3-hydroxybutyryl-CoA dehydrogenase 334:deletion of the Bateman domain in 25: 3238:Glucose-6-phosphate dehydrogenase 2860:Adenine phosphoribosyltransferase 1306:Structure (London, England: 1993) 254:nicotinamide adenine dinucleotide 3817: 2968:Uridine monophosphate synthetase 2721:Ribose-phosphate diphosphokinase 2433:International Immunopharmacology 2400:10.1128/MCB.23.18.6702-6712.2003 1756:10.1111/j.1365-2958.2008.06153.x 973:Hedstrom, Lizbeth (2009-07-08). 628: 3151:3-hydroxyacyl-CoA dehydrogenase 3001:Dihydropyrimidine dehydrogenase 2934:Carbamoyl phosphate synthase II 2881:Purine nucleoside phosphorylase 3477:Malate dehydrogenase (quinone) 3303:Phosphogluconate dehydrogenase 2939:Aspartate carbamoyltransferase 2726:Amidophosphoribosyltransferase 2388:Molecular and Cellular Biology 1: 3046:Nucleoside-diphosphate kinase 2736:AIR synthetase (FGAM cyclase) 2445:10.1016/s1567-5769(02)00210-2 2310:10.1016/S0079-6603(08)60827-2 2196:10.1016/S0021-9258(19)34120-1 2104:10.1016/S0021-9258(19)37654-9 2012:10.1016/S0014-5793(02)02580-2 1862:10.1016/s0300-9084(02)01400-1 1379:10.1016/S0021-9258(18)64835-5 1279:10.1016/S0022-2836(02)01383-9 1103:10.1016/S0162-3109(00)00193-4 256:(NAD)-dependent oxidation of 3316:Hydroxysteroid dehydrogenase 3288:Malate dehydrogenase (NADP+) 2959:Dihydroorotate dehydrogenase 2232:10.1016/0024-3205(94)90150-3 2145:10.1371/journal.pbio.0060206 2063:10.1016/j.molcel.2012.04.030 1263:Tritrichomonasfoetus inosine 886:Leber's congenital amaurosis 791:Humans express two distinct 3845:Genes on human chromosome 3 3840:Genes on human chromosome 7 3449:Vitamin K epoxide reductase 3218:Carbohydrate dehydrogenases 3213:Beta-Ketoacyl ACP reductase 3876: 3860:Enzymes of known structure 3071: 1049:10.3389/fphar.2024.1329011 3695:Michaelis–Menten kinetics 3268:L-threonine dehydrogenase 2976: 2954: 2924: 2775:Adenylosuccinate synthase 2542:10.1038/s41586-020-2332-7 1318:10.1016/j.str.2013.03.011 1036:Frontiers in Pharmacology 756: 627: 578: 190: 37: 3587:Diffusion-limited enzyme 3258:Isocitrate dehydrogenase 3041:Ribonucleotide reductase 2347:Human Molecular Genetics 1131:Hedstrom L (July 2009). 262:xanthosine monophosphate 3416:L-gulonolactone oxidase 3223:Carnitine dehydrogenase 3121:alcohol oxidoreductases 3061:Dihydrofolate reductase 2609:10.1038/sj.clpt.6100347 1801:The Biochemical Journal 1448:The Biochemical Journal 424:xanthosine 5'-phosphate 3855:NADH-dependent enzymes 3308:Sorbitol dehydrogenase 2780:Adenylosuccinate lyase 2571:Clinical trial number 1962:10.1074/jbc.M806143200 1744:Molecular Microbiology 1706:10.1074/jbc.M808541200 1601:10.1006/prep.1999.1136 1505:10.1006/prep.1999.1136 1420:10.1074/jbc.271.3.1435 417: 382: 300: 284:Structure and function 3680:Eadie–Hofstee diagram 3613:Allosteric regulation 3501:Choline dehydrogenase 3263:Lactate dehydrogenase 3161:Alcohol dehydrogenase 3015:Beta-ureidopropionase 2910:Pyrimidine metabolism 2670:amino acid metabolism 2597:Clin. Pharmacol. Ther 1532:Nature Communications 837:Clinical significance 418: 380: 351:Staphylococcus aureus 298: 258:inosine monophosphate 3690:Lineweaver–Burk plot 3278:Malate