| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-08-07 12:12:47 |
| Accession Number |
HMDB00071 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Deoxyinosine |
| Description |
Deoxyinosine is a nucleoside that is formed when hypoxanthine is attached to a deoxyribose ring (also known as a ribofuranose) via a beta-N9-glycosidic bond. Deoxyinosine is found in DNA while Inosine is found in RNA. Inosine is a nucleic acid important for RNA editing. Adenosine deaminase (ADA) catalyzes the conversion of adenosine and deoxyadenosine to inosine and deoxyinosine, respectively. ADA-deficient individuals suffer from severe combined immunodeficiency (SCID) and are unable to produce significant numbers of mature T or B lymphocytes. This occurs as a consequence of the accumulation of ADA substrates or their metabolites. Inosine is also an intermediate in a chain of purine nucleotides reactions required for muscle movements. |
| Synonyms |
- 2'-Deoxyinosine
- 2deoxy-Inosine
- 9-(2-Deoxy-b-D-erythro-pentofuranosyl)-1,9-dihydro-6H-purin-6-one
- 9-(2-deoxy-b-D-erythro-pentofuranosyl)-Hypoxanthine
- 9-(2-deoxy-beta-D-erythro-pentofuranosyl)-Hypoxanthine
- Deoxyinosine
- d-Ino
- 9-(2-Deoxy-beta-delta-erythro-pentofuranosyl)-1,9-dihydro-6H-purin-6-one
- 9-(2-deoxy-beta-delta-erythro-pentofuranosyl)-Hypoxanthine
- delta-Ino
|
| Chemical IUPAC Name |
9-[4-hydroxy-5-(hydroxymethyl)oxolan-2-yl]-3H-purin-6-one |
| Chemical Formula |
C10H12N4O4 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Nucleosides and Nucleoside conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- primary alcohol
- secondary alcohol
- phenol or hydroxyhetarene
- aromatic compound
- heterocyclic compound
|
| Biofunction |
| — |
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
252.227 |
| Monoisotopic Molecular Weight |
252.085861 |
| Isomeric SMILES |
OC[C@H]1O[C@H](C[C@@H]1O)N1C=NC2=C1N=CN=C2O |
| Canonical SMILES |
OCC1OC(CC1O)N1C=NC2=C1N=CN=C2O |
| KEGG Compound ID |
C05512  |
| BioCyc ID |
DEOXYINOSINE  |
| BiGG ID |
45942  |
| Wikipedia Link |
Not Available |
| NuGOwiki Link |
HMDB00071  |
| Metagene Link |
HMDB00071  |
| METLIN ID |
3383  |
| PubChem Compound |
65058  |
| PubChem Substance |
3139569  |
| ChEBI ID |
Not Available |
| CAS Registry Number |
890-38-0 |
| InChI Identifier |
InChI=1/C10H12N4O4/c15-2-6-5(16)1-7(18-6)14-4-13-8-9(14)11-3-12-10(8)17/h3-7,15-16H,1-2H2,(H,11,12,17)/t5-,6+,7+/m0/s1 |
| Synthesis Reference |
Robins, Morris J.; Basom, Gerald L. Nucleic acid-related compounds. 8. Direct conversion of 2'-deoxyinosine to 9-(2-deoxy-b-D-erythro-pentofuranosyl)-6-chloropurine and selected 6-substituted deoxynucleosides and their evaluation as substrates of adenosin |
| Melting Point (Experimental) |
250 oC |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
32.5 mg/mL [MEYLAN,WM et al. (1996)]; 18.7 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
0 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
-1.71 [FORD,H ET AL. (1991)]
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-1.62 [Predicted by ALOGPS]; -0.8 [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 |
1Z39  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Varian) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm
- nucleus
- Extracellular
|
| Biofluid Location |
|
| Tissue Location |
| Tissue |
References |
| All Tissues |
— |
|
| Concentrations (Normal) |
| Biofluid |
Urine |
| Value |
< 0.1 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. [PubMed
]
|
| Biofluid |
Urine |
| Value |
1.00 (0.00-2.00) umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Hartmann S, Okun JG, Schmidt C, Langhans CD, Garbade SF, Burgard P, Haas D, Sass JO, Nyhan WL, Hoffmann GF: Comprehensive detection of disorders of purine and pyrimidine metabolism by HPLC with electrospray ionization tandem mass spectrometry. Clin Chem. 2006 Jun;52(6):1127-37. Epub 2006 Apr 13. [PubMed
]
|
|
| Concentrations (Abnormal) |
| Biofluid |
Urine |
| Value |
3.2 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Purine nucleoside phosphorylase deficiency |
| Comments |
Not Available |
| References |
- Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Purine nucleoside phosphorylase deficiency |
- Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. [PubMed
]
|
|
| OMIM ID |
- 164050
(Purine nucleoside phosphorylase deficiency)
|
| Pathways |
|
| General References |
- Cohen A, Doyle D, Martin DW Jr, Ammann AJ: Abnormal purine metabolism and purine overproduction in a patient deficient in purine nucleoside phosphorylase. N Engl J Med. 1976 Dec 23;295(26):1449-54. [PubMed
]
- Kewn S, Hoggard PG, Henry-Mowatt JS, Veal GJ, Sales SD, Barry MG, Back DJ: Intracellular activation of 2',3'-dideoxyinosine and drug interactions in vitro. AIDS Res Hum Retroviruses. 1999 Jun 10;15(9):793-802. [PubMed
]
- Bemi V, Tazzni N, Banditelli S, Giorgelli F, Pesi R, Turchi G, Mattana A, Sgarrella F, Tozzi MG, Camici M: Deoxyadenosine metabolism in a human colon-carcinoma cell line (LoVo) in relation to its cytotoxic effect in combination with deoxycoformycin. Int J Cancer. 1998 Mar 2;75(5):713-20. [PubMed
]
- Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. [PubMed
]
- Ablett E, Pedley J, Dannoy PA, Sturm RA, Parsons PG: UVB-specific regulation of gene expression in human melanocytic cells: cell cycle effects and implication in the generation of melanoma. Mutat Res. 1998 Nov 9;422(1):31-41. [PubMed
]
- Bazar LS, Collier GB, Vanek PG, Siles BA, Kow YW, Doetsch PW, Cunningham RP, Chirikjian JG: Mutation identification DNA analysis system (MIDAS) for detection of known mutations. Electrophoresis. 1999 Jun;20(6):1141-8. [PubMed
]
- Sjoberg AH, Wang L, Eriksson S: Substrate specificity of human recombinant mitochondrial deoxyguanosine kinase with cytostatic and antiviral purine and pyrimidine analogs. Mol Pharmacol. 1998 Feb;53(2):270-3. [PubMed
]
|
| Metabolic Enzymes |
- Purine nucleoside phosphorylase
- Thymidine phosphorylase precursor
- Adenosine deaminase
- cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5805 |
| Enzyme 1 Name |
Purine nucleoside phosphorylase |
| Enzyme 1 Synonyms |
- Inosine phosphorylase
- PNP
|
| Enzyme 1 Gene Name |
NP |
| Enzyme 1 Protein Sequence |
>Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
|
| Enzyme 1 Number of Residues |
289 |
| Enzyme 1 Molecular Weight |
32118 |
| Enzyme 1 Theoretical pI |
6.95 |
