Pathway Map Details

ATP/ITP metabolism



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AK3, POLR2J, PPA5, POLR3B, POLR2B, ITPA, RPB10, PM/SCL-75, RRP40, 3.1.3.2, 3.1.13.-, 3.1.3.5, 3.6.1.5, Adenosine kinase, Adenine, ENP1, RPA16, AMP, NDPK C, 2.4.2.1, POLR1A, 2.7.4.6, PPAP, 2.7.4.3, KAD6, RRP41, 3.6.1.5, AK2, 3.5.4.6, ADAR3, RPOM, NDPK 8, exosome multienzyme ribonuclease complex, RPA39, ADAR1, APRT, PPA5, NDPK D (mitochondrial), ITP, ADP, RRP42, AK1, 2.4.2.7, POLR2I, 5'-NTC, POLR2G, 6.3.4.4, 4.3.2.2, NDPK B, RRM1, ALPP, dADP, ENTPD6, 1.17.4.1, PNPH, POLR1B, 5'-NT1B, 2.7.1.20, RRP43, Small RR subunit, RPB5, PPAL, POLR2A, 1.17.4.1, PPA5, RNA polymerase I, RPB8, AMD3, NDPK A, 3.1.3.5, ATP, RNA polymerase II, 3.1.3.2, Adenylo-succinate , Hypoxanthine, AMP deaminase, HPRT, Inosine, AMP deaminase 2, Adenosine, 3.6.1.3, AK5, RNA polymerase III, POLR3F, NDPK complex, ADAR2, POLR2D, dIDP, AMP deaminase 1, 5'-NT1A, ENP1, IDP, phosphoribosyl- diphosphate, RPB7.0, IMP, POLR3A, 3.5.4.4, 5'-NTD, 3.1.3.2, KGUA, Ribonucleotide reductase, RPB6, 2.7.4.8, PM/SCL-100, RNA, ADSL, 2.4.2.1, 3.6.1.19, KAD7, ADA, CSL4, POLR3K, ADSS, ENP3, RRP4, 2.7.4.6, NDPK 7, RRM2B, RRM2, 2.4.2.8, ENP3, EPHX2, 2.7.7.6, ENTPD2-alpha, RRP46, ADSSL1, ACYP2, PR44, ACYP1, NDPK 6

Description:

ATP/ITP metabolism

ATP plays the important role in a metabolism. This compound is a universal energy source for all biochemical processes occurring in live systems. Knowledge of Inosine metabolism has led to advances in immunotherapy in recent decades.

ATP is often used as a phosphate source, e.g., in the reaction with Neopterin diphosphate ( NDP ) that results in formation of ADP and Neopterin-3'-triphosphate ( NTP ), as well as in the reaction with Inosine diphosphate ( IDP ) in which Inosine triphosphate ( ITP ) is formed. These reactions are catalyzed by similar enzymes, Nucleoside diphosphate kinase ( NDPK complex) [1], [2], [3], [4], [5], Non-metastatic cells 4, protein expressed in ( NDPK D (mitochondrial) ) [6], [7], [8], Non-metastatic cells 3, protein expressed in ( NDPK C ) [9], [10], [7], Nucleoside non-metastatic cells 6, protein expressed in (nucleoside-diphosphate kinase) ( NDPK 6 ) [11], [8], Non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) ( NDPK 7 ) [8] and non-metastatic cells 2, protein (NM23B) expressed in, pseudogene 1 ( NDPK 8 ) [12].

Hydrolysis of ATP to ADP proceeds in two ways and catalyzed by specific groups of enzymes. The first group consists of Ectonucleoside triphosphate diphosphohydrolase 2 ( ENTPD2-alpha ) [13], [14], Ectonucleoside triphosphate diphosphohydrolase 1 ( ENP1 ) [15], [16], [17], [18], Ectonucleoside triphosphate diphosphohydrolase 3 ( ENP3 ) [19], [20], [21], Acylphosphatase 1, erythrocyte (common) type ( ACYP1 ) [22], [23], Acylphosphatase 2, muscle type ( ACYP2 ) [22], [23], Acid phosphatase 5, tartrate resistant ( PPA5 ) [24], [25], Epoxide hydrolase 2, cytoplasmic ( EPHX2 ) [26], and Alkaline phosphatase, placental (Regan isozyme) ( ALPP ) [26]. The second group consists of Acid phosphatase 2, lysosomal ( PPAL ) [27], [28], [29], Acid phosphatase 5, tartrate resistant ( PPA5 ) [30], [31], [32], [33], and Acid phosphatase, prostate ( PPAP ) [34], [35], [36], [37]. Second group also catalyzes further hydrolysis of ADP to AMP and AMP to release Adenosine.

