Drugbank Logo

Showing drug card for Mycophenolic acid (DB01024)

Legend: drug field target field enzyme field

for drugs
Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:31
Primary Accession Number DB01024
Secondary Accession Number
  • APRD01603
  • EXPT02208
Name Mycophenolic acid
Drug Type
  • Approved
  • Small Molecule
Description Mycophenolic acid is an an immunosuppresant drug and potent anti-proliferative, and can be used in place of the older anti-proliferative azathioprine. It is usually used as part of triple therapy including a calcineurin inhibitor (ciclosporin or tacrolimus) and prednisolone. It is also useful in research for the selection of animal cells that express the E. coli gene coding for XGPRT (xanthine guanine phosphoribosyltransferase).
Synonyms
  1. Mycophenoic acid
Brand Names
  1. Melbex
  2. Myfortic
Brand Mixtures Not Available
Chemical IUPAC Name (E)-6-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1H-2-benzofuran-5-yl)-4-methylhex-4-enoic acid
Chemical Formula C17H20O6
Chemical Structure Structure
CAS Registry Number 24280-93-1
InChI Identifier InChI=1/C17H20O6/c1-9(5-7-13(18)19)4-6-11-15(20)14-12(8-23-17(14)21)10(2)16(11)22-3/h4,20H,5-8H2,1-3H3,(H,18,19)/b9-4+/f/h18H
InChI Key HPNSFSBZBAHARI-NMYHMHKZDH
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound 446541 Link Image
PubChem Substance 602720 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID MOA Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02264560 Link Image
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Mycophenolic_acid Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 320.3371
Monoisotopic Molecular Weight 320.1260
State Solid
Melting Point 141 oC
Experimental Water Solubility Insoluble Source: PhysProp
Predicted Water Solubility 3.55e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.8 Source: PhysProp
Predicted LogP 2.36 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.96 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1MEH Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES COC1=C(C\C=C(/C)CCC(O)=O)C(O)=C2C(=O)OCC2=C1C
Canonical SMILES COC1=C(CC=C(C)CCC(O)=O)C(O)=C2C(=O)OCC2=C1C
Drug Category
  • Antibiotics, Antineoplastic
  • Enzyme Inhibitors
ATC Codes
AHFS Codes
  • 92:00.00
Indication For the prophylaxis of organ rejection in patients receiving allogeneic renal transplants, administered in combination with cyclosporine and corticosteroids.
Pharmacology Mycophenolic acid is an antibiotic substance derived from Penicillium stoloniferum. It blocks de novo biosynthesis of purine nucleotides by inhibition of the enzyme inosine monophosphate dehydrogenase. Mycophenolic acid is important because of its selective effects on the immune system. It prevents the proliferation of T-cells, lymphocytes, and the formation of antibodies from B-cells. It also may inhibit recruitment of leukocytes to inflammatory sites.
Mechanism of Action Mycophenolic acid is a potent, selective, uncompetitive, and reversible inhibitor of inosine monophosphate dehydrogenase (IMPDH), and therefore inhibits the de novo pathway of guanosine nucleotide synthesis without incorporation into DNA. Because T- and B-lymphocytes are critically dependent for their proliferation on de novo synthesis of purines, whereas other cell types can utilize salvage pathways, mycophenolic acid has potent cytostatic effects on lymphocytes. Mycophenolic acid inhibits proliferative responses of T- and B-lymphocytes to both mitogenic and allospecific stimulation. Addition of guanosine or deoxyguanosine reverses the cytostatic effects of mycophenolic acid on lymphocytes. Mycophenolic acid also suppresses antibody formation by B-lymphocytes. Mycophenolic acid prevents the glycosylation of lymphocyte and monocyte glycoproteins that are involved in intercellular adhesion to endothelial cells and may inhibit recruitment of leukocytes into sites of inflammation and graft rejection.