| Enzyme 1 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 1 General Function |
Nucleotide transport and metabolism |
| Enzyme 1 Specific Function |
Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
35565  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P00491  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PNPH_HUMAN  |
| Enzyme 1 PDB ID |
1RT9  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
|
| Enzyme 1 GenBank Gene ID |
X00737  |
| Enzyme 1 GeneCard ID |
NP  |
| Enzyme 1 GenAtlas ID |
NP  |
| Enzyme 1 HGNC ID |
HGNC:7892  |
| Enzyme 1 Chromosome Location |
14 |
| Enzyme 1 Locus |
14q13.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5806 |
| Enzyme 2 Name |
Thymidine phosphorylase precursor |
| Enzyme 2 Synonyms |
- TdRPase
- TP
- Platelet-derived endothelial cell growth factor
- PD-ECGF
- Gliostatin
|
| Enzyme 2 Gene Name |
ECGF1 |
| Enzyme 2 Protein Sequence |
>Thymidine phosphorylase precursor
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA
VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG
VGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA
GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA
VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP
DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL
CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG
AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP
QQ
|
| Enzyme 2 Number of Residues |
482 |
| Enzyme 2 Molecular Weight |
49956 |
| Enzyme 2 Theoretical pI |
5.19 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- pyrimidine base metabolism
|
| Component |
| — |
|
| Enzyme 2 General Function |
Nucleotide transport and metabolism |
| Enzyme 2 Specific Function |
Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
189701  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P19971  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
TYPH_HUMAN  |
| Enzyme 2 PDB ID |
1UOU  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1449 bp
ATGGCAGCCTTGATGACCCCGGGAACCGGGGCCCCACCCGCGCCTGGTGACTTCTCCGGG
GAAGGGAGCCAGGGACTTCCCGACCCTTCGCCAGAGCCCAAGCAGCTCCCGGAGCTGATC
CGCATGAAGCGAGACGGAGGCCGCCTGAGCGAAGCGGACATCAGGGGCTTCGTGGCCGCT
GTGGTGAATGGGAGCGCGCAGGGCGCACAGATCGGGGCCATGCTGATGGCCATCCGACTT
CGGGGCATGGATCTGGAGGAGACCTCGGTGCTGACCCAGGCCCTGGCTCAGTCGGGACAG
CAGCTGGAGTGGCCAGAGGCCTGGCGCCAGCAGCTTGTGGACAAGCATTCCACAGGGGGT
GTGGGTGACAAGGTCAGCCTGGTCCTCGCACCTGCCCTGGCGGCATGTGGCTGCAAGGTG
CCAATGATCAGCGGACGTGGTCTGGGGCACACAGGAGGCACCTTGGATAAGCTGGAGTCT
ATTCCTGGATTCAATGTCATCCAGAGCCCAGAGCAGATGCAAGTGCTGCTGGACCAGGCG
GGCTGCTGTATCGTGGGTCAGAGTGAGCAGCTGGTTCCTGCGGACGGAATCCTATATGCA
GCCAGAGATGTGACAGCCACCGTGGACAGCCTGCCACTCATCACAGCCTCCATTCTCAGT
AAGAAACTCGTGGAGGGGCTGTCCGCTCTGGTGGTGGACGTTAAGTTCGGAGGGGCCGCC
GTCTTCCCCAACCAGGAGCAGGCCCGGGAGCTGGCAAAGACGCTGGTTGGCGTGGGAGCC
AGCCTAGGGCTTCGGGTCGCGGCAGCGCTGACCGCCATGGACAAGCCCCTGGGTCGCTGC
GTGGGCCACGCCCTGGAGGTGGAGGAGGCGCTGCTCTGCATGGACGGCGCAGGCCCGCCA
GACTTAAGGGACCTGGTCACCACGCTCGGGGGCGCCCTGCTCTGGCTCAGCGGACACGCG
GGGACTCAGGCTCAGGGCGCTGCCCGGGTGGCCGCGGCGCTGGACGACGGCTCGGCCCTT
GGCCGCTTCGAGCGGATGCTGGCGGCGCAGGGCGTGGATCCCGGTCTGGCCCGAGCCCTG
TGCTCGGGAAGTCCCGCAGAACGCCGGCAGCTGCTGCCTCGCGCCCGGGAGCAGGAGGAG
CTGCTGGCGCCCGCAGATGGCACCGTGGAGCTGGTCCGGGCGCTGCCGCTGGCGCTGGTG
