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Record Information
StatusExpected but not Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2017-12-20 20:30:23 UTC
Secondary Accession Numbers
  • HMDB01554
Metabolite Identification
Common NameXanthylic acid
DescriptionXanthylic acid is an important metabolic intermediate in the Purine Metabolism, and is a product or substrate of the enzymes Inosine monophosphate dehydrogenase (EC, Hypoxanthine phosphoribosyltransferase (EC, Xanthine phosphoribosyltransferase (EC, 5'-Ribonucleotide phosphohydrolase (EC, Ap4A hydrolase (EC, Nucleoside-triphosphate diphosphatase (EC, Phosphoribosylamine-glycine ligase (EC, and glutamine amidotransferase (EC (KEGG) Xanthylic acid can also be used in quantitative measurements of the Inosine monophosphate dehydrogenase enzyme activities in purine metabolism. This measurement is important for optimal thiopurine therapy for children with acute lymphoblastic leukaemia (ALL). (PMID: 16725387 ).
Xanthosine 5'-phosphateChEBI
Xanthosine monophosphateChEBI
(9-D-Ribosylxanthine)-5'-phosphoric acidGenerator
Xanthosine 5'-phosphoric acidGenerator
Xanthosine monophosphoric acidGenerator
5'-Xanthonylate monophosphateHMDB
Xanthosine monophosphate, 8-(14)C-labeledMeSH
Chemical FormulaC10H13N4O9P
Average Molecular Weight364.2054
Monoisotopic Molecular Weight364.042014546
IUPAC Name{[(2R,3S,4R,5R)-5-(2,6-dioxo-2,3,6,9-tetrahydro-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}phosphonic acid
Traditional Namexanthosine monophosphate
CAS Registry Number523-98-8
InChI Identifier
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as purine ribonucleoside monophosphates. These are nucleotides consisting of a purine base linked to a ribose to which one monophosphate group is attached.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
ClassPurine nucleotides
Sub ClassPurine ribonucleotides
Direct ParentPurine ribonucleoside monophosphates
Alternative Parents
  • Purine ribonucleoside monophosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • Xanthine
  • 6-oxopurine
  • Monosaccharide phosphate
  • Pentose monosaccharide
  • Purinone
  • Imidazopyrimidine
  • Purine
  • Alkaloid or derivatives
  • Monoalkyl phosphate
  • Pyrimidone
  • Monosaccharide
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Alkyl phosphate
  • Phosphoric acid ester
  • Pyrimidine
  • Heteroaromatic compound
  • Azole
  • Vinylogous amide
  • Imidazole
  • Tetrahydrofuran
  • Lactam
  • 1,2-diol
  • Urea
  • Secondary alcohol
  • Azacycle
  • Oxacycle
  • Organoheterocyclic compound
  • Alcohol
  • Organic oxide
  • Organonitrogen compound
  • Organopnictogen compound
  • Organic oxygen compound
  • Organooxygen compound
  • Hydrocarbon derivative
  • Organic nitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors

Biological location:



Route of exposure:





Naturally occurring process:

  Biological process:

    Biochemical pathway:

Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
Water Solubility2.49 g/LALOGPS
pKa (Strongest Acidic)1.26ChemAxon
pKa (Strongest Basic)0.069ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count9ChemAxon
Hydrogen Donor Count6ChemAxon
Polar Surface Area192.47 ŲChemAxon
Rotatable Bond Count4ChemAxon
Refractivity73.08 m³·mol⁻¹ChemAxon
Polarizability29.99 ųChemAxon
Number of Rings3ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0002-9613000000-3054f73e4c9456039ed6View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positivesplash10-01ot-9521200000-1e6fc3c628d8ebd23b37View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF , negativesplash10-0ik9-7964000000-bce7ee60221f82790f35View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF , positivesplash10-0002-9400000000-05c1ae772c001a15a8c6View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0udi-0913000000-d17f1d77b992fc6e9f04View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0udi-0900000000-efbdb918f50ba610575dView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0udi-2900000000-cf070bd16aacd3dcb6fbView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0imi-6509000000-d931cb1dcaeba678220cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0fbc-9300000000-e596281ec38113a9653cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9100000000-1caa46ecd17db343ddd3View in MoNA
Biological Properties
Cellular Locations
  • Cytoplasm
Biofluid LocationsNot Available
Tissue LocationNot Available
2-Hydroxyglutric Aciduria (D And L Form)ThumbThumb?image type=greyscaleThumb?image type=simpleNot Available
4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase DeficiencyThumbThumb?image type=greyscaleThumb?image type=simpleNot Available
AICA-RibosiduriaThumbThumb?image type=greyscaleThumb?image type=simpleNot Available
Adenine phosphoribosyltransferase deficiency (APRT)ThumbThumb?image type=greyscaleThumb?image type=simpleNot Available
Adenosine Deaminase DeficiencyThumbThumb?image type=greyscaleThumb?image type=simpleNot Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FoodDB IDFDB022687
KNApSAcK IDC00007396
Chemspider ID66054
KEGG Compound IDC00655
BiGG ID35623
Wikipedia LinkXanthosine monophosphate
METLIN IDNot Available
PubChem Compound73323
PDB IDNot Available
ChEBI ID15652
Synthesis ReferenceHattori, Kyoji; Kawahara, Shin; Hagiwara, Takeshige. 5'-Xanthylic acid. Jpn. Kokai Tokkyo Koho (1985), 3 pp.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Wolan DW, Cheong CG, Greasley SE, Wilson IA: Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor. Biochemistry. 2004 Feb 10;43(5):1171-83. [PubMed:14756553 ]
  2. Vethe NT, Bergan S: Determination of inosine monophosphate dehydrogenase activity in human CD4+ cells isolated from whole blood during mycophenolic acid therapy. Ther Drug Monit. 2006 Oct;28(5):608-13. [PubMed:17038874 ]
  3. Khalil PN, Erb N, Khalil MN, Escherich G, Janka-Schaub GE: Validation and application of a high-performance liquid chromatographic-based assay for determination of the inosine 5'-monophosphate dehydrogenase activity in erythrocytes. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Sep 14;842(1):1-7. Epub 2006 May 24. [PubMed:16725387 ]
  4. Barsotti C, Pesi R, Giannecchini M, Ipata PL: Evidence for the involvement of cytosolic 5'-nucleotidase (cN-II) in the synthesis of guanine nucleotides from xanthosine. J Biol Chem. 2005 Apr 8;280(14):13465-9. Epub 2005 Feb 6. [PubMed:15699053 ]
  5. Prosise GL, Luecke H: Crystal structures of Tritrichomonasfoetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism. J Mol Biol. 2003 Feb 14;326(2):517-27. [PubMed:12559919 ]
  6. Stoychev G, Kierdaszuk B, Shugar D: Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems. Eur J Biochem. 2002 Aug;269(16):4048-57. [PubMed:12180982 ]
  7. Daxecker H, Raab M, Muller MM: Influence of mycophenolic acid on inosine 5'-monophosphate dehydrogenase activity in human peripheral blood mononuclear cells. Clin Chim Acta. 2002 Apr;318(1-2):71-7. [PubMed:11880114 ]
  8. Rauniyar RK, Suzuma K, King AL, Aiello LP, King GL: Differential effects of bactericidal/permeability-increasing protein (BPI) analogues on retinal neovascularization and retinal pericyte growth. Invest Ophthalmol Vis Sci. 2002 Feb;43(2):503-9. [PubMed:11818397 ]
  9. Glander P, Braun KP, Hambach P, Bauer S, Mai I, Roots I, Waiser J, Fritsche L, Neumayer HH, Budde K: Non-radioactive determination of inosine 5'-monophosphate dehydro-genase (IMPDH) in peripheral mononuclear cells. Clin Biochem. 2001 Oct;34(7):543-9. [PubMed:11738390 ]
  10. Frueh FW, Hayashibara KC, Brown PO, Whitlock JP Jr: Use of cDNA microarrays to analyze dioxin-induced changes in human liver gene expression. Toxicol Lett. 2001 Jul 6;122(3):189-203. [PubMed:11489354 ]
  11. Wall M, Shim JH, Benkovic SJ: Human AICAR transformylase: role of the 4-carboxamide of AICAR in binding and catalysis. Biochemistry. 2000 Sep 19;39(37):11303-11. [PubMed:10985775 ]
  12. Sintchak MD, Nimmesgern E: The structure of inosine 5'-monophosphate dehydrogenase and the design of novel inhibitors. Immunopharmacology. 2000 May;47(2-3):163-84. [PubMed:10878288 ]
  13. Albrecht W, Storck M, Pfetsch E, Martin W, Abendroth D: Development and application of a high-performance liquid chromatography-based assay for determination of the activity of inosine 5'-monophosphate dehydrogenase in whole blood and isolated mononuclear cells. Ther Drug Monit. 2000 Jun;22(3):283-94. [PubMed:10850395 ]
  14. McMillan FM, Cahoon M, White A, Hedstrom L, Petsko GA, Ringe D: Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6. Biochemistry. 2000 Apr 18;39(15):4533-42. [PubMed:10758003 ]
  15. Markland W, McQuaid TJ, Jain J, Kwong AD: Broad-spectrum antiviral activity of the IMP dehydrogenase inhibitor VX-497: a comparison with ribavirin and demonstration of antiviral additivity with alpha interferon. Antimicrob Agents Chemother. 2000 Apr;44(4):859-66. [PubMed:10722482 ]
  16. Digits JA, Hedstrom L: Drug selectivity is determined by coupling across the NAD+ site of IMP dehydrogenase. Biochemistry. 2000 Feb 22;39(7):1771-7. [PubMed:10677226 ]
  17. Digits JA, Hedstrom L: Species-specific inhibition of inosine 5'-monophosphate dehydrogenase by mycophenolic acid. Biochemistry. 1999 Nov 16;38(46):15388-97. [PubMed:10563825 ]
  18. Heroux A, White EL, Ross LJ, Davis RL, Borhani DW: Crystal structure of Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase with XMP, pyrophosphate, and two Mg(2+) ions bound: insights into the catalytic mechanism. Biochemistry. 1999 Nov 2;38(44):14495-506. [PubMed:10545171 ]
  19. Heroux A, White EL, Ross LJ, Borhani DW: Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex. Biochemistry. 1999 Nov 2;38(44):14485-94. [PubMed:10545170 ]
  20. Pitera JW, Munagala NR, Wang CC, Kollman PA: Understanding substrate specificity in human and parasite phosphoribosyltransferases through calculation and experiment. Biochemistry. 1999 Aug 10;38(32):10298-306. [PubMed:10441123 ]
  21. Minakawa N, Matsuda A: Mechanism-based design of inosine 5-monophosphate dehydrogenase inhibitors: synthesis and biological activities of 5-ethynyl-1-beta-D-ribofuranosylimidazole-4-carboxamide (EICAR) and its derivatives. Curr Med Chem. 1999 Jul;6(7):615-28. [PubMed:10390604 ]
  22. Franchetti P, Grifantini M: Nucleoside and non-nucleoside IMP dehydrogenase inhibitors as antitumor and antiviral agents. Curr Med Chem. 1999 Jul;6(7):599-614. [PubMed:10390603 ]
  23. Jayaram HN, Cooney DA, Grusch M, Krupitza G: Consequences of IMP dehydrogenase inhibition, and its relationship to cancer and apoptosis. Curr Med Chem. 1999 Jul;6(7):561-74. [PubMed:10390601 ]
  24. Hedstrom L: IMP dehydrogenase: mechanism of action and inhibition. Curr Med Chem. 1999 Jul;6(7):545-60. [PubMed:10390600 ]