dehydrogenase 3273:L-xylulose reductase 3233:DXP reductoisomerase 3056:Thymidylate synthase 3033:Deoxyribonucleotides 1912:10.1167/iovs.05-0868 1360:Aerobacter aerogenes 882:retinitis pigmentosa 865:transplant rejection 407: 390:inosine 5'-phosphate 3166:Aldo-keto reductase 3006:Dihydropyrimidinase 2876:Adenosine deaminase 2533:2020Natur.583..469B 622:IMP dehydrogenase 2 456:IMP dehydrogenase 1 276:, energy transfer, 274:signal transduction 252:that catalyzes the 3649:Enzyme superfamily 3582:Enzyme promiscuity 2847:Nucleotide salvage 2579:ClinicalTrials.gov 2360:10.1093/hmg/ddh061 1813:10.1042/BJ20031585 1544:10.1038/ncomms9923 1460:10.1042/BJ20042051 1091:Immunopharmacology 413: 383: 301: 44:Structure of IMPDH 3805: 3804: 3514: 3513: 3494:: other acceptors 3470:/similar acceptor 3253:IMP dehydrogenase 3248:HMG-CoA reductase 3069: 3068: 3027: 3026: 2989: 2988: 2904: 2903: 2886:Guanine deaminase 2841: 2840: 2816:IMP dehydrogenase 2688:Purine metabolism 2527:(7816): 469–472. 2319:978-0-12-540061-9 1240:10.1021/bi9708850 1204:10.1021/bi982858v 1149:10.1021/cr900021w 991:10.1021/cr900021w 952:10.1021/bi0271401 914:Purine metabolism 848:immunosuppressive 789: 788: 785: 784: 611: 610: 607: 606: 239: 238: 235: 234: 138:metabolic pathway 16:(Redirected from 3867: 3822: 3821: 3813: 3685:Hanes–Woolf plot 3628:Enzyme activator 3623:Enzyme inhibitor 3597:Enzyme catalysis 3541: 3534: 3527: 3518: 3421:Xanthine oxidase 3208:Aldose reductase 3110: 3103: 3096: 3087: 2922: 2915: 2891:Xanthine oxidase 2809: 2768: 2714: 2700: 2693: 2657: 2650: 2643: 2634: 2628: 2581: 2569: 2563: 2562: 2544: 2512: 2506: 2505: 2495: 2463: 2457: 2456: 2428: 2422: 2421: 2411: 2379: 2373: 2372: 2362: 2338: 2332: 2331: 2297: 2288: 2287: 2277: 2275:10.2172/10148922 2253: 2244: 2243: 2215: 2209: 2208: 2198: 2174: 2168: 2167: 2157: 2147: 2123: 2117: 2116: 2106: 2097:(30): 15769–72. 2082: 2076: 2075: 2065: 2041: 2032: 2031: 1991: 1985: 1984: 1974: 1964: 1955:(52): 36354–60. 1940: 1934: 1933: 1923: 1891: 1882: 1881: 1841: 1835: 1834: 1824: 1807:(Pt 2): 243–51. 1792: 1786: 1785: 1775: 1735: 1729: 1728: 1718: 1708: 1684: 1678: 1677: 1667: 1648:10.1002/pro.4703 1627: 1621: 1620: 1580: 1574: 1573: 1563: 1523: 1517: 1516: 1488: 1482: 1481: 1471: 1439: 1433: 1432: 1422: 1398: 1392: 1391: 1381: 1353: 1347: 1344: 1338: 1337: 1297: 1291: 1290: 1258: 1252: 1251: 1234:(35): 10666–74. 1222: 1216: 1215: 1197: 1188:(15): 4691–700. 1177: 1171: 1170: 1160: 1137:Chemical Reviews 1128: 1115: 1114: 1086: 1080: 1079: 1069: 1051: 1027: 1021: 1020: 1010: 985:(7): 2903–2928. 979:Chemical Reviews 970: 964: 963: 934: 758: 632: 618: 580: 452: 422: 420: 419: 414: 268:biosynthesis of 192: 42: 30: 27:Class of enzymes 21: 3875: 3874: 3870: 3869: 3868: 3866: 3865: 3864: 3830: 3829: 3828: 3816: 3808: 3806: 3801: 3713:Oxidoreductases 3699: 3675:Enzyme kinetics 3663: 3659:List of enzymes 3632: 3601: 3572:Catalytic triad 3550: 3545: 3515: 3510: 3486: 3458: 3430: 3426:Alcohol oxidase 3411:Glucose oxidase 3392: 3359: 3128: 3117:Oxidoreductases 3114: 3084: 3070: 3065: 3023: 2985: 2972: 2950: 2900: 2864: 2837: 2801: 2796: 2760: 2755: 2703: 2682: 2661: 2631: 2593: 2589: 2587:Further reading 2584: 2570: 2566: 2514: 2513: 2509: 2484:10.1172/JCI8669 2465: 2464: 2460: 2430: 2429: 2425: 2394:(18): 6702–12. 