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Human Metabolome Database Version 2.5

 

Showing metabocard for Xanthine (HMDB00292)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-09 00:11:27
Accession Number HMDB00292
Secondary Accession Numbers Not Available
Common Name Xanthine
Description A purine base found in most body tissues and fluids, certain plants, and some urinary calculi. It is an intermediate in the degradation of adenosine monophosphate to uric acid, being formed by oxidation of hypoxanthine. The methylated xanthine compounds caffeine, theobromine, and theophylline and their derivatives are used in medicine for their bronchodilator effects. (Dorland, 28th ed.)
Synonyms
  1. 1H-Purine-2,6-diol
  2. 2,6(1,3)-Purinedion
  3. 2,6-Dihydroxypurine
  4. 2,6-Dioxopurine
  5. 3,7-Dihydro-1H-purine-2,6-dione
  6. 3,7-dihydropurine-2,6-dione
  7. 9H-Purine-2,6(1H,3H)-dione
  8. 9H-Purine-2,6-diol
  9. Dioxopurine
  10. Isoxanthine
  11. Pseudoxanthine
  12. Purine-2,6(1H,3H)-dione
  13. Purine-2,6-diol
  14. Xanthic oxide
  15. Xanthin
  16. Xanthine
Chemical IUPAC Name 2,6-dihydroxypurin
Chemical Formula C5H4N4O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Purines and Purine Derivatives
Sub Class
  • Hydroxy purines
Family
  • Mammalian Metabolite
Species
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Purine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 152.111
Monoisotopic Molecular Weight 152.033432
Isomeric SMILES O=C1NC(=O)C2=C(N1)N=CN2
Canonical SMILES O=C1NC(=O)C2=C(N1)N=CN2
KEGG Compound ID C00385 Link Image
BioCyc ID XANTHINE Link Image
BiGG ID 34825 Link Image
Wikipedia Link Xanthine Link Image
NuGOwiki Link HMDB00292 Link Image
Metagene Link HMDB00292 Link Image
METLIN ID 82 Link Image
PubChem Compound 1188 Link Image
PubChem Substance 149179 Link Image
ChEBI ID 17712 Link Image
CAS Registry Number 69-89-6
InChI Identifier InChI=1/C5H4N4O2/c10-4-2-3(7-1-6-2)8-5(11)9-4/h1H,(H3,6,7,8,9,10,11)
Synthesis Reference Procedure for the production of xanthine and xanthine-like materials. Fr. (1967), 4 pp.
Melting Point (Experimental) >300 oC
Experimental Water Solubility 0.069 mg/mL at 16 oC [MERCK INDEX [1996)]; 9.5 mg/mL (sodium salt, HMP experimental] Source: PhysProp
Predicted Water Solubility 4.91 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity -0.73 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -0.65 [Predicted by ALOGPS]; -1.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1A96 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • peroxisome
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Bladder —
Epidermis —
Fibroblasts —
Intestine —
Kidney —
Prostate —
Skeletal Muscle —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 0.35 +/- 0.19 uM
Age Adult:>18 yrs old
Sex Male
Patient information Overnight fast except for water, blood draw at 10.5 hours from start of experiment
Comments Not Available
References
  • Kaya M, Moriwaki Y, Ka T, Inokuchi T, Yamamoto A, Takahashi S, Tsutsumi Z, Tsuzita J, Oku Y, Yamamoto T: Plasma concentrations and urinary excretion of purine bases (uric acid, hypoxanthine, and xanthine) and oxypurinol after rigorous exercise. Metabolism. 2006 Jan;55(1):103-7. [PubMed Link Image]
Biofluid Blood
Value 0.45 (2.7-8.0) uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 0.91 +/- 0.45 uM
Age Adult:>18 yrs old
Sex Male
Patient information Overnight fast except for water, exercise performed at VO2 max 70%, blood draw at 11.5 hours from start of experiment
Comments Not Available
References
  • Kaya M, Moriwaki Y, Ka T, Inokuchi T, Yamamoto A, Takahashi S, Tsutsumi Z, Tsuzita J, Oku Y, Yamamoto T: Plasma concentrations and urinary excretion of purine bases (uric acid, hypoxanthine, and xanthine) and oxypurinol after rigorous exercise. Metabolism. 2006 Jan;55(1):103-7. [PubMed Link Image]
Biofluid Blood
Value 1.07 +/- 0.21 uM
Age Adult:>18 yrs old
Sex Male
Patient information Overnight fast except for water, exercise performed at VO2 max 70%, blood draw at 12.5 hours from start of experiment
Comments Not Available
References
