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Volumn 51, Issue 3, 2010, Pages 326-336

Characterisation of the first wheat (Triticum aestivum L.) nucleotide pyrophosphatase/phosphodiesterase resembling mammalian counterparts

Author keywords

Nicotinamide coenzymes; Nucleotide pyrophosphatase phosphodiesterase; Wheat

Indexed keywords

HORDEUM; MAMMALIA; PICHIA PASTORIS; TRITICUM AESTIVUM;

EID: 77953129022     PISSN: 07335210     EISSN: 10959963     Source Type: Journal    
DOI: 10.1016/j.jcs.2010.01.009     Document Type: Article
Times cited : (8)

References (32)
  • 1
    • 0028964748 scopus 로고
    • Autophosphorylation of PC-1 (alkaline phosphodiesterase-I nucleotide pyrophosphatase) and analysis of the active site
    • Belli S.I., Mercuri F.A., Sali A., and Goding J.W. Autophosphorylation of PC-1 (alkaline phosphodiesterase-I nucleotide pyrophosphatase) and analysis of the active site. European Journal of Biochemistry 228 (1995) 669-676
    • (1995) European Journal of Biochemistry , vol.228 , pp. 669-676
    • Belli, S.I.1    Mercuri, F.A.2    Sali, A.3    Goding, J.W.4
  • 2
    • 0027490009 scopus 로고
    • Identification and characterization of a soluble form of the plasma-cell membrane glycoprotein PC-1 (5′-nucleotide phosphodiesterase)
    • Belli S.I., Vandriel I.R., and Goding J.W. Identification and characterization of a soluble form of the plasma-cell membrane glycoprotein PC-1 (5′-nucleotide phosphodiesterase). European Journal of Biochemistry 217 (1993) 421-428
    • (1993) European Journal of Biochemistry , vol.217 , pp. 421-428
    • Belli, S.I.1    Vandriel, I.R.2    Goding, J.W.3
  • 3
    • 0035158370 scopus 로고    scopus 로고
    • Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis
    • Bello V., Goding J.W., Greengrass V., Sali A., Dubljevic V., Lenoir C., Trugnan G., and Maurice M. Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis. Molecular Biology of the Cell 12 (2001) 3004-3015
    • (2001) Molecular Biology of the Cell , vol.12 , pp. 3004-3015
    • Bello, V.1    Goding, J.W.2    Greengrass, V.3    Sali, A.4    Dubljevic, V.5    Lenoir, C.6    Trugnan, G.7    Maurice, M.8
  • 5
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0141532169 scopus 로고    scopus 로고
    • Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family
    • Duan R.D., Bergman T., Xu N., Wu J., Cheng Y., Duan J.X., Nelander S., Palmberg C., and Nilsson A. Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family. Journal of Biological Chemistry 278 (2003) 38528-38536
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 38528-38536
    • Duan, R.D.1    Bergman, T.2    Xu, N.3    Wu, J.4    Cheng, Y.5    Duan, J.X.6    Nelander, S.7    Palmberg, C.8    Nilsson, A.9
  • 8
    • 0031732134 scopus 로고    scopus 로고
    • The hydrolytic activity of bovine adrenal medullary plasma membranes towards diadenosine polyphosphates is due to alkaline phosphodiesterase-I
    • Gasmi L., Cartwright J.L., and McLennan A.G. The hydrolytic activity of bovine adrenal medullary plasma membranes towards diadenosine polyphosphates is due to alkaline phosphodiesterase-I. Biochimica Et Biophysica Acta-Molecular Cell Research 1405 (1998) 121-127
    • (1998) Biochimica Et Biophysica Acta-Molecular Cell Research , vol.1405 , pp. 121-127
    • Gasmi, L.1    Cartwright, J.L.2    McLennan, A.G.3
  • 10
    • 0035847049 scopus 로고    scopus 로고
    • Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases
    • Gijsbers R., Ceulemans H., Stalmans W., and Bollen M. Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases. Journal of Biological Chemistry 276 (2001) 1361-1368
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 1361-1368