CTGCACGAGCTCGGGGCCGGGCGCAGCCGCGCTGGGGAGCCGCTCCGCCTGGGGGTGGGC
GCAGAGCTGCTGGTCGACGTGGGTCAGAGGCTGCGCCGTGGGACCCCCTGGCTCCGCGTG
CACCGGGACGGCCCCGCGCTCAGCGGCCCGCAGAGCCGCGCCCTGCAGGAGGCGCTCGTA
CTCTCCGACCGCGCGCCATTCGCCGCCCCCTCGCCCTTCGCAGAGCTCGTTCTGCCGCCG
CAGCAATAA
|
| Enzyme 2 GenBank Gene ID |
M63193  |
| Enzyme 2 GeneCard ID |
ECGF1  |
| Enzyme 2 GenAtlas ID |
ECGF1  |
| Enzyme 2 HGNC ID |
HGNC:3148  |
| Enzyme 2 Chromosome Location |
22 |
| Enzyme 2 Locus |
22q13|22q13.33 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Ishikawa F, Miyazono K, Hellman U, Drexler H, Wernstedt C, Hagiwara K, Usuki K, Takaku F, Risau W, Heldin CH: Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor. Nature. 1989 Apr 13;338(6216):557-62. [PubMed
]
- Furukawa T, Yoshimura A, Sumizawa T, Haraguchi M, Akiyama S, Fukui K, Ishizawa M, Yamada Y: Angiogenic factor. Nature. 1992 Apr 23;356(6371):668. [PubMed
]
- Asai K, Nakanishi K, Isobe I, Eksioglu YZ, Hirano A, Hama K, Miyamoto T, Kato T: Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor. J Biol Chem. 1992 Oct 5;267(28):20311-6. [PubMed
]
- Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH: Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity. Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. [PubMed
]
- Nishino I, Spinazzola A, Hirano M: Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. Science. 1999 Jan 29;283(5402):689-92. [PubMed
]
- Gamez J, Ferreiro C, Accarino ML, Guarner L, Tadesse S, Marti RA, Andreu AL, Raguer N, Cervera C, Hirano M: Phenotypic variability in a Spanish family with MNGIE. Neurology. 2002 Aug 13;59(3):455-7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5937 |
| Enzyme 3 Name |
Adenosine deaminase |
| Enzyme 3 Synonyms |
- Adenosine aminohydrolase
|
| Enzyme 3 Gene Name |
ADA |
| Enzyme 3 Protein Sequence |
>Adenosine deaminase
MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPD
FLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQA
EGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAI
DLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGY
HTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIF
KSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAG
QNL
|
| Enzyme 3 Number of Residues |
363 |
| Enzyme 3 Molecular Weight |
40765 |
| Enzyme 3 Theoretical pI |
5.80 |
| Enzyme 3 GO Classification |
| Function |
- adenosine deaminase activity
- catalytic activity
- deaminase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- purine nucleoside monophosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside monophosphate biosynthesis
|
| Component |
| — |
|
| Enzyme 3 General Function |
Replication, recombination and repair |
| Enzyme 3 Specific Function |
Adenosine + H(2)O = inosine + NH(3) |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- adenosine + H2O = inosine + ammonia
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
28380  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P00813  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ADA_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1092 bp
ATGGCCCAGACGCCCGCCTTCGACAAGCCCAAAGTAGAACTGCATGTCCACCTAGACGGA
TCCATCAAGCCTGAAACCATCTTATACTATGGCAGGAGGAGAGGGATCGCCCTCCCAGCT