  • Kaya M, Moriwaki Y, Ka T, Inokuchi T, Yamamoto A, Takahashi S, Tsutsumi Z, Tsuzita J, Oku Y, Yamamoto T: Plasma concentrations and urinary excretion of purine bases (uric acid, hypoxanthine, and xanthine) and oxypurinol after rigorous exercise. Metabolism. 2006 Jan;55(1):103-7. [PubMed Link Image]
Biofluid Blood
Value 0.99 +/- 0.48 uM
Age Adult:>18 yrs old
Sex Male
Patient information Overnight fast except for water, exercise performed at VO2 max 70%, blood draw at 13.5 hours from start of experiment
Comments Not Available
References
  • Kaya M, Moriwaki Y, Ka T, Inokuchi T, Yamamoto A, Takahashi S, Tsutsumi Z, Tsuzita J, Oku Y, Yamamoto T: Plasma concentrations and urinary excretion of purine bases (uric acid, hypoxanthine, and xanthine) and oxypurinol after rigorous exercise. Metabolism. 2006 Jan;55(1):103-7. [PubMed Link Image]
Biofluid Blood
Value 1.27 +/- 0.78 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Blood
Value 5.00 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid CSF
Value 5.20 (4.33-6.07) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Castro-Gago M, Rodriguez IN, Rodriguez-Nunez A, Guitian JP, Rocamonde SL, Rodriguez-Segade S: Therapeutic criteria in hydrocephalic children. Childs Nerv Syst. 1989 Dec;5(6):361-3. [PubMed Link Image]
Biofluid CSF
Value 13 +/- 7 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Urine
Value 2.6 (2.2-3.75) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 2.9 (1.3-4.6) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 2.2 +/- 0.3 uM
Age Adult:>18 yrs old
Sex Both
Condition Lesch-Nyhan syndrome
Comments Not Available
References
  • Harkness RA, McCreanor GM, Watts RW: Lesch-Nyhan syndrome and its pathogenesis: purine concentrations in plasma and urine with metabolite profiles in CSF. J Inherit Metab Dis. 1988;11(3):239-52. [PubMed Link Image]
Biofluid Blood
Value 6.37 +/- 1.95 uM
Age Adult:>18 yrs old
Sex Both
Condition Canavan disease
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Blood
Value 25.00 (10.00-40.00) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid CSF
Value 2.30 (2.10-2.50) uM
Age Adult:>18 yrs old
Sex Both
Condition Degenerative disc disease
Comments Not Available
References
  • Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed Link Image]
Biofluid CSF
Value 5.17 (3.64-6.70) uM
Age Adult:>18 yrs old
Sex Both
Condition Hydrocephalus
Comments Self-compensated hydrocephalics
References
  • Castro-Gago M, Rodriguez IN, Rodriguez-Nunez A, Guitian JP, Rocamonde SL, Rodriguez-Segade S: Therapeutic criteria in hydrocephalic children. Childs Nerv Syst. 1989 Dec;5(6):361-3. [PubMed Link Image]
Biofluid CSF
Value 9.90 (7.46-12.3) uM
Age Children:1-13 yrs old
Sex Both
Condition Hydrocephalus
Comments Non-compensated hydrocephalic infants and children (pre-shunt implanted)
References
  • Castro-Gago M, Rodriguez IN, Rodriguez-Nunez A, Guitian JP, Rocamonde SL, Rodriguez-Segade S: Therapeutic criteria in hydrocephalic children. Childs Nerv Syst. 1989 Dec;5(6):361-3. [PubMed Link Image]
Biofluid Urine
Value 131.5 (65.7-197.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Associated Disorders
Condition References
Canavan disease
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Degenerative disc disease
  • Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed Link Image]
Hydrocephalus
  • Castro-Gago M, Rodriguez IN, Rodriguez-Nunez A, Guitian JP, Rocamonde SL, Rodriguez-Segade S: Therapeutic criteria in hydrocephalic children. Childs Nerv Syst. 1989 Dec;5(6):361-3. [PubMed Link Image]
Lesch-Nyhan syndrome
  • Harkness RA, McCreanor GM, Watts RW: Lesch-Nyhan syndrome and its pathogenesis: purine concentrations in plasma and urine with metabolite profiles in CSF. J Inherit Metab Dis. 1988;11(3):239-52. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Ihara H, Shino Y, Morita Y, Kawaguchi E, Hashizume N, Yoshida M: Is skeletal muscle damaged by the oxidative stress following anaerobic exercise? J Clin Lab Anal. 2001;15(5):239-43. [PubMed Link Image]
  2. Niklasson F: Simultaneous liquid-chromatographic determination of hypoxanthine, xanthine, urate, and creatinine in cerebrospinal fluid, with direct injection. Clin Chem. 1983 Aug;29(8):1543-6. [PubMed Link Image]