2381: 2380: 2376: 2340: 2339: 2335: 2320: 2299: 2298: 2291: 2262:Cancer Research 2255: 2254: 2247: 2226:(24): 1917–26. 2217: 2216: 2212: 2176: 2175: 2171: 2125: 2124: 2120: 2084: 2083: 2079: 2043: 2042: 2035: 1993: 1992: 1988: 1942: 1941: 1937: 1893: 1892: 1885: 1843: 1842: 1838: 1794: 1793: 1789: 1737: 1736: 1732: 1686: 1685: 1681: 1636:Protein Science 1629: 1628: 1624: 1582: 1581: 1577: 1525: 1524: 1520: 1490: 1489: 1485: 1441: 1440: 1436: 1400: 1399: 1395: 1355: 1354: 1350: 1345: 1341: 1299: 1298: 1294: 1260: 1259: 1255: 1224: 1223: 1219: 1195:10.1.1.488.2542 1179: 1178: 1174: 1130: 1129: 1118: 1097:(2–3): 163–84. 1088: 1087: 1083: 1029: 1028: 1024: 972: 971: 967: 936: 935: 931: 927: 910: 894: 839: 635: 616: 405: 404: 401: 375: 308: 286: 45: 28: 23: 22: 15: 12: 11: 5: 3873: 3871: 3863: 3862: 3857: 3852: 3847: 3842: 3832: 3831: 3827: 3826: 3803: 3802: 3800: 3799: 3786: 3773: 3760: 3747: 3734: 3721: 3707: 3705: 3701: 3700: 3698: 3697: 3692: 3687: 3682: 3677: 3671: 3669: 3665: 3664: 3662: 3661: 3656: 3651: 3646: 3640: 3638: 3637:Classification 3634: 3633: 3631: 3630: 3625: 3620: 3615: 3609: 3607: 3603: 3602: 3600: 3599: 3594: 3589: 3584: 3579: 3574: 3569: 3564: 3558: 3556: 3552: 3551: 3546: 3544: 3543: 3536: 3529: 3521: 3512: 3511: 3509: 3508: 3503: 3497: 3495: 3488: 3487: 3485: 3484: 3479: 3473: 3471: 3460: 3459: 3457: 3456: 3451: 3445: 3443: 3432: 3431: 3429: 3428: 3423: 3418: 3413: 3407: 3405: 3394: 3393: 3391: 3390: 3385: 3380: 3374: 3372: 3361: 3360: 3358: 3357: 3352: 3351: 3350: 3345: 3335: 3334: 3333: 3328: 3311: 3310: 3305: 3300: 3295: 3290: 3285: 3280: 3275: 3270: 3265: 3260: 3255: 3250: 3245: 3240: 3235: 3230: 3225: 3220: 3215: 3210: 3205: 3204: 3203: 3198: 3193: 3188: 3183: 3178: 3173: 3163: 3158: 3153: 3147: 3145: 3130: 3129: 3115: 3113: 3112: 3105: 3098: 3090: 3067: 3066: 3064: 3063: 3058: 3053: 3051:DCMP deaminase 3048: 3043: 3037: 3035: 3029: 3028: 3025: 3024: 3022: 3021: 3012: 3003: 2997: 2995: 2991: 2990: 2987: 2986: 2984: 2983: 2981:CTP synthetase 2977: 2974: 2973: 2971: 2970: 2961: 2955: 2952: 2951: 2949: 2948: 2947: 2946: 2944:Dihydroorotase 2941: 2936: 2925: 2919: 2912: 2906: 2905: 2902: 2901: 2899: 2898: 2893: 2888: 2883: 2878: 2872: 2870: 2866: 2865: 2863: 2862: 2857: 2851: 2849: 2843: 2842: 2839: 2838: 2836: 2835: 2834: 2833: 2823: 2818: 2812: 2810: 2798: 2797: 2795: 2794: 2793: 2792: 2782: 2777: 2771: 2769: 2757: 2756: 2754: 2753: 2748: 2743: 2738: 2733: 2728: 2723: 2717: 2715: 2697: 2690: 2684: 2683: 2681: 2680: 2672: 2662: 2660: 2659: 2652: 2645: 2637: 2630: 2629: 2590: 2588: 2585: 2583: 2582: 2564: 2507: 2478:(4): 599–606. 2458: 2423: 2374: 2333: 2318: 2289: 2268:(20): 5826–8. 2245: 2210: 2169: 2118: 2077: 2050:Molecular Cell 2033: 2006:(1–3): 72–78. 1986: 1935: 1883: 1856:(4): 279–289. 1836: 1787: 1750:(2): 342–359. 1730: 1699:(12): 7960–9. 1679: 1622: 1595:(2): 282–289. 1575: 1518: 1483: 1454:(Pt 1): 41–7. 1434: 1413:(3): 1435–40. 1393: 1348: 1339: 1312:(6): 975–985. 1292: 1253: 1217: 1172: 1143:(7): 2903–28. 