Only showing the first 10 proteins. There are 14 proteins in total.


General function:
Involved in hydrolase activity
Specific function:
Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.
Gene Name:
Uniprot ID:
Molecular weight:
Xanthylic acid + Water → Xanthosine + Phosphoric aciddetails
General function:
Involved in nucleotide binding
Specific function:
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels (By similarity).
Gene Name:
Uniprot ID:
Molecular weight:
Xanthylic acid + Water → Xanthosine + Phosphoric aciddetails
General function:
Involved in nucleotide binding
Specific function:
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia.
Gene Name:
Uniprot ID:
Molecular weight:
Xanthylic acid + Water → Xanthosine + Phosphoric aciddetails
General function:
Involved in metal ion binding
Specific function:
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP.
Gene Name:
Uniprot ID:
Molecular weight:
Not Available
Xanthylic acid + Water → Xanthosine + Phosphoric aciddetails
General function:
Involved in phosphatase activity
Specific function:
Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP.
Gene Name:
Uniprot ID:
Molecular weight:
Not Available
Xanthylic acid + Water → Xanthosine + Phosphoric aciddetails
General function:
Involved in hydrolase activity
Specific function:
Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Gene Name:
Uniprot ID:
Molecular weight:
Xanthosine 5-triphosphate + Water → Xanthylic acid + Pyrophosphatedetails
General function:
Involved in hypoxanthine phosphoribosyltransferase activity
Specific function:
Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.
Gene Name:
Uniprot ID:
Molecular weight:
Xanthylic acid + Pyrophosphate → Xanthine + Phosphoribosyl pyrophosphatedetails
General function:
Involved in catalytic activity
Specific function:
Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.
Gene Name:
Uniprot ID:
Molecular weight:
Adenosine triphosphate + Xanthylic acid + L-Glutamine + Water → Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate + L-Glutamic aciddetails
Adenosine triphosphate + Xanthylic acid + Ammonia → Adenosine monophosphate + Pyrophosphate + Guanosine monophosphatedetails
General function:
Involved in hydrolase activity
Specific function:
Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
Gene Name:
Uniprot ID:
Molecular weight:
P1,P4-Bis(5'-xanthosyl) tetraphosphate + Water → Xanthosine 5-triphosphate + Xanthylic aciddetails
General function:
Involved in catalytic activity
Specific function:
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
Gene Name:
Uniprot ID:
Molecular weight:
Inosinic acid + NAD + Water → Xanthylic acid + NADHdetails
Inosinic acid + NAD + Water → Xanthylic acid + NADH + Hydrogen Iondetails

Only showing the first 10 proteins. There are 14 proteins in total.