  3. Teeuwen HW, Elbers EL, van Rossum JM: Rapid and sensitive gas-chromatographic determination of caffeine in blood plasma, saliva, and xanthine beverages. Mol Biol Rep. 1991 Feb;15(1):1-7. [PubMed Link Image]
  4. Castro-Gago M, Rodriguez IN, Rodriguez-Nunez A, Guitian JP, Rocamonde SL, Rodriguez-Segade S: Therapeutic criteria in hydrocephalic children. Childs Nerv Syst. 1989 Dec;5(6):361-3. [PubMed Link Image]
  5. Kaya M, Moriwaki Y, Ka T, Inokuchi T, Yamamoto A, Takahashi S, Tsutsumi Z, Tsuzita J, Oku Y, Yamamoto T: Plasma concentrations and urinary excretion of purine bases (uric acid, hypoxanthine, and xanthine) and oxypurinol after rigorous exercise. Metabolism. 2006 Jan;55(1):103-7. [PubMed Link Image]
  6. Liu Z, Li T, Wang E: Simultaneous determination of guanine, uric acid, hypoxanthine and xanthine in human plasma by reversed-phase high-performance liquid chromatography with amperometric detection. Analyst. 1995 Aug;120(8):2181-4. [PubMed Link Image]
  7. Becker MA, Kisicki J, Khosravan R, Wu J, Mulford D, Hunt B, MacDonald P, Joseph-Ridge N: Febuxostat (TMX-67), a novel, non-purine, selective inhibitor of xanthine oxidase, is safe and decreases serum urate in healthy volunteers. Nucleosides Nucleotides Nucleic Acids. 2004 Oct;23(8-9):1111-6. [PubMed Link Image]
  8. Kawasaki N, Tanimoto T, Tanaka A, Hayakawa T, Miyasaka N: Determination of non-protein-bound iron in human synovial fluid by high-performance liquid chromatography with electrochemical detection. J Chromatogr B Biomed Appl. 1994 Jun 17;656(2):436-40. [PubMed Link Image]
  9. Cooper N, Khosravan R, Erdmann C, Fiene J, Lee JW: Quantification of uric acid, xanthine and hypoxanthine in human serum by HPLC for pharmacodynamic studies. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Jun 6;837(1-2):1-10. Epub 2006 May 2. [PubMed Link Image]
  10. Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed Link Image]
  11. Kiss A, Barenyi M, Csontai A: Xanthine stone in the urinary bladder of a male child. Urol Int. 1999;63(4):242-4. [PubMed Link Image]
  12. Kjaergaard N, Moller-Petersen JF, Kristiansen FV, Petersen PL, Ekelund S, Skovbo P: Xanthine and hypoxanthine in amniotic fluid during pregnancy. Dan Med Bull. 1990 Dec;37(6):559-60. [PubMed Link Image]
  13. Wiley DM, Szabo I, Maguire MH, Finley BE, Bennett TL: Measurement of hypoxanthine and xanthine in late-gestation human amniotic fluid by reversed-phase high-performance liquid chromatography with photodiode-array detection. J Chromatogr. 1990 Nov 30;533:73-86. [PubMed Link Image]
  14. Gudbjornsson B, Zak A, Niklasson F, Hallgren R: Hypoxanthine, xanthine, and urate in synovial fluid from patients with inflammatory arthritides. Ann Rheum Dis. 1991 Oct;50(10):669-72. [PubMed Link Image]
  15. Ginsburg I: Could synergistic interactions among reactive oxygen species, proteinases, membrane-perforating enzymes, hydrolases, microbial hemolysins and cytokines be the main cause of tissue damage in infectious and inflammatory conditions? Med Hypotheses. 1998 Oct;51(4):337-46. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase
  2. Hypoxanthine-guanine phosphoribosyltransferase
  3. Purine nucleoside phosphorylase
  4. Guanine deaminase
  5. Guanine deaminase (Guanine deaminase, isoform CRA_b)
Enzyme 1 [top]
Enzyme 1 ID 5413
Enzyme 1 Name Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase
Enzyme 1 Synonyms
  1. XD
  2. Xanthine oxidase
  3. XO
  4. Xanthine oxidoreductase]
Enzyme 1 Gene Name XDH
Enzyme 1 Protein Sequence >Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase 
MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDR
LQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI
VMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCC
MNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAS
TLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFG
AACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISD
LNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSA
FKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKE
ELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLD
PTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRY
ENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDK
VTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDL
KKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKM
LGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGR
HPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGR
LCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKL
EGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGA
LLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAA
SVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLG
YSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAF
VQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAV
GEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVT
GVPENCKPWSVRV
Enzyme 1 Number of Residues 1333
Enzyme 1 Molecular Weight 146426
Enzyme 1 Theoretical pI 7.70
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function This enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups
Enzyme 1 Pathways
Enzyme 1 Reactions
  • xanthine + H2O + O2 = urate + H2O2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 10336525 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P47989 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name XDH_HUMAN Link Image
Enzyme 1 PDB ID 1V97 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >4002 bp 
ATGACAGCAGACAAATTGGTTTTCTTTGTGAATGGCAGAAAGGTGGTGGAGAAAAATGCA
GATCCAGAGACAACCCTTTTGGCCTACCTGAGAAGAAAGTTGGGGCTGAGTGGAACCAAG
CTCGGCTGTGGAGAGGGGGGCTGCGGGGCTTGCACAGTGATGCTCTCCAAGTATGATCGT
CTGCAGAACAAGATCGTCCACTTTTCTGCCAATGCCTGCCTGGCCCCCATCTGCTCCTTG
CACCATGTTGCAGTGACAACTGTGGAAGGAATAGGAAGCACCAAGACGAGGCTGCATCCT
GTGCAGGAGAGAATTGCCAAAAGCCACGGCTCCCAGTGCGGGTTCTGCACCCCTGGCATC
GTCATGAGTATGTACACACTGCTCCGGAATCAGCCCGAGCCCACCATGGAGGAGATTGAG
AATGCCTTCCAAGGAAATCTGTGCCGCTGCACAGGCTACAGACCCATCCTCCAGGGCTTC
CGGACCTTTGCCAGGGATGGTGGATGCTGTGGAGGAGATGGGAATAATCCAAATTGCTGC
ATGAACCAGAAGAAAGACCACTCAGTCAGCCTCTCGCCATCTTTATTCAAACCAGAGGAG
TTCACGCCCCTGGATCCAACCCAGGAGCCCATTTTTCCCCCAGAGTTGCTGAGGCTGAAA
GACACTCCTCGGAAGCAGCTGCGATTTGAAGGGGAGCGTGTGACGTGGATACAGGCCTCA
ACCCTCAAGGAGCTGCTGGACCTCAAGGCTCAGCACCCTGACGCCAAGCTGGTCGTGGGG
AACACGGAGATTGGCATTGAGATGAAGTTCAAGAATATGCTGTTTCCTATGATTGTCTGC
CCAGCCTGGATCCCTGAGCTGAATTCGGTAGAACATGGACCCGACGGTATCTCCTTTGGA
GCTGCTTGCCCCCTGAGCATTGTGGAAAAAACCCTGGTGGATGCTGTTGCTAAGCTTCCT
GCCCAAAAGACAGAGGTGTTCAGAGGGGTCCTGGAGCAGCTGCGCTGGTTTGCTGGGAAG
CAAGTCAAGTCTGTGGCGTCCGTTGGAGGGAACATCATCACTGCCAGCCCCATCTCCGAC
CTCAACCCCGTGTTCATGGCCAGTGGGGCCAAGCTGACACTTGTGTCCAGAGGCACCAGG
AGAACTGTCCAGATGGACCACACCTTCTTCCCTGGCTACAGAAAGACCCTGCTGAGCCCG
GAGGAGATACTGCTCTCCATAGAGATCCCCTACAGCAGGGAGGGGGAGTATTTCTCAGCA
TTCAAGCAGGCCTCCCGGAGAGAAGATGACATTGCCAAGGTAACCAGTGGCATGAGAGTT
TTATTCAAGCCAGGAACCACAGAGGTACAGGAGCTGGCCCTTTGCTATGGTGGAATGGCC
AACAGAACCATCTCAGCCCTCAAGACCACTCAGAGGCAGCTTTCCAAGCTCTGGAAGGAG
GAGCTGCTGCAGGACGTGTGTGCAGGACTGGCAGAGGAGCTGCATCTGCCTCCCGATGCC
CCTGGTGGCATGGTGGACTTCCGGTGCACCCTCACCCTCAGCTTCTTCTTCAAGTTCTAC
CTGACAGTCCTTCAGAAGCTGGGCCAAGAGAACCTGGAAGACAAGTGTGGTAAACTGGAC
CCCACTTTCGCCAGTGCAACTTTACTGTTTCAGAAAGACCCCCCAGCCGATGTCCAGCTC
TTCCAAGAGGTGCCCAAGGGTCAGTCTGAGGAGGACATGGTGGGCCGGCCCCTGCCCCAC
CTGGCAGCGGACATGCAGGCCTCTGGTGAGGCCGTGTACTGTGACGACATTCCTCGCTAC
GAGAATGAGCTGTCTCTCCGGCTGGTCACCAGCACCCGGGCCCACGCCAAGATCAAGTCC
ATAGATACATCAGAAGCTAAGAAGGTTCCAGGGTTTGTTTGTTTCATTTCCGCTGATGAT
GTTCCTGGGAGTAACATAACTGGAATTTGTAATGATGAGACAGTCTTTGCGAAGGATAAG
GTTACTTGTGTTGGGCATATCATTGGTGCTGTGGTTGCTGACACCCCGGAACACACACAG
AGAGCTGCCCAAGGGGTGAAAATCACCTATGAAGAACTACCAGCCATTATCACAATTGAG
GATGCTATAAAGAACAACTCCTTTTATGGACCTGAGCTGAAGATCGAGAAAGGGGACCTA
AAGAAGGGGTTTTCCGAAGCAGATAATGTTGTGTCAGGGGAGATATACATCGGTGGCCAA
GAGCACTTCTACCTGGAGACTCACTGCACCATTGCTGTTCCAAAAGGCGAGGCAGGGGAG
ATGGAGCTCTTTGTGTCTACACAGAACACCATGAAGACCCAGAGCTTTGTTGCAAAAATG
TTGGGGGTTCCAGCAAACCGGATTGTGGTTCGAGTGAAGAGAATGGGAGGAGGCTTTGGA
GGCAAGGAGACCCGGAGCACTGTGGTGTCCACGGCAGTGGCCCTGGCTGCATATAAGACC
GGCCGCCCTGTGCGATGCATGCTGGACCGTGATGAGGACATGCTGATAACTGGTGGCAGA
CATCCCTTCCTGGCCAGATACAAGGTTGGCTTCATGAAGACTGGGACAGTTGTGGCTCTT
GAGGTGGACCACTTCAGCAATGTGGGGAACACCCAGGATCTCTCTCAGAGTATTATGGAA
CGAGCTTTATTCCACATGGACAACTGCTATAAAATCCCCAACATCCGGGGCACTGGGCGG
CTGTGCAAAACCAACCTTCCCTCCAACACGGCCTTCCGGGGCTTTGGGGGGCCCCAGGGG
ATGCTCATTGCCGAGTGCTGGATGAGTGAAGTTGCAGTGACCTGTGGGATGCCTGCAGAG
GAGGTGCGGAGAAAAAACCTGTACAAAGAAGGGGACCTGACACACTTCAACCAGAAGCTT
GAGGGTTTCACCTTGCCCAGATGCTGGGAAGAATGCCTAGCAAGCTCTCAGTATCATGCT