1116: 1081: 1022: 965: 928: 926: 923: 922: 921: 916: 909: 906: 893: 890: 838: 835: 787: 786: 783: 782: 777: 773: 772: 767: 763: 762: 754: 753: 743: 737: 736: 731: 725: 724: 720: 719: 714: 708: 707: 702: 696: 695: 690: 684: 683: 678: 672: 671: 666: 660: 659: 656: 652: 651: 646: 642: 641: 637: 636: 633: 625: 624: 615: 612: 609: 608: 605: 604: 599: 595: 594: 589: 585: 584: 576: 575: 565: 559: 558: 553: 547: 546: 542: 541: 536: 530: 529: 524: 518: 517: 512: 506: 505: 500: 494: 493: 488: 482: 481: 478: 474: 473: 468: 464: 463: 459: 458: 428: 427: 412: 399: 374: 371: 306: 285: 282: 237: 236: 233: 232: 227: 221: 220: 215: 209: 208: 203: 197: 196: 188: 187: 178: 172: 171: 160: 153: 152: 147: 141: 140: 135: 129: 128: 123: 117: 116: 111: 105: 104: 99: 93: 92: 87: 81: 80: 76: 75: 70: 64: 63: 58: 52: 51: 47: 46: 43: 35: 34: 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 3872: 3861: 3858: 3856: 3853: 3851: 3848: 3846: 3843: 3841: 3838: 3837: 3835: 3825: 3820: 3815: 3811: 3797: 3793: 3792: 3787: 3784: 3780: 3779: 3774: 3771: 3767: 3766: 3761: 3758: 3754: 3753: 3748: 3745: 3741: 3740: 3735: 3732: 3728: 3727: 3722: 3719: 3715: 3714: 3709: 3708: 3706: 3702: 3696: 3693: 3691: 3688: 3686: 3683: 3681: 3678: 3676: 3673: 3672: 3670: 3666: 3660: 3657: 3655: 3654:Enzyme family 3652: 3650: 3647: 3645: 3642: 3641: 3639: 3635: 3629: 3626: 3624: 3621: 3619: 3618:Cooperativity 3616: 3614: 3611: 3610: 3608: 3604: 3598: 3595: 3593: 3590: 3588: 3585: 3583: 3580: 3578: 3577:Oxyanion hole 3575: 3573: 3570: 3568: 3565: 3563: 3560: 3559: 3557: 3553: 3549: 3542: 3537: 3535: 3530: 3528: 3523: 3522: 3519: 3507: 3504: 3502: 3499: 3498: 3496: 3493: 3489: 3483: 3480: 3478: 3475: 3474: 3472: 3469: 3465: 3461: 3455: 3452: 3450: 3447: 3446: 3444: 3441: 3437: 3433: 3427: 3424: 3422: 3419: 3417: 3414: 3412: 3409: 3408: 3406: 3403: 3399: 3395: 3389: 3386: 3384: 3381: 3379: 3376: 3375: 3373: 3370: 3366: 3362: 3356: 3353: 3349: 3346: 3344: 3341: 3340: 3339: 3336: 3332: 3329: 3327: 3324: 3323: 3322: 3319: 3317: 3313: 3312: 3309: 3306: 3304: 3301: 3299: 3296: 3294: 3291: 3289: 3286: 3284: 3281: 3279: 3276: 3274: 3271: 3269: 3266: 3264: 3261: 3259: 3256: 3254: 3251: 3249: 3246: 3244: 3241: 3239: 3236: 3234: 3231: 3229: 3226: 3224: 3221: 3219: 3216: 3214: 3211: 3209: 3206: 3202: 3199: 3197: 3194: 3192: 3189: 3187: 3184: 3182: 3179: 3177: 3174: 3172: 3169: 3168: 3167: 3164: 3162: 3159: 3157: 3154: 3152: 3149: 3148: 3146: 3143: 3139: 3135: 3131: 3126: 3122: 3118: 3111: 3106: 3104: 3099: 3097: 3092: 3091: 3088: 3083: 3079: 3075: 3062: 3059: 3057: 3054: 3052: 3049: 3047: 3044: 3042: 3039: 3038: 3036: 3034: 3030: 3020: 3016: 3013: 3011: 3007: 3004: 3002: 2999: 2998: 2996: 2992: 2982: 2979: 2978: 2975: 2969: 2965: 2962: 2960: 2957: 2956: 2953: 2945: 2942: 2940: 2937: 2935: 2932: 2931: 2930: 2927: 2926: 2923: 2920: 2916: 2913: 2911: 2907: 2897: 2896:Urate oxidase 2894: 2892: 2889: 2887: 2884: 2882: 2879: 2877: 2874: 2873: 2871: 2867: 2861: 2858: 2856: 2853: 2852: 2850: 2848: 2844: 2832: 2831:GMP reductase 2829: 2828: 2827: 2824: 2822: 2819: 2817: 2814: 2813: 2811: 2808: 2806: 2799: 2791: 2790:AMP deaminase 2788: 2787: 