    • Gijsbers, R.1    Ceulemans, H.2    Stalmans, W.3    Bollen, M.4
  • 11
    • 0033816854 scopus 로고    scopus 로고
    • Ecto-enzymes: physiology meets pathology
    • Goding J.W. Ecto-enzymes: physiology meets pathology. Journal of Leukocyte Biology 67 (2000) 285-311
    • (2000) Journal of Leukocyte Biology , vol.67 , pp. 285-311
    • Goding, J.W.1
  • 12
    • 0038664247 scopus 로고    scopus 로고
    • Physiological and pathophysiological functions of the ecto-nucleotide pyrophosphatase/phosphodiesterase family
    • Goding J.W., Grobben B., and Slegers H. Physiological and pathophysiological functions of the ecto-nucleotide pyrophosphatase/phosphodiesterase family. Biochimica et Biophysica-Molecular Basis of Disease 1638 (2003) 1-19
    • (2003) Biochimica et Biophysica-Molecular Basis of Disease , vol.1638 , pp. 1-19
    • Goding, J.W.1    Grobben, B.2    Slegers, H.3
  • 13
    • 0006366015 scopus 로고    scopus 로고
    • Inhibition of phosphodiesterase/pyrophosphatase activity of PC-1 by its association with glycosaminoglycans
    • Hosoda N., Hoshino S., Kanda Y., and Katada T. Inhibition of phosphodiesterase/pyrophosphatase activity of PC-1 by its association with glycosaminoglycans. European Journal of Biochemistry 265 (1999) 763-770
    • (1999) European Journal of Biochemistry , vol.265 , pp. 763-770
    • Hosoda, N.1    Hoshino, S.2    Kanda, Y.3    Katada, T.4
  • 14
    • 34247495740 scopus 로고    scopus 로고
    • An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D
    • Jansen S., Callewaert N., Dewerte I., Andries M., Ceulemans H., and Bollen M. An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D. Journal of Biological Chemistry 282 (2007) 11084-11091
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 11084-11091
    • Jansen, S.1    Callewaert, N.2    Dewerte, I.3    Andries, M.4    Ceulemans, H.5    Bollen, M.6
  • 16
    • 33748539040 scopus 로고    scopus 로고
    • Plant responses to extracellular nucleotides: cellular processes and biological effects
    • Jeter C.R., and Roux S.J. Plant responses to extracellular nucleotides: cellular processes and biological effects. Purinergic Signalling 2 (2006) 443-449
    • (2006) Purinergic Signalling , vol.2 , pp. 443-449
    • Jeter, C.R.1    Roux, S.J.2
  • 17
    • 67649205136 scopus 로고    scopus 로고
    • Endogenous redox agents and enzymes affecting protein network formation during breadmaking - a review
    • Joye I.J., Lagrain B., and Delcour J.A. Endogenous redox agents and enzymes affecting protein network formation during breadmaking - a review. Journal of Cereal Science 50 (2009) 1-10
    • (2009) Journal of Cereal Science , vol.50 , pp. 1-10
    • Joye, I.J.1    Lagrain, B.2    Delcour, J.A.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laëmmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227 (1970) 680
    • (1970) Nature , vol.227 , pp. 680
    • Laëmmli, U.K.1
  • 19
    • 0021099576 scopus 로고
    • The catalytic mechanism of bovine intestinal 5′-nucleotide phosphodiesterase - pH and inhibition studies
    • Moe O.A., and Butler L.G. The catalytic mechanism of bovine intestinal 5′-nucleotide phosphodiesterase - pH and inhibition studies. Journal of Biological Chemistry 258 (1983) 6941-6946
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 6941-6946
    • Moe, O.A.1    Butler, L.G.2
  • 21
    • 70349783589 scopus 로고    scopus 로고
    • Nucleotide pyrophosphatase/phosphodiesterase from Euphorbia characias latex: purification and characterization
    • Pintus F., Spano D., Bellelli A., Angelucci F., Floris G., and Medda R. Nucleotide pyrophosphatase/phosphodiesterase from Euphorbia characias latex: purification and characterization. Plant Science 177 (2009) 636-642