Absorption Bioavailability following oral administration of Myfortic delayed-release tablet ranges from 70-95%
Toxicity Oral (LD50): Acute: 352 mg/kg [Rat], 1000 mg/kg [Mouse], and >6000 mg/kg [Rabbit]. Possible signs and symptoms of acute overdose could include the following: hematological abnormalities such as leukopenia and neutropenia, and gastrointestinal symptoms such as abdominal pain, diarrhea, nausea and vomiting, and dyspepsia.
Protein Binding >98%
Biotransformation Mycophenolic acid is metabolized mainly by glucuronyl transferase to glucuronidated metabolites, predominantly the phenolic glucuronide, mycophenolic acid glucuronide (MPAG). MPAG does not manifest pharmacological activity. The acyl glucuronide minor metabolite has pharmacological activity similar to mycophenolic acid. The AUC ratio of Mycophenolic acid:MPAG:acyl glucuronide is approximately 1:24:0.28 at steady state.
Half Life The mean elimination half-life for mycophenolic acid ranges from 8-16 hours, while that of the MPAG metabolite ranges from 13-17 hours.
Dosage Forms
Form Route
Tablet, coated Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Woodroffe R, Yao GL, Meads C, Bayliss S, Ready A, Raftery J, Taylor RS: Clinical and cost-effectiveness of newer immunosuppressive regimens in renal transplantation: a systematic review and modelling study. Health Technol Assess. 2005 May;9(21):1-179, iii-iv. [PubMed Link Image]
  2. Drugs.com Link Image
  3. Wikipedia Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. UDP-glucuronosyltransferase 1-9 (UGT1A9)
  2. Glucuronosyltransferase
Targets
  1. Inosine-5'-monophosphate dehydrogenase 2
  2. Inosine-5'-monophosphate dehydrogenase 1
  3. Inosine-5'-monophosphate dehydrogenase
  4. Inosine-5'-monophosphate dehydrogenase 2
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name UDP-glucuronosyltransferase 1-9 (UGT1A9)
Enzyme 1 Gene Name UGT1A9
Enzyme 1 SwissProt ID O60656 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >UDP-glucuronosyltransferase 1-9 precursor, microsomal 
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Glucuronosyltransferase
Enzyme 2 Gene Name UGT1A1
Enzyme 2 SwissProt ID P22309 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P22309|UD11_HUMAN UDP-glucuronosyltransferase 1-1 precursor 
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Drug Target 1 [top]
Target 1 ID 796
Target 1 Name Inosine-5'-monophosphate dehydrogenase 2
Target 1 Synonyms
  1. EC 1.1.1.205
  2. IMP dehydrogenase 2
  3. IMPD 2
  4. IMPDH-II
Target 1 Gene Name IMPDH2
Target 1 Protein Sequence >Inosine-5'-monophosphate dehydrogenase 2 
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKIT
LKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVV
LSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMT
KREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDA
KKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVI
GGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVP
VIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAM
DKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVR
AMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Target 1 Number of Residues 522
Target 1 Molecular Weight 55806
Target 1 Theoretical pI 6.90
Target 1 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
IMP dehydrogenase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
GMP biosynthesis
Component
Not Available
Target 1 General Function Nucleotide transport and metabolism
Target 1 Specific Function Rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors
Target 1 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 1 Reactions
  • inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 307066 Link Image
Target 1 UniProtKB/Swiss-Prot ID P12268 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name IMDH2_HUMAN Link Image
Target 1 PDB ID 1NFB Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >1545 bp 
ATGGCCGACTACCTGATTAGTGGGGGCACGTCCTACGTGCCAGACGACGGACTCACAGCA
CAGCAGCTCTTCAACTGCGGAGACGGCCTCACCTACAATGACTTTCTCATTCTCCCTGGG
TACATCGACTTCACTGCAGACCAGGTGGACCTGACTTCTGCTCTGACCAAGAAAATCACT
CTTAAGACCCCACTGGTTTCCTCTCCCATGGACACAGTCACAGAGGCTGGGATGGCCATA
GCAATGGCGCTTACAGGCGGTATTGGCTTCATCCACCACAACTGTACACCTGAATTCCAG
GCCAATGAAGTTCGGAAAGTGAAGAAATATGAACAGGGATTCATCACAGACCCTGTGGTC
CTCAGCCCCAAGGATCGCGTGCGGGATGTTTTTGAGGCCAAGGCCCGGCATGGTTTCTGC
GGTATCCCAATCACAGACACAGGCCGGATGGGGAGCCGCTTGGTGGGCATCATCTCCTCC
AGGGACATTGATTTTCTCAAAGAGGAGGAACATGACTGTTTCTTGGAAGAGATAATGACA
AAGAGGGAAGACTTGGTGGTAGCCCCCCGCAGCATCACACTGAAGGAGGCAAATGAAATT
CTGCAGCGCAGCAAGAAGGGAAAGTTGCCCATTGTAAATGAAGATGATGAGCTTGTGGCC
ATCATTGCCCGGACAGACCTGAAGAAGAATCGGGACTACCCACTAGCCTCCAAAGATGCC
AAGAAACAGCTGCTGTGTGGGGCAGCCATTGGCACTCATGAGGATGACAAGTATAGGCTG
GACTTGCTCGCCCAGGCTGGTGTGGATGTAGTGGTTTTGGACTCTTCCCAGGGAAATTCC
ATCTTCCAGATCAATATGATCAAGTACATCAAAGACAAATACCCTAATCTCCAAGTCATT
GGAGGCAATGTGGTCACTGCTGCCCAGGCCAAGAACCTCATTGATGCAGGTGTGGATGCC
CTGCGGGTGGGCATGGGAAGTGGCTCCATCTGCATTACGCAGGAAGTGCTGGCCTGTGGG
CGGCCCCAAGCAACAGCAGTGTACAAGGTGTCAGAGTATGCACGGCGCTTTGGTGTTCCG
GTCATTGCTGATGGAGGAATCCAAAATGTGGGTCATATTGCGAAAGCCTTGGCCCTTGGG
GCCTCCACAGTCATGATGGGCTCTCTCCTGGCTGCCACCACTGAGGCCCCTGGTGAATAC
TTCTTTTCCGATGGGATCCGGCTAAAGAAATATCGCGGTATGGGTTCTCTCGATGCCATG
GACAAGCACCTCAGCAGCCAGAACAGATATTTCAGTGAAGCTGACAAAATCAAAGTGGCC
CAGGGAGTGTCTGGTGCTGTGCAGGACAAAGGGTCAATCCACAAATTTGTCCCTTACCTG
ATTGCTGGCATCCAACACTCATGCCAGGACATTGGTGCCAAGAGCTTGACCCAAGTCCGA
GCCATGATGTACTCTGGGGAGCTTAAGTTTGAGAAGAGAACGTCCTCAGCCCAGGTGGAA
GGTGGCGTCCATAGCCTCCATTCGTATGAGAAGCGGCTTTTCTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID IMPDH2 Link Image
Target 1 GenAtlas ID IMPDH2 Link Image
Target 1 HGNC ID HGNC:6053 Link Image
Target 1 Chromosome Location 3
Target 1 Locus 3p21.2
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Colby TD, Vanderveen K, Strickler MD, Markham GD, Goldstein BM: Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3531-6. [PubMed Link Image]