2786: 2783: 2781: 2778: 2776: 2773: 2772: 2770: 2767: 2765: 2758: 2752: 2749: 2747: 2744: 2742: 2739: 2737: 2734: 2732: 2729: 2727: 2724: 2722: 2719: 2718: 2716: 2713: 2711: 2707: 2701: 2698: 2694: 2691: 2689: 2685: 2679: 2676: 2673: 2671: 2667: 2664: 2663: 2658: 2653: 2651: 2646: 2644: 2639: 2638: 2635: 2626: 2622: 2618: 2614: 2610: 2606: 2602: 2598: 2592: 2591: 2586: 2580: 2576: 2575: 2568: 2565: 2560: 2556: 2552: 2548: 2543: 2538: 2534: 2530: 2526: 2522: 2518: 2511: 2508: 2503: 2499: 2494: 2489: 2485: 2481: 2477: 2473: 2469: 2462: 2459: 2454: 2450: 2446: 2442: 2438: 2434: 2427: 2424: 2419: 2415: 2410: 2405: 2401: 2397: 2393: 2389: 2385: 2378: 2375: 2370: 2366: 2361: 2356: 2353:(6): 641–50. 2352: 2348: 2344: 2337: 2334: 2329: 2325: 2321: 2315: 2311: 2307: 2303: 2296: 2294: 2290: 2285: 2281: 2276: 2271: 2267: 2263: 2259: 2252: 2250: 2246: 2241: 2237: 2233: 2229: 2225: 2221: 2220:Life Sciences 2214: 2211: 2206: 2202: 2197: 2192: 2189:(9): 5292–5. 2188: 2184: 2180: 2173: 2170: 2165: 2161: 2156: 2151: 2146: 2141: 2137: 2133: 2129: 2122: 2119: 2114: 2110: 2105: 2100: 2096: 2092: 2091:J. Biol. Chem 2088: 2081: 2078: 2073: 2069: 2064: 2059: 2055: 2051: 2047: 2040: 2038: 2034: 2029: 2025: 2021: 2017: 2013: 2009: 2005: 2001: 1997: 1990: 1987: 1982: 1978: 1973: 1968: 1963: 1958: 1954: 1950: 1946: 1939: 1936: 1931: 1927: 1922: 1917: 1913: 1909: 1905: 1901: 1897: 1890: 1888: 1884: 1879: 1875: 1871: 1867: 1863: 1859: 1855: 1851: 1847: 1840: 1837: 1832: 1828: 1823: 1818: 1814: 1810: 1806: 1802: 1798: 1791: 1788: 1783: 1779: 1774: 1769: 1765: 1761: 1757: 1753: 1749: 1745: 1741: 1734: 1731: 1726: 1722: 1717: 1712: 1707: 1702: 1698: 1694: 1690: 1683: 1680: 1675: 1671: 1666: 1661: 1657: 1653: 1649: 1645: 1641: 1637: 1633: 1626: 1623: 1618: 1614: 1610: 1606: 1602: 1598: 1594: 1590: 1586: 1579: 1576: 1571: 1567: 1562: 1557: 1553: 1549: 1545: 1541: 1537: 1533: 1529: 1522: 1519: 1514: 1510: 1506: 1502: 1498: 1494: 1487: 1484: 1479: 1475: 1470: 1465: 1461: 1457: 1453: 1449: 1445: 1438: 1435: 1430: 1426: 1421: 1416: 1412: 1408: 1404: 1397: 1394: 1389: 1385: 1380: 1375: 1372:(1): 339–50. 1371: 1367: 1366:J. Biol. Chem 1363: 1361: 1352: 1349: 1343: 1340: 1335: 1331: 1327: 1323: 1319: 1315: 1311: 1307: 1303: 1296: 1293: 1288: 1284: 1280: 1276: 1273:(2): 517–27. 1272: 1268: 1264: 1257: 1254: 1249: 1245: 1241: 1237: 1233: 1229: 1221: 1218: 1213: 1209: 1205: 1201: 1196: 1191: 1187: 1183: 1176: 1173: 1168: 1164: 1159: 1154: 1150: 1146: 1142: 1138: 1134: 1127: 1125: 1123: 1121: 1117: 1112: 1108: 1104: 1100: 1096: 1092: 1085: 1082: 1077: 1073: 1068: 1063: 1059: 1055: 1050: 1045: 1041: 1037: 1033: 1026: 1023: 1018: 1014: 1009: 1004: 1000: 996: 992: 988: 984: 980: 976: 969: 966: 961: 957: 953: 949: 946:(4): 857–63. 