CGGAAGAGTGAGGTTGACAAGTTCAACAAGGAGAATTGTTGGAAAAAGAGAGGATTGTGC
ATAATTCCCACCAAGTTTGGAATAAGCTTCACAGTTCCTTTTCTGAATCAGGCAGGAGCC
CTACTTCATGTGTACACAGATGGCTCTGTGCTGCTGACCCACGGGGGGACTGAGATGGGC
CAAGGCCTTCATACCAAAATGGTCCAGGTGGCCAGTAGAGCTCTGAAAATCCCCACCTCT
AAGATTTATATCAGCGAGACAAGCACTAACACTGTGCCCAACACCTCTCCCACGGCTGCC
TCTGTCAGCGCTGACCTCAATGGACAGGCCGTCTATGCGGCTTGTCAGACCATCTTGAAA
AGGCTGGAACCCTACAAGAAGAAGAATCCCAGTGGCTCCTGGGAAGACTGGGTCACAGCT
GCCTACATGGACACAGTGAGCTTGTCTGCCACTGGGTTTTATAGAACACCCAATCTGGGC
TACAGCTTTGAGACTAACTCAGGGAACCCCTTCCACTACTTCAGCTATGGGGTGGCTTGC
TCTGAAGTAGAAATCGACTGCCTAACAGGAGATCATAAGAACCTCCGCACAGATATTGTC
ATGGATGTTGGCTCCAGTCTAAACCCTGCCATTGATATTGGACAGGTGGAAGGGGCATTT
GTCCAGGGCCTTGGCCTCTTCACCCTAGAGGAGCTACACTATTCCCCCGAGGGGAGCCTG
CACACCCGTGGCCCTAGCACCTACAAGATCCCGGCATTTGGCAGCATCCCCATTGAGTTC
AGGGTGTCCCTGCTCCGCGACTGCCCCAACAAGAAGGCCATCTATGCATCGAAGGCTGTT
GGAGAGCCGCCCCTCTTCCTGGCTGCTTCTATCTTCTTTGCCATCAAAGATGCCATCCGT
GCAGCTCGAGCTCAGCACACAGGTAATAACGTGAAGGAACTCTTCCGGCTAGACAGCCCT
GCCACCCCGGAGAAGATCCGCAATGCCTGCGTGGACAAGTTCACCACCCTGTGTGTCACT
GGTGTCCCAGAAAACTGCAAACCCTGGTCTGTGAGGGTCTAA
Enzyme 1 GenBank Gene ID D11456 Link Image
Enzyme 1 GeneCard ID XDH Link Image
Enzyme 1 GenAtlas ID XDH Link Image
Enzyme 1 HGNC ID HGNC:12805 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p23.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T: Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene. 1993 Nov 15;133(2):279-84. [PubMed Link Image]
  2. Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1994 Mar 15;199(2):998-1004. [PubMed Link Image]
  3. Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1995 Oct 4;215(1):429. [PubMed Link Image]
  4. Saksela M, Raivio KO: Cloning and expression in vitro of human xanthine dehydrogenase/oxidase. Biochem J. 1996 Apr 1;315 ( Pt 1):235-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5715
Enzyme 2 Name Hypoxanthine-guanine phosphoribosyltransferase
Enzyme 2 Synonyms
  1. HGPRT
  2. HGPRTase
Enzyme 2 Gene Name HPRT1
Enzyme 2 Protein Sequence >Hypoxanthine-guanine phosphoribosyltransferase 
MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGH
HIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGD
DLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVG
FEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
Enzyme 2 Number of Residues 218
Enzyme 2 Molecular Weight 24580
Enzyme 2 Theoretical pI 6.67
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hypoxanthine phosphoribosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • physiological process
  • purine ribonucleoside salvage
  • purine salvage
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function IMP + diphosphate = hypoxanthine + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 306885 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00492 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HPRT_HUMAN Link Image
Enzyme 2 PDB ID 1BZY Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >657 bp 
ATGGCGACCCGCAGCCCTGGCGTCGTGATTAGTGATGATGAACCAGGTTATGACCTTGAT
TTATTTTGCATACCTAATCATTATGCTGAGGATTTGGAAAGGGTGTTTATTCCTCATGGA
CTAATTATGGACAGGACTGAACGTCTTGCTCGAGATGTGATGAAGGAGATGGGAGGCCAT
CACATTGTAGCCCTCTGTGTGCTCAAGGGGGGCTATAAATTCTTTGCTGACCTGCTGGAT
TACATCAAAGCACTGAATAGAAATAGTGATAGATCCATTCCTATGACTGTAGATTTTATC
AGACTGAAGAGCTATTGTAATGACCAGTCAACAGGGGACATAAAAGTAATTGGTGGAGAT
GATCTCTCAACTTTAACTGGAAAGAATGTCTTGATTGTGGAAGATATAATTGACACTGGC
AAAACAATGCAGACTTTGCTTTCCTTGGTCAGGCAGTATAATCCAAAGATGGTCAAGGTC
GCAAGCTTGCTGGTGAAAAGGACCCCACGAAGTGTTGGATATAAGCCAGACTTTGTTGGA
TTTGAAATTCCAGACAAGTTTGTTGTAGGATATGCCCTTGACTATAATGAATACTTCAGG
GATTTGAATCATGTTTGTGTCATTAGTGAAACTGGAAAAGCAAAATACAAAGCCTAA
Enzyme 2 GenBank Gene ID M31642 Link Image
Enzyme 2 GeneCard ID HPRT1 Link Image
Enzyme 2 GenAtlas ID HPRT1 Link Image
Enzyme 2 HGNC ID HGNC:5157 Link Image
Enzyme 2 Chromosome Location X
Enzyme 2 Locus Xq26.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T: Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):477-81. [PubMed Link Image]
  2. Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W: Automated DNA sequencing of the human HPRT locus. Genomics. 1990 Apr;6(4):593-608. [PubMed Link Image]
  3. Wilson JM, Tarr GE, Mahoney WC, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1982 Sep 25;257(18):10978-85. [PubMed Link Image]
