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Volumn 413, Issue 1, 2008, Pages 103-113

Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: A novel metallophosphoesterase family preferentially expressed in rodent immune cells

Author keywords

ADP ribose; CDP choline; Immune system; Metallophosphoesterase; Nudix; Signalling

Indexed keywords

MANGANESE COMPOUNDS;

EID: 46249105799     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071471     Document Type: Article
Times cited : (12)

References (51)
  • 1
    • 0030998860 scopus 로고    scopus 로고
    • ADP-ribose. A historical overview
    • Hilz, H. (1997) ADP-ribose. A historical overview. Adv. Exp. Med. Biol. 419, 15-24
    • (1997) Adv. Exp. Med. Biol , vol.419 , pp. 15-24
    • Hilz, H.1
  • 2
    • 1542346420 scopus 로고    scopus 로고
    • The new life of a centenarian: Signalling functions of NAD(P)
    • Berger, F., Ramirez-Hernandez, M. H. and Ziegler, M. (2004) The new life of a centenarian: signalling functions of NAD(P). Trends Biochem. Sci. 29, 111-118
    • (2004) Trends Biochem. Sci , vol.29 , pp. 111-118
    • Berger, F.1    Ramirez-Hernandez, M.H.2    Ziegler, M.3
  • 9
    • 26444439972 scopus 로고    scopus 로고
    • TRPM2: A calcium influx pathway regulated by oxidative stress and the novel second messenger ADP-ribose
    • Kühn, F. J., Heiner, I. and Lückhoff, A. (2005) TRPM2: a calcium influx pathway regulated by oxidative stress and the novel second messenger ADP-ribose. Pflugers Arch. 451, 212-219
    • (2005) Pflugers Arch , vol.451 , pp. 212-219
    • Kühn, F.J.1    Heiner, I.2    Lückhoff, A.3
  • 13
    • 0037203939 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5′-diphosphoribose (ADP-ribose)
    • Lin, S., Gasmi, L., Xie, Y., Ying, K., Gu, S., Wang, Z., Jin, H., Chao, Y., Wu, C., Zhou, Z. et al. (2002) Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5′-diphosphoribose (ADP-ribose). Biochim. Biophys. Acta 1594, 127-135
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 127-135
    • Lin, S.1    Gasmi, L.2    Xie, Y.3    Ying, K.4    Gu, S.5    Wang, Z.6    Jin, H.7    Chao, Y.8    Wu, C.9    Zhou, Z.10
  • 14
    • 0037449761 scopus 로고    scopus 로고
    • NUDT9, a member of the Nudix hydrolase family, is an evolutionary conserved mitochondrial ADP-ribose pyrophosphatase
    • Perraud, A. L., Shen, B., Dunn, C. A., Rippe, K., Smith, M. K., Bessman, M. J., Stoddard, B. L. and Scharenberg, A. M. (2003) NUDT9, a member of the Nudix hydrolase family, is an evolutionary conserved mitochondrial ADP-ribose pyrophosphatase. J. Biol. Chem. 278, 1794-1801
    • (2003) J. Biol. Chem , vol.278 , pp. 1794-1801
    • Perraud, A.L.1    Shen, B.2    Dunn, C.A.3    Rippe, K.4    Smith, M.K.5    Bessman, M.J.6    Stoddard, B.L.7    Scharenberg, A.M.8
  • 16
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes
    • Bessman, M. J., Frick, D. N. and O'Handley, S. F. (1996) The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. J. Biol. Chem. 271, 25059-25062
    • (1996) J. Biol. Chem , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 17
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superiamily
    • McLennan, A. G. (2006) The Nudix hydrolase superiamily. Cell. Mol. Life Sci. 63, 123-143
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 18
    • 0021287324 scopus 로고
    • 4-tetraphosphates in rat liver. Characterization as the specific dinucleoside tetraphosphatase and a phosphodiesterase I-like enzyme
    • 4-tetraphosphates in rat liver. Characterization as the specific dinucleoside tetraphosphatase and a phosphodiesterase I-like enzyme. J. Biol. Chem. 259, 2879-2885
    • (1984) J. Biol. Chem , vol.259 , pp. 2879-2885
    • Cameselle, J.C.1    Costas, M.J.2    Günther Sillero, M.A.3    Sillero, A.4
  • 21
    • 0035799396 scopus 로고    scopus 로고
    • Human placenta hydrolases active on free ADP-ribose: An ADP-sugar pyrophosphatase and a specific ADP-ribose pyrophosphatase
    • Ribeiro, J. M., Carloto, A., Costas, M. J. and Cameselle, J. C. (2001) Human placenta hydrolases active on free ADP-ribose: an ADP-sugar pyrophosphatase and a specific ADP-ribose pyrophosphatase. Biochim. Biophys. Acta 1526, 86-94
    • (2001) Biochim. Biophys. Acta , vol.1526 , pp. 86-94
    • Ribeiro, J.M.1    Carloto, A.2    Costas, M.J.3    Cameselle, J.C.4
  • 22
    • 0033452851 scopus 로고    scopus 로고
    • Cloning, expression and characterization of YSA1H, a human adenosine 5′- diphosphosugar pyrophosphatase possessing a MutT motif
    • Gasmi, L., Cartwright, J. L. and McLennan, A. G. (1999) Cloning, expression and characterization of YSA1H, a human adenosine 5′- diphosphosugar pyrophosphatase possessing a MutT motif. Biochem. J. 344, 331-337
    • (1999) Biochem. J , vol.344 , pp. 331-337
    • Gasmi, L.1    Cartwright, J.L.2    McLennan, A.G.3
  • 23
    • 27844608412 scopus 로고    scopus 로고
    • Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases
    • Cabezas, A., Costas, M. J., Pinto, R. M., Couto, A. and Cameselle, J. C. (2005) Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases. Biochem. Biophys. Res. Commun. 338, 1682-1689
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 1682-1689
    • Cabezas, A.1    Costas, M.J.2    Pinto, R.M.3    Couto, A.4    Cameselle, J.C.5
  • 24
    • 0014163158 scopus 로고
    • The statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1967) The statistical analysis of enzyme kinetic data. Adv. Enzymol. Relat. Areas Mol. Biol. 29, 1-32
    • (1967) Adv. Enzymol. Relat. Areas Mol. Biol , vol.29 , pp. 1-32
    • Cleland, W.W.1
  • 26
    • 46749158696 scopus 로고    scopus 로고
    • Kruisbeek, A. M. (2000) Isolation and fractionation of mononuclear cell populations. Current Protocols in Immunology, (Coligan, J. E., Bierer, B. E., Margulies, D. H., Shevach, E. M. and Strober, W., eds), pp. 3.1.1-3.1.5, John Wiley and Sons, New York
    • Kruisbeek, A. M. (2000) Isolation and fractionation of mononuclear cell populations. Current Protocols in Immunology, (Coligan, J. E., Bierer, B. E., Margulies, D. H., Shevach, E. M. and Strober, W., eds), pp. 3.1.1-3.1.5, John Wiley and Sons, New York
  • 29
    • 14844293471 scopus 로고    scopus 로고
    • A component-based software environment for visualizing large macromolecular assemblies
    • Sanner, M. F. (2005) A component-based software environment for visualizing large macromolecular assemblies. Structure 13, 447-462
    • (2005) Structure , vol.13 , pp. 447-462
    • Sanner, M.F.1
  • 30
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word, J. M., Lovell, S. C., Richardson, J. S. and Richardson, D. C. (1999) Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285, 1735-1747
    • (1999) J. Mol. Biol , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 31
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K. and Olson, A. J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19, 1639-1662
    • (1998) J. Comput. Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 32
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M. and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 33
    • 0029645578 scopus 로고
    • Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1
    • Lohse, D. L., Denu, J. M. and Dixon, J. E. (1995) Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1. Structure 3, 987-990
    • (1995) Structure , vol.3 , pp. 987-990
    • Lohse, D.L.1    Denu, J.M.2    Dixon, J.E.3
  • 34
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
    • Klabunde, T., Strater, N., Frohlich, R., Witzel, H. and Krebs, B. (1996) Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures. J. Mol. Biol. 259, 737-748
    • (1996) J. Mol. Biol , vol.259 , pp. 737-748
    • Klabunde, T.1    Strater, N.2    Frohlich, R.3    Witzel, H.4    Krebs, B.5
  • 35
    • 0037083671 scopus 로고    scopus 로고
    • 3,5′-Cyclic nucleotide phosphodiesterases class III: Members, structure, and catalytic mechanism
    • Richter, W. (2002) 3,5′-Cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism. Proteins 46, 278-286
    • (2002) Proteins , vol.46 , pp. 278-286
    • Richter, W.1
  • 36
    • 33751515585 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis
    • Shenoy, A. R., Capuder, M., Draskovic, P., Lamba, D., Visweswariah, S. S. and Podobnik, M. (2007) Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis. J. Mol. Biol. 365, 211-225
    • (2007) J. Mol. Biol , vol.365 , pp. 211-225
    • Shenoy, A.R.1    Capuder, M.2    Draskovic, P.3    Lamba, D.4    Visweswariah, S.S.5    Podobnik, M.6
  • 38
    • 9444285520 scopus 로고    scopus 로고
    • Microarray and comparative genomics-based identification of genes and gene regulatory regions of the mouse immune system
    • Hutton, J. J., Jegga, A. G., Kong, S., Gupta, A., Ebert, C., Williams, S., Katz, J. D. and Aronow, B. J. (2004) Microarray and comparative genomics-based identification of genes and gene regulatory regions of the mouse immune system. BMC Genomics 5, 82
    • (2004) BMC Genomics , vol.5 , pp. 82
    • Hutton, J.J.1    Jegga, A.G.2    Kong, S.3    Gupta, A.4    Ebert, C.5    Williams, S.6    Katz, J.D.7    Aronow, B.J.8
  • 39
    • 25144473903 scopus 로고    scopus 로고
    • NPP-type ectophosphodiesterases: Unity in diversity
    • Stefan, C., Jansen, S. and Bollen, M. (2005) NPP-type ectophosphodiesterases: unity in diversity. Trends Biochem. Sci. 30, 542-550
    • (2005) Trends Biochem. Sci , vol.30 , pp. 542-550
    • Stefan, C.1    Jansen, S.2    Bollen, M.3
  • 41
    • 0242501006 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose
    • Yagi, T., Baroja-Fernández, E., Yamamoto, R., Muñoz, F. J., Akazawa, T., Hong, K. S. and Pozueta-Romero, J. (2003) Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose. Biochem. J. 370, 409-415
    • (2003) Biochem. J , vol.370 , pp. 409-415
    • Yagi, T.1    Baroja-Fernández, E.2    Yamamoto, R.3    Muñoz, F.J.4    Akazawa, T.5    Hong, K.S.6    Pozueta-Romero, J.7
  • 42
    • 33645014444 scopus 로고    scopus 로고
    • YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate X) hydrolase superfamily
    • Tirrell, I. M., Wall, J. L., Daley, C. J., Denial, S. J., Tennis, F. G., Galens, K. G. and O'Handley, S. F. (2006) YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate X) hydrolase superfamily. Biochem. J. 394, 665-674
    • (2006) Biochem. J , vol.394 , pp. 665-674
    • Tirrell, I.M.1    Wall, J.L.2    Daley, C.J.3    Denial, S.J.4    Tennis, F.G.5    Galens, K.G.6    O'Handley, S.F.7
  • 43
    • 2642579311 scopus 로고    scopus 로고
    • The 26 Nudix hydrolases of Bacillus cereus, a close relative of Bacillus anthracis
    • Xu, W., Dunn, C. A., Jones, C. R., D'Souza, G. and Bessman, M. J. (2004) The 26 Nudix hydrolases of Bacillus cereus, a close relative of Bacillus anthracis. J. Biol. Chem. 279, 24861-24865
    • (2004) J. Biol. Chem , vol.279 , pp. 24861-24865
    • Xu, W.1    Dunn, C.A.2    Jones, C.R.3    D'Souza, G.4    Bessman, M.J.5
  • 44
    • 0020452229 scopus 로고
    • Determination of free and bound manganese(II) in hepatocytes from fed and fasted rats
    • Ash, D. E. and Schramm, V. L. (1982) Determination of free and bound manganese(II) in hepatocytes from fed and fasted rats. J. Biol. Chem. 257, 9261-9264
    • (1982) J. Biol. Chem , vol.257 , pp. 9261-9264
    • Ash, D.E.1    Schramm, V.L.2
  • 46
    • 0030908472 scopus 로고    scopus 로고
    • Intramolecular ADP-ribose transfer reactions and calcium signalling. Potential role of 2′-phospho-cyclic ADP-ribose in oxidative stress
    • Vu, C. Q., Coyle, D. L., Tai, H. H., Jacobson, E. L. and Jacobson, M. K. (1997) Intramolecular ADP-ribose transfer reactions and calcium signalling. Potential role of 2′-phospho-cyclic ADP-ribose in oxidative stress. Adv. Exp. Med. Biol. 419, 381-388
    • (1997) Adv. Exp. Med. Biol , vol.419 , pp. 381-388
    • Vu, C.Q.1    Coyle, D.L.2    Tai, H.H.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 48
    • 34848922987 scopus 로고    scopus 로고
    • New molecular mechanisms on the activation of TRPM2 channels by oxidative stress and ADP-Ribose
    • Naziroglu, M. (2007) New molecular mechanisms on the activation of TRPM2 channels by oxidative stress and ADP-Ribose. Neurochem. Res. 32, 1990-2001
    • (2007) Neurochem. Res , vol.32 , pp. 1990-2001
    • Naziroglu, M.1
  • 49
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in mammalian cells
    • Vance, J. E. and Vance, D. E. (2004) Phospholipid biosynthesis in mammalian cells. Biochem. Cell Biol. 82, 113-128
    • (2004) Biochem. Cell Biol , vol.82 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 50
    • 14644423932 scopus 로고    scopus 로고
    • Regulatory enzymes of phosphatidylcholine biosynthesis: A personal perspective
    • Kent, C. (2005) Regulatory enzymes of phosphatidylcholine biosynthesis: a personal perspective. Biochim. Biophys. Acta 1733, 53-66
    • (2005) Biochim. Biophys. Acta , vol.1733 , pp. 53-66
    • Kent, C.1
  • 51
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1


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