945: 941: 933: 930: 924: 920: 917: 915: 912: 911: 907: 905: 903: 899: 891: 889: 887: 884:and dominant 883: 880: 877: 873: 868: 866: 862: 861:Mycophenolate 858: 856: 853: 849: 845: 836: 834: 832: 828: 825: 821: 817: 813: 808: 806: 805: 800: 799: 794: 781: 778: 774: 771: 768: 764: 759: 755: 752: 751: 747: 744: 742: 738: 735: 732: 730: 726: 721: 718: 715: 713: 709: 706: 703: 701: 697: 694: 691: 689: 685: 682: 679: 677: 673: 670: 667: 665: 661: 657: 653: 650: 647: 643: 638: 631: 626: 623: 619: 613: 603: 600: 596: 593: 590: 586: 581: 577: 574: 573: 569: 566: 564: 560: 557: 554: 552: 548: 543: 540: 537: 535: 531: 528: 525: 523: 519: 516: 513: 511: 507: 504: 501: 499: 495: 492: 489: 487: 483: 479: 475: 472: 469: 465: 460: 457: 453: 450: 447: 443: 438: 433: 425: 403: 395: 391: 388: 387: 386: 379: 372: 370: 368: 364: 360: 356: 352: 348: 343: 339: 338: 333: 332: 327: 323: 322: 316: 314: 310: 297: 293: 291: 283: 281: 279: 275: 271: 267: 263: 259: 255: 251: 248:biosynthetic 247: 244:(IMPDH) is a 243: 231: 228: 226: 222: 219: 216: 214: 210: 207: 204: 202: 198: 193: 189: 186: 182: 179: 177: 176:Gene Ontology 173: 170: 167: 164: 161: 158: 154: 151: 148: 146: 142: 139: 136: 134: 130: 127: 124: 122: 118: 115: 114:NiceZyme view 112: 110: 106: 103: 100: 98: 94: 91: 88: 86: 82: 77: 74: 71: 69: 65: 62: 59: 57: 53: 48: 41: 36: 31: 19: 3791:Translocases 3788: 3775: 3762: 3749: 3736: 3726:Transferases 3723: 3710: 3567:Binding site 3314: 2825: 2821:GMP synthase 2802: 2784: 2761: 2751:IMP synthase 2704: 2603:(5): 711–7. 2600: 2596: 2572: 2567: 2524: 2520: 2510: 2475: 2471: 2461: 2436: 2432: 2426: 2391: 2387: 2377: 2350: 2346: 2336: 2301: 2265: 2261: 2223: 2219: 2213: 2186: 2182: 2172: 2135: 2132:PLOS Biology 2131: 2121: 2094: 2090: 2080: 2056:(1): 133–9. 2053: 2049: 2003: 2000:FEBS Letters 1999: 1989: 1952: 1948: 1938: 1906:(1): 34–42. 1903: 1899: 1853: 1849: 1839: 1804: 1800: 1790: 1747: 1743: 1733: 1696: 1692: 1682: 1642:(8): e4703. 1639: 1635: 1625: 1592: 1588: 1578: 1535: 1531: 1521: 1499:(2): 282–9. 1496: 1492: 1486: 1451: 1447: 1437: 1410: 1406: 1396: 1369: 1365: 1359: 1351: 1342: 1309: 1305: 1295: 1270: 1267:J. Mol. Biol 1266: 1262: 1256: 1231: 1228:Biochemistry 1227: 1220: 1185: 1182:Biochemistry 1181: 1175: 1140: 1136: 1094: 1090: 1084: 1039: 1035: 1025: 982: 978: 968: 943: 940:Biochemistry 939: 932: 895: 871: 869: 859: 855:chemotherapy 840: 830: 823: 819: 815: 811: 809: 802: 796: 790: 748: 655:Alt. symbols 570: 477:Alt. symbols 429: 384: 350: 347:moonlighting 335: 329: 325: 319: 317: 302: 287: 278:glycoprotein 265: 241: 240: 102:BRENDA entry 3562:Active site 3442:as acceptor 2574:NCT04356677 2439:(1): 31–7. 2138:(8): e206. 1538:(1): 8923. 844:lymphocytes 770:Swiss-model 640:Identifiers 592:Swiss-model 462:Identifiers 90:IntEnz view 50:Identifiers 3834:Categories 3765:Isomerases 3739:Hydrolases 3606:Regulation 3369:cytochrome 2994:Catabolism 2869:Catabolism 2675:nucleotide 2666:Metabolism 925:References 919:Xanthosine 898:SARS-CoV-2 766:Structures 761:Search for 723:Other data 588:Structures 583:Search for 545:Other data 426:+ NADH + H 357:genes and 290:tetrameric 159:structures 126:KEGG entry 73:9028-93-7 3644:EC number 3440:disulfide 3082:IPR001093 2918:Anabolism 2696:Anabolism 2551:1476-4687 2020:0014-5793 1870:0300-9084 1850:Biochimie 1764:1365-2958 1656:0961-8368 1609:1046-5928 1552:2041-1723 1326:1878-4186 1190:CiteSeerX 1058:1663-9812 999:0009-2665 876:autosomal 734:1.1.1.205 729:EC number 705:NM_000884 664:NCBI gene 614:In humans 572:q31.3-q32 556:1.1.1.205 551:EC