AACACAGCAGAGGGGCTGCTGAACGTCATTGGCATGGACAAGCCGCTCACCCTTCCAGAC
TTCCTGGCCAAGTTTGACTACTACATGCCTGCTATCGCGGGCTGCCGGGAGGCTATCAAA
AGGATCGCCTATGAGTTTGTAGAGATGAAGGCCAAAGAGGGCGTGGTGTATGTGGAGGTG
CGGTACAGTCCGCACCTGCTGGCCAACTCCAAAGTGGAGCCAATCCCCTGGAACCAGGCT
GAAGGGGACCTCACCCCAGACGAGGTGGTGGCCCTAGTGGGCCAGGGCCTGCAGGAGGGG
GAGCGAGACTTCGGGGTCAAGGCCCGGTCCATCCTGTGCTGCATGCGCCACCAGCCCAAC
TGGTCCCCCAAGGTGGTGGAGCTGTGTAAGAAGTACCAGCAGCAGACCGTGGTGGCCATT
GACCTGGCTGGAGATGAGACCATCCCAGGAAGCAGCCTCTTGCCTGGACATGTCCAGGCC
TACCAGGAGGCTGTGAAGAGCGGCATTCACCGTACTGTCCACGCCGGGGAGGTGGGCTCG
GCCGAAGTAGTAAAAGAGGCTGTGGACATACTCAAGACAGAGCGGCTGGGACACGGCTAC
CACACCCTGGAAGACCAGGCCCTTTATAACAGGCTGCGGCAGGAAAACATGCACTTCGAG
ATCTGCCCCTGGTCCAGCTACCTCACTGGTGCCTGGAAGCCGGACACGGAGCATGCAGTC
ATTCGGCTCAAAAATGACCAGGCTAACTACTCGCTCAACACAGATGACCCGCTCATCTTC
AAGTCCACCCTGGACACTGATTACCAGATGACCAAACGGGACATGGGCTTTACTGAAGAG
GAGTTTAAAAGGCTGAACATCAATGCGGCCAAATCTAGTTTCCTCCCAGAAGATGAAAAG
AGGGAGCTTCTCGACCTGCTCTATAAAGCCTATGGGATGCCACCTTCAGCCTCTGCAGGG
CAGAACCTCTGA
|
| Enzyme 3 GenBank Gene ID |
X02994  |
| Enzyme 3 GeneCard ID |
ADA  |
| Enzyme 3 GenAtlas ID |
ADA  |
| Enzyme 3 HGNC ID |
HGNC:186  |
| Enzyme 3 Chromosome Location |
20 |
| Enzyme 3 Locus |
20q12-q13.11 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Daddona PE, Shewach DS, Kelley WN, Argos P, Markham AF, Orkin SH: Human adenosine deaminase. cDNA and complete primary amino acid sequence. J Biol Chem. 1984 Oct 10;259(19):12101-6. [PubMed
]
- Wiginton DA, Adrian GS, Hutton JJ: Sequence of human adenosine deaminase cDNA including the coding region and a small intron. Nucleic Acids Res. 1984 Mar 12;12(5):2439-46. [PubMed
]
- Valerio D, Duyvesteyn MG, Dekker BM, Weeda G, Berkvens TM, van der Voorn L, van Ormondt H, van der Eb AJ: Adenosine deaminase: characterization and expression of a gene with a remarkable promoter. EMBO J. 1985 Feb;4(2):437-43. [PubMed
]
- Wiginton DA, Kaplan DJ, States JC, Akeson AL, Perme CM, Bilyk IJ, Vaughn AJ, Lattier DL, Hutton JJ: Complete sequence and structure of the gene for human adenosine deaminase. Biochemistry. 1986 Dec 16;25(25):8234-44. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Orkin SH, Daddona PE, Shewach DS, Markham AF, Bruns GA, Goff SC, Kelley WN: Molecular cloning of human adenosine deaminase gene sequences. J Biol Chem. 1983 Nov 10;258(21):12753-6. [PubMed
]
- Hirschhorn R, Yang DR, Israni A: An Asp8Asn substitution results in the adenosine deaminase (ADA) genetic polymorphism (ADA 2 allozyme): occurrence on different chromosomal backgrounds and apparent intragenic crossover. Ann Hum Genet. 1994 Jan;58(Pt 1):1-9. [PubMed
]
- Adrian GS, Wiginton DA, Hutton JJ: Structure of adenosine deaminase mRNAs from normal and adenosine deaminase-deficient human cell lines. Mol Cell Biol. 1984 Sep;4(9):1712-7. [PubMed
]
- Bonthron DT, Markham AF, Ginsburg D, Orkin SH: Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency. J Clin Invest. 1985 Aug;76(2):894-7. [PubMed
]
- Akeson AL, Wiginton DA, Dusing MR, States JC, Hutton JJ: Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts. J Biol Chem. 1988 Nov 5;263(31):16291-6. [PubMed
]