  4. Patel PI, Framson PE, Caskey CT, Chinault AC: Fine structure of the human hypoxanthine phosphoribosyltransferase gene. Mol Cell Biol. 1986 Feb;6(2):393-403. [PubMed Link Image]
  5. Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC: The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 1994 Jul 29;78(2):325-34. [PubMed Link Image]
  6. Shi W, Li CM, Tyler PC, Furneaux RH, Grubmeyer C, Schramm VL, Almo SC: The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat Struct Biol. 1999 Jun;6(6):588-93. [PubMed Link Image]
  7. Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP 3rd: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding. Protein Sci. 1999 May;8(5):1023-31. [PubMed Link Image]
  8. Sculley DG, Dawson PA, Emmerson BT, Gordon RB: A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Hum Genet. 1992 Nov;90(3):195-207. [PubMed Link Image]
  9. Wilson JM, Kobayashi R, Fox IH, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. J Biol Chem. 1983 May 25;258(10):6458-60. [PubMed Link Image]
  10. Wilson JM, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome. J Clin Invest. 1983 May;71(5):1331-5. [PubMed Link Image]
  11. Wilson JM, Tarr GE, Kelley WN: Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout. Proc Natl Acad Sci U S A. 1983 Feb;80(3):870-3. [PubMed Link Image]
  12. Wilson JM, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout. J Biol Chem. 1984 Jan 10;259(1):27-30. [PubMed Link Image]
  13. Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P: Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich. Am J Hum Genet. 1988 May;42(5):726-34. [PubMed Link Image]
  14. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint). Gene. 1988 Mar 31;63(2):331-6. [PubMed Link Image]
  15. Davidson BL, Palella TD, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland). Gene. 1988 Aug 15;68(1):85-91. [PubMed Link Image]
  16. Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN: Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). Hum Genet. 1988 May;79(1):39-43. [PubMed Link Image]
  17. Davidson BL, Chin SJ, Wilson JM, Kelley WN, Palella TD: Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects. J Clin Invest. 1988 Dec;82(6):2164-7. [PubMed Link Image]
  18. Keough DT, Gordon RB, de Jersey J, Emmerson BT: Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families. J Inherit Metab Dis. 1988;11(3):229-38. [PubMed Link Image]
  19. Igarashi T, Minami M, Nishida Y: Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients. Acta Paediatr Jpn. 1989 Jun;31(3):303-13. [PubMed Link Image]
  20. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). J Biol Chem. 1989 Jan 5;264(1):520-5. [PubMed Link Image]
  21. Fujimori S, Davidson BL, Kelley WN, Palella TD: Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. J Clin Invest. 1989 Jan;83(1):11-3. [PubMed Link Image]
  22. Davidson BL, Tarle SA, Palella TD, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. J Clin Invest. 1989 Jul;84(1):342-6. [PubMed Link Image]
  23. Gibbs RA, Nguyen PN, McBride LJ, Koepf SM, Caskey CT: Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1919-23. [PubMed Link Image]
  24. Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT: Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. Genomics. 1990 Jun;7(2):235-44. [PubMed Link Image]
  25. Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ: Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. Hum Genet. 1990 Jun;85(1):111-6. [PubMed Link Image]
  26. Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT: Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). J Inherit Metab Dis. 1990;13(5):692-700. [PubMed Link Image]
  27. Davidson BL, Tarle SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD: Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Am J Hum Genet. 1991 May;48(5):951-8. [PubMed Link Image]
  28. Tarle SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD: Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. Genomics. 1991 Jun;10(2):499-501. [PubMed Link Image]
  29. Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB: Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. Hum Genet. 1991 Oct;87(6):688-92. [PubMed Link Image]