number 527:NM_000883 486:NCBI gene 446:threonine 411:⇌ 373:Mechanism 260:(IMP) to 79:Databases 61:1.1.1.205 3850:EC 1.1.1 3668:Kinetics 3592:Cofactor 3555:Activity 3404:acceptor 3371:acceptor 3348:11β-HSD2 3343:11β-HSD1 3144:acceptor 3078:InterPro 2625:12718828 2617:17851563 2559:32408336 2502:10953035 2453:12538032 2418:12944494 2369:14981049 2164:18752347 2072:22658723 2028:12062412 1981:18974094 1930:16384941 1878:12106905 1831:14766016 1782:18312263 1725:19153081 1674:37338125 1665:10357500 1617:10545277 1570:26558346 1513:10545277 1478:15882147 1388:13428767 1334:23643948 1287:12559919 1212:10200156 1167:19480389 1111:10878288 1076:38444943 1067:10912719 1017:19480389 960:12549902 908:See also 902:COVID-19 892:Research 879:dominant 827:knockout 793:isozymes 780:InterPro 602:InterPro 442:arginine 437:cysteine 367:G2 phase 326:in vitro 321:in vitro 230:proteins 218:articles 206:articles 163:RCSB PDB 3824:Biology 3778:Ligases 3548:Enzymes 3468:quinone 2826:reverse 2785:reverse 2678:enzymes 2529:Bibcode 2328:9752721 2284:1356621 2240:7910933 2205:1969416 2155:2525682 2113:2902093 1972:2605994 1921:2581444 1822:1224093 1773:2279236 1716:2658089 1561:4660370 1469:1184561 1429:8576135 1248:9271497 1158:2737513 1008:2737513 776:Domains 712:UniProt 598:Domains 534:UniProt 363:S phase 355:histone 342:adenine 337:E. coli 331:in vivo 270:guanine 266:de novo 185:QuickGO 150:profile 133:MetaCyc 68:CAS no. 3810:Portal 3752:Lyases 3506:L2HGDH 3492:1.1.99 3402:oxygen 3326:3β-HSD 2623:  2615:  2557:  2549:  2521:Nature 2500:  2493:380246 2490:  2451:  2416:  2409:193693 2406:  2367:  2326:  2316:  2282:  2238:  2203:  2162:  2152:  2111:  2070:  2026:  2018:  1979:  1969:  1928:  1918:  1876:  1868:  1829:  1819:  1780:  1770:  1762:  1723:  1713:  1672:  1662:  1654:  1615:  1607:  1568:  1558:  1550:  1511:  1476:  1466:  1427:  1386:  1332:  1324:  1285:  1246:  1210:  1192:  1165:  1155:  1109:  1074:  1064:  1056:  1015:  1005:  997:  958:  872:IMPDH1 852:cancer 831:IMPDH2 824:IMPDH1 820:IMPDH2 816:IMPDH1 812:IMPDH1 804:IMPDH2 798:IMPDH1 746:Chr. 3 717:P12268 700:RefSeq 693:146691 649:IMPDH2 645:Symbol 568:Chr. 7 539:P20839 522:RefSeq 515:146690 471:IMPDH1 467:Symbol 309:barrel 250:enzyme 246:purine 213:PubMed 195:Search 181:AmiGO 169:PDBsum 109:ExPASy 97:BRENDA 85:IntEnz 56:EC no. 3704:Types 3464:1.1.5 3436:1.1.4 3398:1.1.3 3365:1.1.2 3331:NSDHL 3134:1.1.1 2621:S2CID 750:p21.2 741:Locus 658:IMPD2 563:Locus 432:redox 305:(β/α) 145:PRIAM 3796:list 3789:EC7 3783:list 3776:EC6 3770:list 3763:EC5 3757:list 3750:EC4 3744:list 3737:EC3 3731:list 3724:EC2 3718:list 3711:EC1 3181:1B10 3142:NADP 3127:1.1) 3076:and 3074:Pfam 3019:UPB1 3010:DPYS 2803:IMP→ 2762:IMP→ 2613:PMID 2555:PMID 2547:ISSN 2498:PMID 2449:PMID 2414:PMID 2365:PMID 2324:PMID 2314:ISBN 2280:PMID 2236:PMID 2201:PMID 2160:PMID 2109:PMID 2068:PMID 2024:PMID 2016:ISSN 1977:PMID 1926:PMID 1874:PMID 1866:ISSN 1827:PMID 1778:PMID 1760:ISSN 1721:PMID 1670:PMID 1652:ISSN 1613:PMID 1605:ISSN 1566:PMID 1548:ISSN 1509:PMID 1474:PMID 1425:PMID 1384:PMID 1330:PMID 1322:ISSN 1283:PMID 1244:PMID 1208:PMID 1163:PMID 1107:PMID 1072:PMID 