- Hirschhorn R, Tzall S, Ellenbogen A, Orkin SH: Identification of a point mutation resulting in a heat-labile adenosine deaminase (ADA) in two unrelated children with partial ADA deficiency. J Clin Invest. 1989 Feb;83(2):497-501. [PubMed
]
- Hirschhorn R: Identification of two new missense mutations (R156C and S291L) in two ADA- SCID patients unusual for response to therapy with partial exchange transfusions. Hum Mutat. 1992;1(2):166-8. [PubMed
]
- Santisteban I, Arredondo-Vega FX, Kelly S, Mary A, Fischer A, Hummell DS, Lawton A, Sorensen RU, Stiehm ER, Uribe L, et al.: Novel splicing, missense, and deletion mutations in seven adenosine deaminase-deficient patients with late/delayed onset of combined immunodeficiency disease. Contribution of genotype to phenotype. J Clin Invest. 1993 Nov;92(5):2291-302. [PubMed
]
- Yang DR, Huie ML, Hirschhorn R: Homozygosity for a missense mutation (G20R) associated with neonatal onset adenosine deaminase-deficient severe combined immunodeficiency (ADA-SCID). Clin Immunol Immunopathol. 1994 Feb;70(2):171-5. [PubMed
]
- Santisteban I, Arredondo-Vega FX, Kelly S, Loubser M, Meydan N, Roifman C, Howell PL, Bowen T, Weinberg KI, Schroeder ML, et al.: Three new adenosine deaminase mutations that define a splicing enhancer and cause severe and partial phenotypes: implications for evolution of a CpG hotspot and expression of a transduced ADA cDNA. Hum Mol Genet. 1995 Nov;4(11):2081-7. [PubMed
]
- Santisteban I, Arredondo-Vega FX, Kelly S, Debre M, Fischer A, Perignon JL, Hilman B, elDahr J, Dreyfus DH, Gelfand EW, et al.: Four new adenosine deaminase mutations, altering a zinc-binding histidine, two conserved alanines, and a 5' splice site. Hum Mutat. 1995;5(3):243-50. [PubMed
]
- Hirschhorn R, Borkowsky W, Jiang CK, Yang DR, Jenkins T: Two newly identified mutations (Thr233Ile and Leu152Met) in partially adenosine deaminase-deficient (ADA-) individuals that result in differing biochemical and metabolic phenotypes. Hum Genet. 1997 Jul;100(1):22-9. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
16421 |
| Enzyme 4 Name |
cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
Not Available |
| Enzyme 4 Protein Sequence |
>cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA
VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG
VGDKVSLVLAPALAACGCKVPVISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA
GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA
VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP
DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL
CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG
AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP
QQ
|
| Enzyme 4 Number of Residues |
482 |
| Enzyme 4 Molecular Weight |
49924 |
| Enzyme 4 Theoretical pI |
5.19 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- pyrimidine base metabolism
|
| Component |
| — |
|
| Enzyme 4 General Function |
Nucleotide transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
B2RBL3  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
B2RBL3_HUMAN  |
| Enzyme 4 PDB ID |
1UOU  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK314716  |
| Enzyme 4 GeneCard ID |
B2RBL3  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
Not Available |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |