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) [7], 
      [9], [10], 
      Nucleoside non-metastatic cells 6, protein expressed in 
      (nucleoside-diphosphate kinase) (NDPK 6) [8], 
      [11], 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], [18], 
      [19], 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) [44], 
      [45], Adenylate kinase 2 (AK2) [44], 
      [45], Adenylate kinase 3-like 1 (AK3) [44], 
      [46], 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 [87], 
      [88], [89], [90], 
      [91], [92]. 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
    
    
      - 
        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
       
      - 
        Guignard F, Markert M
The 
        nucleoside diphosphate kinase of human neutrophils. The 
        Biochemical journal 1996 May 15;316 ( Pt 1):233-8
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        Wang TF, Guidotti G
CD39 
        is an ecto-(Ca2+,Mg2+)-apyrase. The Journal of biological 
        chemistry 1996 Apr 26;271(17):9898-901
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        Sharief FS, Li SS
Structure 
        of human prostatic acid phosphatase gene. Biochemical and 
        biophysical research communications 1992 May 15;184(3):1468-76
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        Chang CH, Cheng YC
Substrate 
        specificity of human ribonucleotide reductase from Molt-4F cells. 
        Cancer research 1979 Dec;39(12):5081-6
       
      - 
        Fox RM
Changes 
        in deoxynucleoside triphosphate pools induced by inhibitors and 
        modulators of ribonucleotide reductase. Pharmacology & 
        therapeutics 1985;30(1):31-42
       
      - 
        Holmgren A
Thioredoxin 
        and glutaredoxin systems. The Journal of biological chemistry 1989 
        Aug 25;264(24):13963-6
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        Sabina RL, Fishbein WN, Pezeshkpour G, Clarke PR, Holmes EW
Molecular 
        analysis of the myoadenylate deaminase deficiencies. Neurology 
        1992 Jan;42(1):170-9
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        Craig SP 3rd, Eakin AE
Purine 
        phosphoribosyltransferases. The Journal of biological chemistry 
        2000 Jul 7;275(27):20231-4
       
      - 
        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
       
      - 
        Puig JG, Torres RJ, Mateos FA, Ramos TH, Arcas JM, Bu?o 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
       
      - 
        Erion MD, Stoeckler JD, Guida WC, Walter RL, Ealick SE
Purine 
        nucleoside phosphorylase. 2. Catalytic mechanism. Biochemistry 
        1997 Sep 30;36(39):11735-48
       
      - 
        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
       
      - 
        Pugmire MJ, Ealick SE
Structural 
        analyses reveal two distinct families of nucleoside phosphorylases. 
        The Biochemical journal 2002 Jan 1;361(Pt 1):1-25
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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
       
      - 
        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