1054:ISSN 1013:PMID 995:ISSN 956:PMID 850:and 801:and 688:OMIM 681:6053 676:HGNC 669:3615 510:OMIM 503:6052 498:HGNC 491:3614 480:RP10 444:and 225:NCBI 166:PDBe 121:KEGG 3355:17β 3338:11β 3201:7A2 3196:1C4 3191:1C3 3186:1C1 3176:1B1 3171:1A1 3138:NAD 2929:CAD 2805:GMP 2764:AMP 2710:IMP 2706:R5P 2605:doi 2537:doi 2525:583 2488:PMC 2480:doi 2476:106 2441:doi 2404:PMC 2396:doi 2355:doi 2306:doi 2270:doi 2228:doi 2191:doi 2187:265 2150:PMC 2140:doi 2099:doi 2095:263 2058:doi 2008:doi 2004:517 1967:PMC 1957:doi 1953:283 1916:PMC 1908:doi 1858:doi 1817:PMC 1809:doi 1805:379 1768:PMC 1752:doi 1711:PMC 1701:doi 1697:284 1660:PMC 1644:doi 1597:doi 1556:PMC 1540:doi 1501:doi 1464:PMC 1456:doi 1452:390 1415:doi 1411:271 1374:doi 1370:226 1314:doi 1275:doi 1271:326 1236:doi 1200:doi 1153:PMC 1145:doi 1141:109 1099:doi 1062:PMC 1044:doi 1003:PMC 987:doi 983:109 948:doi 394:NAD 359:E2F 201:PMC 157:PDB 3836:: 3466:: 3438:: 3400:: 3367:: 3321:3β 3136:: 3125:EC 3119:: 3080:: 2668:: 2619:. 2611:. 2601:83 2599:. 2553:. 2545:. 2535:. 2523:. 2519:. 2496:. 2486:. 2474:. 2470:. 2447:. 2435:. 2412:. 2402:. 2392:23 2390:. 2386:. 2363:. 2351:13 2349:. 2345:. 2322:. 2312:. 2292:^ 2278:. 2266:52 2264:. 2260:. 2248:^ 2234:. 2224:54 2222:. 2199:. 2185:. 2181:. 2158:. 2148:. 2134:. 2130:. 2107:. 2093:. 2089:. 2066:. 2054:47 2052:. 2048:. 2036:^ 2022:. 2014:. 2002:. 1998:. 1975:. 1965:. 1951:. 1947:. 1924:. 1914:. 1904:47 1902:. 1898:. 1886:^ 1872:. 1864:. 1854:84 1852:. 1848:. 1825:. 1815:. 1803:. 1799:. 1776:. 1766:. 1758:. 1748:68 1746:. 1742:. 1719:. 1709:. 1695:. 1691:. 1668:. 1658:. 1650:. 1640:32 1638:. 1634:. 1611:. 1603:. 1593:17 1591:. 1587:. 1564:. 1554:. 1546:. 1534:. 1530:. 1507:. 1497:17 1495:. 1472:. 1462:. 1450:. 1446:. 1423:. 1409:. 1405:. 1382:. 1368:. 1364:. 1328:. 1320:. 1310:21 1308:. 1304:. 1281:. 1269:. 1242:. 1232:36 1230:. 1206:. 1198:. 1186:38 1184:. 1161:. 1151:. 1139:. 1135:. 1119:^ 1105:. 1095:47 1093:. 1070:. 1060:. 1052:. 1042:. 1040:15 1038:. 1034:. 1011:. 1001:. 993:. 981:. 977:. 954:. 944:42 942:. 904:. 888:. 857:. 807:. 396:+ 392:+ 183:/ 3812:: 3798:) 3794:( 3785:) 3781:( 3772:) 3768:( 3759:) 3755:( 3746:) 3742:( 3733:) 3729:( 3720:) 3716:( 3540:e 3533:t 3526:v 3318:: 3140:/ 3123:( 3109:e 3102:t 3095:v 3017:/ 3008:/ 2966:/ 2807:: 2766:: 2712:: 2708:→ 2656:e 2649:t 2642:v 2627:. 2607:: 2561:. 2539:: 2531:: 2504:. 2482:: 2455:. 2443:: 2437:3 2420:. 2398:: 2371:. 2357:: 2330:. 2308:: 2286:. 2272:: 2242:. 2230:: 2207:. 2193:: 2166:. 2142:: 2136:6 2115:. 2101:: 2074:. 2060:: 2030:. 2010:: 1983:. 1959:: 1932:. 1910:: 1880:. 1860:: 1833:. 1811:: 1784:. 1754:: 1727:. 1703:: 1676:. 1646:: 1619:. 1599:: 1572:. 1542:: 1536:6 1515:. 1503:: 1480:. 1458:: 1431:. 1417:: 1390:. 1376:: 1362:" 1336:. 1316:: 1289:. 1277:: 1250:. 1238:: 1214:. 1202:: 1169:. 1147:: 1113:. 1101:: 1078:. 1046:: 1019:. 989:: 962:. 950:: 402:O 400:2 398:H 307:8 20:)

Index

Inosine monophosphate dehydrogenase

EC no.
1.1.1.205
CAS no.
9028-93-7
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
Gene Ontology
AmiGO
QuickGO
PMC
articles
PubMed
articles
NCBI

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