  2. Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K: Two distinct cDNAs for human IMP dehydrogenase. J Biol Chem. 1990 Mar 25;265(9):5292-5. [PubMed Link Image]
  3. Collart FR, Huberman E: Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs. J Biol Chem. 1988 Oct 25;263(30):15769-72. [PubMed Link Image]
  4. Hager PW, Collart FR, Huberman E, Mitchell BS: Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding. Biochem Pharmacol. 1995 May 11;49(9):1323-9. [PubMed Link Image]
  5. Zimmermann AG, Spychala J, Mitchell BS: Characterization of the human inosine-5'-monophosphate dehydrogenase type II gene. J Biol Chem. 1995 Mar 24;270(12):6808-14. [PubMed Link Image]
  6. Glesne DA, Huberman E: Cloning and sequence of the human type II IMP dehydrogenase gene. Biochem Biophys Res Commun. 1994 Nov 30;205(1):537-44. [PubMed Link Image]
  7. Glesne D, Collart F, Varkony T, Drabkin H, Huberman E: Chromosomal localization and structure of the human type II IMP dehydrogenase gene (IMPDH2). Genomics. 1993 Apr;16(1):274-7. [PubMed Link Image]
Target 1 Drug References
  1. Penuelas S, Noe V, Morales R, Ciudad CJ: Sensitization of human erythroleukemia K562 cells resistant to methotrexate by inhibiting IMPDH. Med Sci Monit. 2005 Jan;11(1):BR6-12. [PubMed Link Image]
  2. Vannozzi F, Filipponi F, Di Paolo A, Danesi R, Urbani L, Bocci G, Catalano G, De Simone P, Mosca F, Del Tacca M: An exploratory study on pharmacogenetics of inosine-monophosphate dehydrogenase II in peripheral mononuclear cells from liver-transplant recipients. Transplant Proc. 2004 Nov;36(9):2787-90. [PubMed Link Image]
  3. Dzidic A, Prgomet C, Mohr A, Meyer K, Bauer J, Meyer HH, Pfaffl MW: Effects of mycophenolic acid on inosine monophosphate dehydrogenase I and II mRNA expression in white blood cells and various tissues in sheep. J Vet Med A Physiol Pathol Clin Med. 2006 May;53(4):163-9. [PubMed Link Image]
  4. Yam P, Jensen M, Akkina R, Anderson J, Villacres MC, Wu J, Zaia JA, Yee JK: Ex vivo selection and expansion of cells based on expression of a mutated inosine monophosphate dehydrogenase 2 after HIV vector transduction: effects on lymphocytes, monocytes, and CD34+ stem cells. Mol Ther. 2006 Aug;14(2):236-44. Epub 2006 May 2. [PubMed Link Image]
  5. Wang J, Zeevi A, Webber S, Girnita DM, Addonizio L, Selby R, Hutchinson IV, Burckart GJ: A novel variant L263F in human inosine 5'-monophosphate dehydrogenase 2 is associated with diminished enzyme activity. Pharmacogenet Genomics. 2007 Apr;17(4):283-90. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 838
Target 2 Name Inosine-5'-monophosphate dehydrogenase 1
Target 2 Synonyms
  1. EC 1.1.1.205
  2. IMP dehydrogenase 1
  3. IMPD 1
  4. IMPDH-I
Target 2 Gene Name IMPDH1
Target 2 Protein Sequence >Inosine-5'-monophosphate dehydrogenase 1 
MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKIT
LKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVV
LSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMT
PRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDS
QKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVI
GGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVP
IIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAM
EKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLR
SMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY
Target 2 Number of Residues 522
Target 2 Molecular Weight 55407
Target 2 Theoretical pI 6.90
Target 2 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
IMP dehydrogenase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
GMP biosynthesis
Component
Not Available
Target 2 General Function Nucleotide transport and metabolism
Target 2 Specific Function Rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors
Target 2 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 2 Reactions
  • inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 307067 Link Image
Target 2 UniProtKB/Swiss-Prot ID P20839 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name IMDH1_HUMAN Link Image
Target 2 PDB ID 1JCN Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >1545 bp 
ATGGCGGACTACCTGATCAGCGGCGGCACCGGCTACGTGCCCGAGGATGGGCTCACCGCG
CAGCAGCTCTTCGCCAGCGCCGACGACCTCACCTACAACGACTTCCTGATTCTCCCAGGA
TTCATAGACTTCATAGCTGATGAGGTGGACCTGACCTCAGCCCTGACCCGGAAGATCACG
CTGAAGACGCCACTCATCTCCTCCCCCATGGACACTGTGACAGAGGCTGACATGGCCATT
GCCATGGCTCTGATGGGAGGTATTGGGTTCATTCACCACAACTGCACCCCAGAGTTCCAG
GCCAATGAAGTACGCAAGGTCAAGAACTTTGAACAGGGCTTCATCACGGACCCTGTGGTG
CTGAGCCCCTCGCACACTGTGGGCGATGTGCTGGAGGCCAAGATGCGGCATGGCTTCTCT
GGCATCCCCATCACTGAGACGGGCACCATGGGCAGCAAGCTGGTGGGCATCGTCACCTCC
CGAGACATCGACTTTCTTGCTGAGAAGGACCACACCACCCTCCTCAGTGAGGTGATGACG
CCAAGGATTGAACTGGTGGTGGCTCCAGCAGGTGTGACGTTGAAAGAGGCAAATGAGATC
CTGCAGCGTAGCAAGAAAGGGAAGCTGCCTATCGTCAATGATTGCGATGAGCTGGTGGCC
ATCATCGCCCGCACCGACCTGAAGAAGAATCGAGACTACCCTCTGGCCTCCAAGGATTCC
CAGAAGCAGCTGCTCTGTGGGGCAGCTGTGGGCACCCGTGAGGATGACAAATACCGTCTG
GACCTGCTGACCCAGGCGGGGGTCGACGTCATAGTCTTCCACTCGTCCCAAGGGAATTCG
GTGTATCAGATCGCCATGGTGCATTACATCAAACAGAAGTACCCCCACCTCCAGGTGATT
GGGGGGAACGTGGTGACAGCAGCCCAGGCCAAGAACCTGATTGATGCTGGTGTGGACGGG
CTGCGCGTGGGCATGGGCTGCGGCTCCATCTGCATCACCCAGGAAGTGATGGCCTGTGGT
CGGCCCCAGGGCACTGCTGTGTACAAGGTGGCTGAGTATGCCCGGCGCTTTGGTGTGCCC
ATCATAGCCGATGGCGGCATCCAGACCGTGGGACACGTGGTCAAGGCCCTGGCCCTTGGA
GCCTCCACAGTGATGATGGGCTCCCTGCTGGCCGCCACTACGGAGGCCCCTGGCGAGTAC
TTCTTCTCAGACGGGGTGCGGCTCAAGAAGTACCGGGGCATGGGCTCACTGGATCCCATG
GAGAAGAGCAGCAGCAGCCAGAAACGATACTTCAGCGAGGGGGATAAAGTGAAGATCGCA
CAGGGTGTCTCGGGCTCCATCCAGGACAAAGGATCCATTCAGAAGTTCGTGCCCTACCTC
ATAGCAGGCATCCAACACGGCTGCCAGGATATCGGGGCCCGCAGCCTGTCTGTCCTTCGG
TCCATGATGTACTCAGGAGAGCTCAAGTTTGAGAAGCGGACCATGTCGCCCCAGATTGAG
GGTGGTGTCCATGGCCTGCACTCTTACGAAAAGCGGCTGTACTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID IMPDH1 Link Image
Target 2 GenAtlas ID IMPDH1 Link Image
Target 2 HGNC ID HGNC:6052 Link Image
Target 2 Chromosome Location 7
Target 2 Locus 7q31.3-q32