  30. Yamada Y, Goto H, Ogasawara N: Identification of two independent Japanese mutant HPRT genes using the PCR technique. Adv Exp Med Biol. 1991;309B:121-4. [PubMed Link Image]
  31. Lightfoot T, Joshi R, Nuki G, Snyder FF: The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. Hum Genet. 1992 Mar;88(6):695-6. [PubMed Link Image]
  32. Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL: Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. Hum Mol Genet. 1992 Sep;1(6):427-32. [PubMed Link Image]
  33. Burgemeister R, Rotzer E, Gutensohn W, Gehrke M, Schiel W: Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies. Hum Mutat. 1995;5(4):341-4. [PubMed Link Image]
  34. Fujimori S, Sakuma R, Yamaoka N, Hakoda M, Yamanaka H, Kamatani N: An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans. Hum Genet. 1997 Jan;99(1):8-10. [PubMed Link Image]
  35. Liu G, Aral B, Zabot MT, Kamoun P, Ceballos-Picot I: The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations. Hum Mutat. 1998;Suppl 1:S88-90. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5805
Enzyme 3 Name Purine nucleoside phosphorylase
Enzyme 3 Synonyms
  1. Inosine phosphorylase
  2. PNP
Enzyme 3 Gene Name NP
Enzyme 3 Protein Sequence >Purine nucleoside phosphorylase 
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 3 Number of Residues 289
Enzyme 3 Molecular Weight 32118
Enzyme 3 Theoretical pI 6.95
Enzyme 3 GO Classification
Function
  • catalytic activity
  • purine-nucleoside phosphorylase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
—
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 35565 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P00491 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Enzyme 3 PDB ID 1RT9 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >870 bp 
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Enzyme 3 GenBank Gene ID X00737 Link Image
Enzyme 3 GeneCard ID NP Link Image
Enzyme 3 GenAtlas ID NP Link Image
Enzyme 3 HGNC ID HGNC:7892 Link Image
Enzyme 3 Chromosome Location 14
Enzyme 3 Locus 14q13.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed Link Image]
  2. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed Link Image]
  3. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed Link Image]
  4. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed Link Image]
  5. Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed Link Image]
  6. Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5963
Enzyme 4 Name Guanine deaminase
Enzyme 4 Synonyms
  1. Guanase
  2. Guanine aminase
  3. Guanine aminohydrolase
  4. GAH
  5. p51-nedasin
Enzyme 4 Gene Name GDA
Enzyme 4 Protein Sequence >Guanine deaminase 
MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCF
KPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFA
EEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEY
KETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSH
ISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAH
CPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNE
KSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDI
SEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV
Enzyme 4 Number of Residues 454
Enzyme 4 Molecular Weight 51004
Enzyme 4 Theoretical pI 5.45
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia
Enzyme 4 Pathways
Enzyme 4 Reactions
  • guanine + H2O = xanthine + ammonia
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 4588080 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9Y2T3 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GUAD_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1365 bp 
ATGTGTGCCGCTCAGATGCCGCCCCTGGCGCACATCTTCCGAGGGACGTTCGTCCACTCC
ACCTGGACCTGCCCCATGGAGGTGCTGCGGGATCACCTCCTCGGCGTGAGCGACAGCGGC
AAAATAGTGTTTTTAGAAGAAGCATCTCAACAGGAAAAACTGGCCAAAGAATGGTGCTTC
AAGCCGTGTGAAATAAGAGAACTGAGCCACCATGAGTTCTTCATGCCTGGGCTGGTTGAT
ACACACATCCATGCCTCTCAGTATTCCTTTGCTGGAAGTAGCATAGACCTGCCACTCTTG
GAGTGGCTGACCAAGTACACATTTCCTGCAGAACACAGATTCCAGAACATCGACTTTGCA
GAAGAAGTATATACCAGAGTTGTCAGGAGAACACTAAAGAATGGAACAACCACAGCTTGT
TACTTTGCAACAATTCACACTGACTCATCTCTGCTCCTTGCCGACATTACAGATAAATTT
GGACAGCGGGCATTTGTGGGCAAAGTTTGCATGGATTTGAATGACACTTTTCCAGAATAC
AAGGAGACCACTGAGGAATCGATCAAGGAAACTGAGAGATTTGTGTCAGAAATGCTCCAA
AAGAACTATTCTAGAGTGAAGCCCATAGTGACACCACGTTTTTCCCTCTCCTGCTCTGAG
ACTTTGATGGGTGAACTGGGCAACATTGCTAAAACCCGTGATTTGCACATTCAGAGCCAT
ATAAGTGAAAATCGTGATGAAGTTGAAGCTGTGAAAAACTTATACCCCAGTTATAAAAAC
TACACATCTGTGTATGATAAAAACAATCTTTTGACAAATAAGACAGTGATGGCACACGGC
TGCTACCTCTCTGCAGAAGAACTGAACGTATTCCATGAACGAGGAGCATCCATCGCACAC
TGTCCCAATTCTAATTTATCGCTCAGCAGTGGATTTCTAAATGTGCTAGAAGTCCTGAAA
CATGAAGTCAAGATAGGGCTGGGTACAGACGTGGCTGGTGGCTATTCATATTCCATGCTT
GATGCAATCAGAAGAGCAGTGATGGTTTCCAATATCCTTTTAATTAATAAGGTAAATGAG
AAAAGCCTCACCCTCAAAGAAGTCTTCAGACTAGCTACTCTTGGAGGAAGCCAAGCCCTG
GGGCTGGATGGTGAGATTGGAAACTTTGAAGTGGGCAAGGAATTTGATGCCATCCTGATC
AACCCCAAAGCATCCGACTCTCCCATTGACCTGTTTTATGGGGACTTTTTTGGTGATATT
TCTGAGGCTGTTATCCAGAAGTTCCTCTATCTAGGAGATGATCGAAATATTGAAGAGGTT
TATGTGGGCGGAAAGCAGGTGGTTCCGTTTTCCAGCTCAGTGTAA
Enzyme 4 GenBank Gene ID AF095286 Link Image
Enzyme 4 GeneCard ID GDA Link Image
Enzyme 4 GenAtlas ID GDA Link Image
Enzyme 4 HGNC ID HGNC:4212 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q21.13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Yuan G, Bin JC, McKay DJ, Snyder FF: Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein. J Biol Chem. 1999 Mar 19;274(12):8175-80. [PubMed Link Image]
  2. Kuwahara H, Araki N, Makino K, Masuko N, Honda S, Kaibuchi K, Fukunaga K, Miyamoto E, Ogawa M, Saya H: A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between NE-dlg/SAP102 and N-methyl-D-aspartate receptor. J Biol Chem. 1999 Nov 5;274(45):32204-14. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15172
Enzyme 5 Name Guanine deaminase (Guanine deaminase, isoform CRA_b)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name GDA
Enzyme 5 Protein Sequence >Guanine deaminase (Guanine deaminase, isoform CRA_b) 
MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCF
KPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFA
EEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEY
KETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSH
ISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAH
CPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNE
KSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDI
SEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV
Enzyme 5 Number of Residues 454
Enzyme 5 Molecular Weight 51004
Enzyme 5 Theoretical pI 5.45
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 5 General Function Nucleotide transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 55960270 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q5SZC7 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q5SZC7_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1266 bp 
ATGTGTGCCGCTCAGATGCCGCCCCTGGCGCACATCTTCCGAGGGACGTTCGTCCACTCC
ACCTGGACCTGCCCCATGGAGGTGCTGCGGGATCACCTCCTCGGCGTGAGCGACAGCGGC
AAAATAGTGTTTTTAGAAGAAGCATCTCAACAGGAAAAACTGGCCAAAGAATGGTGCTTC
AAGCCGTGTGAAATAAGAGAACTGAGCCACCATGAGTTCTTCATGCCTGGGCTGGTTGAT
ACACACATCCATGCCTCTCAGTATTCCTTTGCTGGAAGTAGCATAGACCTGCCACTCTTG
GAGTGGCTGACCAAGTACACATTTCCTGCAGAACACAGATTCCAGAACATCGACTTTGCA
GAAGAAGTATATACCAGAGTTGTCAGGAGAACACTAAAGAATGGAACAACCACAGCTTGT
TACTTTGCAACAATTCACACTGACTCATCTCTGCTCCTTGCCGACATTACAGATAAATTT
GGACAGCGGGCATTTGTGGGCAAAGTTTGCATGGATTTGAATGACACTTTTCCAGAATAC
AAGGAGACCACTGAGGAATCGATCAAGGAAACTGAGAGATTTGTGTCAGAAATGCTCCAA
AAGAACTATTCTAGAGTGAAGCCCATAGTGACACCACGTTTTTCCCTCTCCTGCTCTGAG
ACTTTGATGGGTGAACTGGGCAACATTGCTAAAACCCGTGATTTGCACATTCAGAGCCAT
ATAAGTGAAAATCGTGATGAAGTTGAAGCTGTGAAAAACTTATACCCCAGTTATAAAAAC
TACACATCTGTGTATGATAAAAACAATCTTTTGACAAATAAGACAGTGATGGCACACGGC
TGCTACCTCTCTGCAGAAGAACTGAACGTATTCCATGAACGAGGAGCATCCATCGCACAC
TGTCCCAATTCTAATTTATCGCTCAGCAGTGGATTTCTAAATGTGCTAGAAGTCCTGAAA
CATGAAGTCAAGATAGGGCTGGGTACAGACGTGGCTGGTGGCTATTCATATTCCATGCTT
GATGCAATCAGAAGAGCAGTGATGGTTTCCAATATCCTTTTAATTAATAAGGTAAATGAG
AAAAGCCTCACCCTCAAAGAAGTCTTCAGACTAGCTACTCTTGGAGGAAGCCAAGCCCTG
GGGCTGGATGGTGAGATTGGAAACTTTGAAGTGGGCAAGGAATTTGATGCCATCCTGATC
AACCCCAAAGCATCCGACTCTCCCATTGACCTGTTTTATGGGGACTTTTTTGGTGATATT
TCTGAG
Enzyme 5 GenBank Gene ID AL590311 Link Image
Enzyme 5 GeneCard ID Q5SZC7 Link Image
Enzyme 5 GenAtlas ID GDA Link Image
Enzyme 5 HGNC ID HGNC:4212 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available