There are two processes that lead to ITP hydrolysis. The first is a reaction catalyzed by Ectonucleoside triphosphate diphosphohydrolase 1 ( ENP1 ) [15], [19], [18], Ectonucleoside triphosphate diphosphohydrolase 3 ( ENP3 ) [19], [20], [21], and Ectonucleoside triphosphate diphosphohydrolase 6 (putative function) ( ENTPD6 ) [38], [39]. It results in formation of IDP. These enzymes also participate in the following hydrolysis of IDP to Inosine monophosphate ( IMP). And in the second case ITP is hydrolyzed directly to IMP by the action Inosine triphosphatase (nucleoside triphosphate pyrophosphatase) ( ITPA ) [40], [41], [42], [43].

Yet another process leading to formation of ADP is the reaction of ATP with AMP catalyzed by Adenylate kinase 5 ( AK5 ) [44], Adenylate kinase 1 ( AK1 ) [45], [44], Adenylate kinase 2 ( AK2 ) [45], [44], Adenylate kinase 3-like 1 ( AK3 ) [46], [44], TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa ( KAD6 ) [47], [48], and Adenylate kinase 7 ( KAD7 ) [49], [50].

ADP can participate in reaction of formation of 2 '-deoxy-ADP ( dADP ). This reaction is catalyzed by Ribonucleotide reductase. This enzyme is involved in one more reaction of formation of 2 '-deoxy-IDP ( dIDP ) from IDP [51], [52], [53], [54], [55]. dADP and dIDP take part in the dATP/dITP metabolism.

AMP can be hydrolyzed to IMP via two pathways. The first is a direct hydrolysis catalyzed by AMP deaminase [56], [57], Adenosine monophosphate deaminase 2 (isoform L) AMP deaminase 2 [58], [59], [60], Adenosine monophosphate deaminase 1 (isoform M) AMP deaminase 1 [61], [62], [63], [64], and Adenosine monophosphate deaminase (isoform E) ( AMD3 ) [65], [66], [67], [68]. The second is represented by a chain of consecutive reactions: formation of Adenylo-succinate catalyzed by Adenylosuccinate lyase ( ADSL ) [69], [70], [71], [72], [73] followed by formation of IMP in the presence of Adenylosuccinate synthase ( ADSS ) [74], [75], [76], [77] and Adenylosuccinate synthase like 1 ( ADSSL1 ) [74], [75], [76], [77], [78]. IMP also takes part in IMP biosynthesis and GTP-XTP metabolism.

AMP can directly form Adenine, this reaction occurs in the presence of Adenine phosphoribosyltransferase ( APRT ) [79], [80], [81]. Similar reaction proceeds for IMP from Hypoxanthine under the action of Hypoxanthine phosphoribosyltransferase 1 ( HPRT ) [82], [83], [84], [85], [86]. Adenine and Hypoxanthine participate in other processes, e.g., dATP/dITP metabolism and in GTP-XTP metabolism.

Nucleoside phosphorylase ( PNPH ) catalyzes the formation of Adenine from Adenosine [87], [88], [89] and Inosine from Hypoxanthine [90], [91], [92], [87], [88], [89]. Inosine can also be produced as a result of hydrolysis of Adenosine by Adenosine deaminase ( ADA ) [93], [94], [95], Adenosine deaminase, RNA-specific ( ADAR1 ) [96], Adenosine deaminase, RNA-specific, B1 (RED1 homolog rat) ( ADAR2 ) [96] Adenosine deaminase, RNA-specific, B2 (RED2 homolog rat) ( ADAR3 ) [96].

References:

  1. Gilles AM, Presecan E, Vonica A, Lascu I
    Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. The Journal of biological chemistry 1991 May 15;266(14):8784-9
  2. Guignard F, Markert M
    The nucleoside diphosphate kinase of human neutrophils. The Biochemical journal 1996 May 15;316 ( Pt 1):233-8
  3. Freije JM, Blay P, MacDonald NJ, Manrow RE, Steeg PS
    Site-directed mutation of Nm23-H1. Mutations lacking motility suppressive capacity upon transfection are deficient in histidine-dependent protein phosphotransferase pathways in vitro. The Journal of biological chemistry 1997 Feb 28;272(9):5525-32
  4. Bosnar MH, De Gunzburg J, Bago R, Brecevic L, Weber I, Pavelic J
    Subcellular localization of A and B Nm23/NDPK subunits. Experimental cell research 2004 Aug 1;298(1):275-84
  5. Arnaud-Dabernat S, Masse K, Smani M, Peuchant E, Landry M, Bourbon PM, Le Floch R, Daniel JY, Larou M
    Nm23-M2/NDP kinase B induces endogenous c-myc and nm23-M1/NDP kinase A overexpression in BAF3 cells. Both NDP kinases protect the cells from oxidative stress-induced death. Experimental cell research 2004 Dec 10;301(2):293-304
  6. Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML
    nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Human genetics 1997 Apr;99(4):550-7
  7. Masse K, Dabernat S, Bourbon PM, Larou M, Amrein L, Barraud P, Perel Y, Camara M, Landry M, Lacombe ML, Daniel JY
    Characterization of the nm23-M2, nm23-M3 and nm23-M4 mouse genes: comparison with their human orthologs. Gene 2002 Aug 21;296(1-2):87-97
  8. Seifert M, Welter C, Mehraein Y, Seitz G
    Expression of the nm23 homologues nm23-H4, nm23-H6, and nm23-H7 in human gastric and colon cancer. The Journal of pathology 2005 Apr;205(5):623-32
  9. Martinez R, Venturelli D, Perrotti D, Veronese ML, Kastury K, Druck T, Huebner K, Calabretta B
    Gene structure, promoter activity, and chromosomal location of the DR-nm23 gene, a related member of the nm23 gene family. Cancer research 1997 Mar 15;57(6):1180-7
  10. Negroni A, Venturelli D, Tanno B, Amendola R, Ransac S, Cesi V, Calabretta B, Raschella G
    Neuroblastoma specific effects of DR-nm23 and its mutant forms on differentiation and apoptosis. Cell death and differentiation 2000 Sep;7(9):843-50
  11. Mehus JG, Deloukas P, Lambeth DO
    NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Human genetics 1999 Jun;104(6):454-9
  12. Heidbuchel H, Callewaert G, Vereecke J, Carmeliet E
    Membrane-bound nucleoside diphosphate kinase activity in atrial cells of frog, guinea pig, and human. Circulation research 1992 Oct;71(4):808-20
  13. Chadwick BP, Frischauf AM
    Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes. Mammalian genome : official journal of the International Mammalian Genome Society 1997 Sep;8(9):668-72
  14. Mateo J, Harden TK, Boyer JL
    Functional expression of a cDNA encoding a human ecto-ATPase. British journal of pharmacology 1999 Sep;128(2):396-402
  15. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O
    Purification and properties of human placental ATP diphosphohydrolase. European journal of biochemistry / FEBS 1995 Nov 15;234(1):66-74
  16. Wang TF, Guidotti G
    CD39 is an ecto-(Ca2+,Mg2+)-apyrase. The Journal of biological chemistry 1996 Apr 26;271(17):9898-901
  17. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC
    Identification and characterization of CD39/vascular ATP diphosphohydrolase. The Journal of biological chemistry 1996 Dec 20;271(51):33116-22
  18. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y
    Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. International journal of hematology 1998 Oct;68(3):297-310
  19. Smith TM, Kirley TL
    Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochimica et biophysica acta 1998 Jul 28;1386(1):65-78
  20. Smith TM, Lewis Carl SA, Kirley TL
    Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry 1999 May 4;38(18):5849-57
  21. Yang F, Hicks-Berger CA, Smith TM, Kirley TL
    Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry 2001 Apr 3;40(13):3943-50
  22. Chiarugi P, Raugei G, Fiaschi T, Taddei L, Camici G, Ramponi G
    Characterization of a novel nucleolytic activity of acylphosphatases. Biochemistry and molecular biology international 1996 Sep;40(1):73-81
  23. Paoli P, Camici G, Manao G, Giannoni E, Ramponi G
    Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities. The Biochemical journal 2000 Jul 1;349(Pt 1):43-9
  24. Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ
    Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. The Biochemical journal 1989 Jul 15;261(2):601-9
  25. Ketcham CM, Baumbach GA, Bazer FW, Roberts RM
    The type 5, acid phosphatase from spleen of humans with hairy cell leukemia. Purification, properties, immunological characterization, and comparison with porcine uteroferrin. The Journal of biological chemistry 1985 May 10;260(9):5768-76
  26. Newman JW, Morisseau C, Harris TR, Hammock BD
    The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proceedings of the National Academy of Sciences of the United States of America 2003 Feb 18;100(4):1558-63
  27. Geier C, von Figura K, Pohlmann R
    Structure of the human lysosomal acid phosphatase gene. European journal of biochemistry / FEBS 1989 Aug 15;183(3):611-6
  28. Pohlmann R, Krentler C, Schmidt B, Schroder W, Lorkowski G, Culley J, Mersmann G, Geier C, Waheed A, Gottschalk S
    Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. The EMBO journal 1988 Aug;7(8):2343-50
  29. Saftig P, Hartmann D, Lullmann-Rauch R, Wolff J, Evers M, Koster A, Hetman M, von Figura K, Peters C
    Mice deficient in lysosomal acid phosphatase develop lysosomal storage in the kidney and central nervous system. The Journal of biological chemistry 1997 Jul 25;272(30):18628-35
  30. Ketcham CM, Roberts RM, Simmen RC, Nick HS
    Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. The Journal of biological chemistry 1989 Jan 5;264(1):557-63
  31. Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM
    Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. European journal of biochemistry / FEBS 1990 Apr 30;189(2):287-93
  32. Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ
    Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. The Biochemical journal 1991 Aug 1;277 ( Pt 3):631-4
  33. Cassady AI, King AG, Cross NC, Hume DA
    Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene 1993 Aug 25;130(2):201-7
  34. Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML
    Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS letters 1988 Aug 29;236(2):275-81
  35. Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL
    Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. The Journal of biological chemistry 1991 Feb 5;266(4):2313-9
  36. Sharief FS, Li SS
    Structure of human prostatic acid phosphatase gene. Biochemical and biophysical research communications 1992 May 15;184(3):1468-76
  37. LaCount MW, Handy G, Lebioda L
    Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. The Journal of biological chemistry 1998 Nov 13;273(46):30406-9
  38. Yeung G, Mulero JJ, McGowan DW, Bajwa SS, Ford JE
    CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry 2000 Oct 24;39(42):12916-23
  39. Ivanenkov VV, Murphy-Piedmonte DM, Kirley TL
    Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function. Biochemistry 2003 Oct 14;42(40):11726-35
  40. Muniz O, Pelletier JP, Martel-Pelletier J, Morales S, Howell DS
    NTP pyrophosphohydrolase in human chondrocalcinotic and osteoarthritic cartilage. I. Some biochemical characteristics. Arthritis and rheumatism 1984 Feb;27(2):186-92
  41. Caswell AM, Russell RG
    Identification of ecto-nucleoside triphosphate pyrophosphatase in human articular chondrocytes in monolayer culture. Biochimica et biophysica acta 1985 Oct 30;847(1):40-7
  42. Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y
    Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. The Journal of biological chemistry 2001 Jun 1;276(22):18695-701
  43. Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA
    Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Human genetics 2002 Oct;111(4-5):360-7
  44. Van Rompay AR, Johansson M, Karlsson A
    Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. European journal of biochemistry / FEBS 1999 Apr;261(2):509-17
  45. Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A
    Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. The Journal of biological chemistry 1989 Jun 15;264(17):10148-55
  46. Xu G, O'Connell P, Stevens J, White R
    Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene. Genomics 1992 Jul;13(3):537-42
  47. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W
    Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome research 2000 May;10(5):703-13
  48. Ren H, Wang L, Bennett M, Liang Y, Zheng X, Lu F, Li L, Nan J, Luo M, Eriksson S, Zhang C, Su XD
    The crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus. Proceedings of the National Academy of Sciences of the United States of America 2005 Jan 11;102(2):303-8
  49. Luz CM, Konig I, Schirmer RH, Frank R
    Human cytosolic adenylate kinase allelozymes; purification and characterization. Biochimica et biophysica acta 1990 Mar 29;1038(1):80-4
  50. Gellerich FN, Ulrich J, Kunz W
    Unusual properties of mitochondria from the human term placenta are caused by alkaline phosphatase. Placenta 1994 Apr;15(3):299-310
  51. Chang CH, Cheng YC
    Substrate specificity of human ribonucleotide reductase from Molt-4F cells. Cancer research 1979 Dec;39(12):5081-6
  52. Fox RM
    Changes in deoxynucleoside triphosphate pools induced by inhibitors and modulators of ribonucleotide reductase. Pharmacology & therapeutics 1985;30(1):31-42
  53. Holmgren A
    Thioredoxin and glutaredoxin systems. The Journal of biological chemistry 1989 Aug 25;264(24):13963-6
  54. Sun C, Berardi MJ, Bushweller JH
    The NMR solution structure of human glutaredoxin in the fully reduced form. Journal of molecular biology 1998 Jul 24;280(4):687-701
  55. Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y
    In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase. Cancer research 2004 Jan 1;64(1):1-6
  56. Bausch-Jurken MT, Sabina RL
    Divergent N-terminal regions in AMP deaminase and isoform-specific catalytic properties of the enzyme. Archives of biochemistry and biophysics 1995 Aug 20;321(2):372-80
  57. Haas AL, Sabina RL
    Expression, purification, and inhibition of in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes. Protein expression and purification 2003 Feb;27(2):293-303
  58. Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL
    Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. The Journal of biological chemistry 1992 Nov 5;267(31):22407-13
  59. Van den Bergh F, Sabina RL
    Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extensions of isoform L. The Biochemical journal 1995 Dec 1;312 ( Pt 2):401-10
  60. Mahnke-Zizelman DK, van den Bergh F, Bausch-Jurken MT, Eddy R, Sait S, Shows TB, Sabina RL
    Cloning, sequence and characterization of the human AMPD2 gene: evidence for transcriptional regulation by two closely spaced promoters. Biochimica et biophysica acta 1996 Aug 14;1308(2):122-32
  61. Sabina RL, Morisaki T, Clarke P, Eddy R, Shows TB, Morton CC, Holmes EW
    Characterization of the human and rat myoadenylate deaminase genes. The Journal of biological chemistry 1990 Jun 5;265(16):9423-33
  62. Sabina RL, Fishbein WN, Pezeshkpour G, Clarke PR, Holmes EW
    Molecular analysis of the myoadenylate deaminase deficiencies. Neurology 1992 Jan;42(1):170-9
  63. Morisaki T, Gross M, Morisaki H, Pongratz D, Zollner N, Holmes EW
    Molecular basis of AMP deaminase deficiency in skeletal muscle. Proceedings of the National Academy of Sciences of the United States of America 1992 Jul 15;89(14):6457-61
  64. Morisaki H, Higuchi I, Abe M, Osame M, Morisaki T
    First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient. Human mutation 2000 Dec;16(6):467-72
  65. Mahnke-Zizelman DK, Sabina RL
    Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. The Journal of biological chemistry 1992 Oct 15;267(29):20866-77
  66. Yamada Y, Goto H, Ogasawara N
    Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase. Biochimica et biophysica acta 1992 Nov 15;1171(1):125-8
  67. Yamada Y, Goto H, Ogasawara N
    A point mutation responsible for human erythrocyte AMP deaminase deficiency. Human molecular genetics 1994 Feb;3(2):331-4
  68. Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL
    Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing. Biochimica et biophysica acta 1996 Apr 10;1306(1):75-92
  69. Stone RL, Aimi J, Barshop BA, Jaeken J, Van den Berghe G, Zalkin H, Dixon JE
    A mutation in adenylosuccinate lyase associated with mental retardation and autistic features. Nature genetics 1992 Apr;1(1):59-63
  70. Maaswinkel-Mooij PD, Laan LA, Onkenhout W, Brouwer OF, Jaeken J, Poorthuis BJ
    Adenylosuccinase deficiency presenting with epilepsy in early infancy. Journal of inherited metabolic disease 1997 Aug;20(4):606-7
  71. Verginelli D, Luckow B, Crifo C, Salerno C, Gross M
    Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells. Biochimica et biophysica acta 1998 Feb 27;1406(1):81-4
  72. Kmoch S, Hartmannova H, Stiburkova B, Krijt J, Zikanova M, Sebesta I
    Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients. Human molecular genetics 2000 Jun 12;9(10):1501-13
  73. Race V, Marie S, Vincent MF, Van den Berghe G
    Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. Human molecular genetics 2000 Sep 1;9(14):2159-65
  74. Guicherit OM, Rudolph FB, Kellems RE, Cooper BF
    Molecular cloning and expression of a mouse muscle cDNA encoding adenylosuccinate synthetase. The Journal of biological chemistry 1991 Nov 25;266(33):22582-7
  75. Powell SM, Zalkin H, Dixon JE
    Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS letters 1992 May 25;303(1):4-10
  76. Guicherit OM, Cooper BF, Rudolph FB, Kellems RE
    Amplification of an adenylosuccinate synthetase gene in alanosine-resistant murine T-lymphoma cells. Molecular cloning of a cDNA encoding the "non-muscle" isozyme. The Journal of biological chemistry 1994 Feb 11;269(6):4488-96
  77. Borza T, Iancu CV, Pike E, Honzatko RB, Fromm HJ
    Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance. The Journal of biological chemistry 2003 Feb 28;278(9):6673-9
  78. Sun H, Li N, Wang X, Chen T, Shi L, Zhang L, Wang J, Wan T, Cao X
    Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells. Molecular and cellular biochemistry 2005 Jan;269(1-2):85-94
  79. Kojima T, Nishina T, Kitamura M, Yamanak H, Nishioka K
    A new method for the determination of adenine phosphoribosyltransferase activity in human erythrocytes by reversed phase high performance liquid chromatography. Biomedical chromatography : BMC. 1991 Mar;5(2):57-61
  80. Kalsi KK, Zych M, Slominska EM, Kochan Z, Yacoub MH, Smolenski RT
    Adenine incorporation in human and rat endothelium. Biochimica et biophysica acta 1999 Nov 11;1452(2):145-50
  81. Silva M, Silva CH, Iulek J, Thiemann OH
    Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis. Biochemistry 2004 Jun 22;43(24):7663-71
  82. Xu Y, Grubmeyer C
    Catalysis in human hypoxanthine-guanine phosphoribosyltransferase: Asp 137 acts as a general acid/base. Biochemistry 1998 Mar 24;37(12):4114-24
  83. Yeh J, Zheng S, Howard BD
    Impaired differentiation of HPRT-deficient dopaminergic neurons: a possible mechanism underlying neuronal dysfunction in Lesch-Nyhan syndrome. Journal of neuroscience research 1998 Jul 1;53(1):78-85
  84. Craig SP 3rd, Eakin AE
    Purine phosphoribosyltransferases. The Journal of biological chemistry 2000 Jul 7;275(27):20231-4
  85. Sujay Subbayya IN, Sukumaran S, Shivashankar K, Balaram H
    Unusual substrate specificity of a chimeric hypoxanthine-guanine phosphoribosyltransferase containing segments from the Plasmodium falciparum and human enzymes. Biochemical and biophysical research communications 2000 Jun 7;272(2):596-602
  86. Puig JG, Torres RJ, Mateos FA, Ramos TH, Arcas JM, Buno AS, O'Neill P
    The spectrum of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Clinical experience based on 22 patients from 18 Spanish families. Medicine 2001 Mar;80(2):102-12
  87. Erion MD, Stoeckler JD, Guida WC, Walter RL, Ealick SE
    Purine nucleoside phosphorylase. 2. Catalytic mechanism. Biochemistry 1997 Sep 30;36(39):11735-48
  88. Mao C, Cook WJ, Zhou M, Federov AA, Almo SC, Ealick SE
    Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues. Biochemistry 1998 May 19;37(20):7135-46
  89. Pugmire MJ, Ealick SE
    Structural analyses reveal two distinct families of nucleoside phosphorylases. The Biochemical journal 2002 Jan 1;361(Pt 1):1-25
  90. Williams SR, Goddard JM, Martin DW Jr
    Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic acids research 1984 Jul 25;12(14):5779-87
  91. Williams SR, Gekeler V, McIvor RS, Martin DW Jr
    A human purine nucleoside phosphorylase deficiency caused by a single base change. The Journal of biological chemistry 1987 Feb 15;262(5):2332-8
  92. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr
    Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. The Journal of biological chemistry 1990 Jan 25;265(3):1812-20
  93. Muller G
    [Immune insufficiency in enzyme defects of purine metabolism] Zeitschrift fur die gesamte innere Medizin und ihre Grenzgebiete. 1983 Feb 1;38(3):83-9
  94. Simmonds HA, Goday A, Morris GS, Brolsma MF
    Metabolism of deoxynucleosides by lymphocytes in long-term culture deficient in different purine enzymes. Biochemical pharmacology 1984 Mar 1;33(5):763-70
  95. Cristalli G, Costanzi S, Lambertucci C, Lupidi G, Vittori S, Volpini R, Camaioni E
    Adenosine deaminase: functional implications and different classes of inhibitors. Medicinal research reviews 2001 Mar;21(2):105-28
  96. Gerber AP, Keller W
    RNA editing by base deamination: more enzymes, more targets, new mysteries. Trends in biochemical sciences 2001 Jun;26(6):376-84