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. 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: 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. 2002 Mar 1;11(5):547-57. [PubMed Link Image]
  2. Bowne SJ, Sullivan LS, Blanton SH, Cepko CL, Blackshaw S, Birch DG, Hughbanks-Wheaton D, Heckenlively JR, Daiger SP: Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa. Hum Mol Genet. 2002 Mar 1;11(5):559-68. [PubMed Link Image]
  3. Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K: Two distinct cDNAs for human IMP dehydrogenase. J Biol Chem. 1990 Mar 25;265(9):5292-5. [PubMed Link Image]
  4. Hager PW, Collart FR, Huberman E, Mitchell BS: Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding. Biochem Pharmacol. 1995 May 11;49(9):1323-9. [PubMed Link Image]
Target 2 Drug References
  1. Dzidic A, Prgomet C, Mohr A, Meyer K, Bauer J, Meyer HH, Pfaffl MW: Effects of mycophenolic acid on inosine monophosphate dehydrogenase I and II mRNA expression in white blood cells and various tissues in sheep. J Vet Med A Physiol Pathol Clin Med. 2006 May;53(4):163-9. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 2316
Target 3 Name Inosine-5'-monophosphate dehydrogenase
Target 3 Synonyms
  1. EC 1.1.1.205
  2. IMP dehydrogenase
  3. IMPD
  4. IMPDH
Target 3 Gene Name IMPDH
Target 3 Protein Sequence >Inosine-5'-monophosphate dehydrogenase 
MAKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLKIPLVSAIMQ
SVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKAGFVVSDSNVKPDQTFADVL
AISQRTTHNTVAVTDDGTPHGVLLGLVTQRDYPIDLTQTETKVSDMMTPFSKLVTAHQDT
KLSEANKIIWEKKLNALPIIDDDQHLRYIVFRKDYDRSQVCHNELVDSQKRYLVGAGINT
RDFRERVPALVEAGADVLCIDSSDGFSEWQKITIGWIREKYGDKVKVGAGNIVDGEGFRY
LADAGADFIKIGIGGGSICITREQKGIGRGQATAVIDVVAERNKYFEETGIYIPVCSDGG
IVYDYHMTLALAMGADFIMLGRYFARFEESPTRKVTINGSVMKEYWGEGSSRARNWQRYD
LGGKQKLSFEEGVDSYVPYAGKLKDNVEASLNKVKSTMCNCGALTIPQLQSKAKITLVSS
VSIVEGGAHDVIVKDRINDYHPK
Target 3 Number of Residues 511
Target 3 Molecular Weight 55474
Target 3 Theoretical pI 6.67
Target 3 GO Classification
Function
catalytic activity
Process
Not Available
Component
Not Available
Target 3 General Function Nucleotide transport and metabolism
Target 3 Specific Function Rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth
Target 3 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 3 Reactions
  • inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein 1352865 Link Image
Target 3 UniProtKB/Swiss-Prot ID P50097 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name IMDH_TRIFO Link Image
Target 3 PDB ID 1MEW Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >1512 bp 
ATGGCAAAATACTACAACGAACCATGCCACACCTTTAACGAATATCTCCTCATTCCAGGA
CTCTCAACAGTCGACTGCATTCCATCCAACGTTAACTTATCTACCCCACTCGTCAAGTTC
CAAAAGGGGCAACAAAGTGAGATCAATTTAAAGATCCCCCTTGTTTCTGCCATCATGCAA
TCTGTCTCAGGAGAAAAGATGGCTATCGCATTGGCACGAGAAGGTGGTATTTCATTCATT
TTCGGATCTCAATCAATTGAAAGCCAAGCAGCCATGGTCCATGCTGTCAAAAATTTCAAA
GCCGGCTTTGTCGTCTCAGATTCAAACGTTAAACCAGATCAAACATTTGCTGATGTTTTA
GCAATTTCTCAACGAACAACCCACAACACTGTCGCTGTCACAGACGATGGAACTCCACAT
GGAGTTTTACTTGGTTTGGTCACTCAACGCGATTATCCAATCGATCTTACCCAGACCGAA
ACAAAGGTTTCCGACATGATGACACCATTCAGCAAGCTCGTTACAGCCCATCAGGACACA
AAACTTTCAGAAGCCAACAAAATTATTTGGGAGAAGAAATTAAATGCTCTTCCTATCATT
GATGACGATCAACATCTTCGTTATATCGTTTTCCGCAAAGATTATGACAGATCGCAAGTC
TGTCACAACGAACTCGTCGATTCGCAAAAACGCTATTTGGTCGGAGCAGGAATTAACACA
CGCGACTTCAGAGAACGCGTTCCAGCACTTGTCGAAGCCGGCGCTGATGTCCTTTGCATT
GATTCCAGCGACGGCTTCTCAGAATGGCAGAAAATTACAATCGGCTGGATTCGCGAGAAA
TACGGCGATAAAGTTAAAGTTGGTGCGGGAAACATTGTTGACGGTGAAGGATTCCGCTAT
TTGGCCGACGCTGGAGCTGATTTCATCAAGATTGGAATTGGCGGTGGATCAATTTGCATC
ACACGCGAGCAGAAAGGTATCGGCCGAGGCCAAGCTACTGCCGTCATTGATGTTGTTGCA
GAGCGTAACAAATACTTCGAAGAGACCGGAATTTATATCCCTGTTTGCTCTGATGGTGGA
ATTGTTTATGATTATCACATGACACTTGCTCTTGCAATGGGCGCAGATTTCATCATGCTT
GGCAGGTACTTCGCCCGTTTTGAGGAGTCACCAACAAGAAAAGTGACAATTAATGGAAGC
GTTATGAAGGAGTACTGGGGAGAAGGCTCTTCGCGCGCTAGGAACTGGCAGCGCTATGAC
CTTGGAGGTAAGCAGAAGCTTTCCTTTGAAGAGGGAGTCGATTCTTACGTCCCATACGCT
GGAAAGTTGAAGGACAACGTGGAGGCATCCTTGAACAAGGTAAAATCAACGATGTGCAAC
TGTGGAGCGCTCACAATCCCGCAGCTCCAGAGCAAGGCAAAGATCACACTTGTATCATCA
GTTTCAATTGTCGAAGGAGGCGCACACGATGTTATTGTTAAGGACAGGATTAACGACTAT
CACCCAAAATAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Huete-Perez JA, Wu JC, Whitby FG, Wang CC: Identification of the IMP binding site in the IMP dehydrogenase from Tritrichomonas foetus. Biochemistry. 1995 Oct 24;34(42):13889-94. [PubMed Link Image]
  2. Beck JT, Zhao S, Wang CC: Cloning, sequencing, and structural analysis of the DNA encoding inosine monophosphate dehydrogenase (EC 1.1.1.205) from Tritrichomonas foetus. Exp Parasitol. 1994 Feb;78(1):101-12. [PubMed Link Image]
  3. Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC: Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. Biochemistry. 1997 Sep 2;36(35):10666-74. [PubMed Link Image]
Target 3 Drug References Not Available
Drug Target 4 [top]
Target 4 ID 2354
Target 4 Name Inosine-5'-monophosphate dehydrogenase 2
Target 4 Synonyms
  1. EC 1.1.1.205
  2. IMP dehydrogenase 2
  3. IMPD 2
  4. IMPDH-II
Target 4 Gene Name IMPDH2
Target 4 Protein Sequence >Inosine-5'-monophosphate dehydrogenase 2 
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKIT
LKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVV
LSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDRFLEEIMT
KREDLVVAPAGITLKEANEILQRSKKGKLPIVNENDELVAIIARTDLKKNRDYPLASKDA
KKQLLCGAAIGTHEDDKYRLDLLALAGVDVVVLDSSQGNSIFQINMIKYMKEKYPNLQVI
GGNVVTAAQAKNLIDAGVDALRVGMGCGSICITQEVLACGRPQATAVYKVSEYARRFGVP
VIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAM
DKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVR
AMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Target 4 Number of Residues 522
Target 4 Molecular Weight 55891
Target 4 Theoretical pI 7.30
Target 4 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
IMP dehydrogenase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
purine nucleotide metabolism
purine nucleotide biosynthesis
purine nucleoside monophosphate biosynthesis
purine ribonucleoside monophosphate biosynthesis
GMP biosynthesis
Component
Not Available
Target 4 General Function Nucleotide transport and metabolism
Target 4 Specific Function Rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors
Target 4 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 4 Reactions
  • inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Essential
Target 4 GenBank ID Protein 304517 Link Image
Target 4 UniProtKB/Swiss-Prot ID P12269 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name IMDH2_CRIGR Link Image
Target 4 PDB ID 1JR1 Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location Not Available
Target 4 Gene Sequence >1545 bp 
ATGGCGGACTACCTGATTAGCGGAGGCACATCTTACGTGCCCGACGACGGGCTCACAGCG
CAGCAGCTCTTCAACTGCGGGGATGGCCTCACCTACAACGATTTTCTCATTCTTCCTGGG
TATATCGACTTCACTGCCGACCAAGTGGATTTGACCTCTGCTCTAACTAAGAAGATCACC
CTGAAGACCCCACTGGTTTCCTCACCTATGGACACTGTCACAGAGGCTGGAATGGCCATT
GCAATGGCGCTTACAGGAGGTATTGGCTTCATCCACCACAACTGTACACCTGAATTCCAG
GCCAATGAAGTTCGGAAAGTAAAGAAATATGAACAGGGATTCATAACTGATCCTGTAGTC
CTTAGCCCCAAGGATCGTGTGAGGGATGTTTTTGAAGCCAAAGCCAGGCATGGCTTCTGT
GGTATCCCCATCACAGATACAGGCCGGATGGGGAGTCGACTGGTGGGCATCATTTCTTCA
AGGGATATTGATTTTCTCAAGGAGGAAGAGCATGACCGTTTCTTGGAGGAGATCATGACA
AAGAGGGAAGATTTGGTGGTGGCCCCTGCAGGCATCACTCTGAAGGAGGCAAATGAAATT
CTGCAGCGCAGTAAAAAGGGAAAGTTGCCCATTGTGAATGAAAATGATGAGCTGGTAGCC
ATCATTGCTCGGACAGACCTGAAGAAGAATCGTGATTACCCATTGGCTTCCAAAGATGCC
AAAAAGCAGCTACTATGTGGGGCAGCCATTGGTACTCATGAGGATGACAAGTATAGGCTG
GACTTACTGGCTCTTGCTGGTGTGGATGTAGTGGTTTTGGACTCTTCCCAGGGAAACTCC
ATTTTCCAAATCAATATGATCAAATACATGAAAGAGAAATACCCCAATCTCCAAGTCATT
GGAGGCAATGTAGTCACTGCTGCTCAAGCCAAGAACCTCATAGACGCAGGTGTGGATGCT
CTGCGAGTTGGCATGGGGTGTGGTTCCATCTGCATTACTCAGGAAGTGTTGGCCTGTGGT
CGGCCCCAAGCAACAGCAGTGTACAAGGTTTCTGAGTATGCTCGGCGCTTTGGTGTTCCT
GTTATTGCTGATGGAGGAATCCAAAATGTGGGTCATATTGCCAAAGCTTTGGCTCTTGGA
GCTTCTACAGTCATGATGGGCTCCCTCTTGGCTGCCACCACCGAAGCCCCTGGTGAGTAC
TTCTTCTCAGATGGGATCCGGCTAAAAAAGTACCGTGGTATGGGTTCTCTTGATGCCATG
GACAAGCATCTCAGCAGCCAGAACCGATATTTCAGTGAAGCTGACAAAATCAAAGTGGCC
CAAGGAGTTTCAGGAGCTGTGCAGGACAAAGGGTCTATCCACAAGTTCGTCCCTTATTTG
ATTGCTGGCATCCAGCATTCCTGTCAGGACATTGGTGCCAAGAGTTTAACCCAAGTCAGA
GCCATGATGTACTCTGGGGAACTCAAGTTTGAGAAGAGAACATCCTCAGCTCAGGTGGAA
GGTGGTGTCCACAGCCTTCATTCGTATGAGAAGCGGCTTTTCTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID Not Available
Target 4 HGNC ID Not Available
Target 4 Chromosome Location Not Available
Target 4 Locus Not Available
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Collart FR, Huberman E: Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs. J Biol Chem. 1988 Oct 25;263(30):15769-72. [PubMed Link Image]
  2. Sintchak MD, Fleming MA, Futer O, Raybuck SA, Chambers SP, Caron PR, Murcko MA, Wilson KP: Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid. Cell. 1996 Jun 14;85(6):921-30. [PubMed Link Image]
Target 4 Drug References Not Available

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.