    • (2009) Plant Science , vol.177 , pp. 636-642
    • Pintus, F.1    Spano, D.2    Bellelli, A.3    Angelucci, F.4    Floris, G.5    Medda, R.6
  • 22
    • 20744450739 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a novel choline-specific glycerophosphodiester phosphodiesterase belonging to the nucleotide pyrophosphatase/phosphodiesterase family
    • Sakagami H., Aoki J., Natori Y., Nishikawa K., Kakehi Y., Natori Y., and Arai H. Biochemical and molecular characterization of a novel choline-specific glycerophosphodiester phosphodiesterase belonging to the nucleotide pyrophosphatase/phosphodiesterase family. Journal of Biological Chemistry 280 (2005) 23084-23093
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 23084-23093
    • Sakagami, H.1    Aoki, J.2    Natori, Y.3    Nishikawa, K.4    Kakehi, Y.5    Natori, Y.6    Arai, H.7
  • 23
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Research 31 (2003) 3381-3385
    • (2003) Nucleic Acids Research , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 24
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., and Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nature Protocols 1 (2006) 2856-2860
    • (2006) Nature Protocols , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 25
    • 34548012770 scopus 로고    scopus 로고
    • Modulation of purinergic signalling by NPP-type ectophosphodiesterases
    • Stefan C., Jansen S., and Bollen M. Modulation of purinergic signalling by NPP-type ectophosphodiesterases. Purinergic Signalling 2 (2006) 361-370
    • (2006) Purinergic Signalling , vol.2 , pp. 361-370
    • Stefan, C.1    Jansen, S.2    Bollen, M.3
  • 26
    • 0029657920 scopus 로고    scopus 로고
    • Threonine autophosphorylation and nucleotidylation of the hepatic membrane protein PC-1
    • Stefan C., Stalmans W., and Bollen M. Threonine autophosphorylation and nucleotidylation of the hepatic membrane protein PC-1. European Journal of Biochemistry 241 (1996) 338-342
    • (1996) European Journal of Biochemistry , vol.241 , pp. 338-342
    • Stefan, C.1    Stalmans, W.2    Bollen, M.3
  • 27
    • 0014600637 scopus 로고
    • Significance of intermediary plateau regions in enzyme saturation curves
    • Teipel J., and Koshland D.E. Significance of intermediary plateau regions in enzyme saturation curves. Biochemistry 8 (1969) 4656
    • (1969) Biochemistry , vol.8 , pp. 4656
    • Teipel, J.1    Koshland, D.E.2
  • 28
    • 0028838955 scopus 로고
    • Regulation of purified hepatic PC-1 (phosphodiesterase-I nucleotide pyrophosphatase) by threonine auto(de)phosphorylation and by binding of acidic fibroblast growth-factor
    • Uriarte M., Stalmans W., Hickman S., and Bollen M. Regulation of purified hepatic PC-1 (phosphodiesterase-I nucleotide pyrophosphatase) by threonine auto(de)phosphorylation and by binding of acidic fibroblast growth-factor. Biochemical Journal 306 (1995) 271-277
    • (1995) Biochemical Journal , vol.306 , pp. 271-277
    • Uriarte, M.1    Stalmans, W.2    Hickman, S.3    Bollen, M.4
  • 29
    • 41949083203 scopus 로고    scopus 로고
    • Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade
    • Yegutkin G.G. Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade. Biochimica Et Biophysica Acta-Molecular Cell Research 1783 (2008) 673-694
    • (2008) Biochimica Et Biophysica Acta-Molecular Cell Research , vol.1783 , pp. 673-694
    • Yegutkin, G.G.1
  • 30
    • 33747517236 scopus 로고    scopus 로고
    • Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: Implications for mechanism and evolution
    • Zalatan J.G., Fenn T.D., Brunger A.T., and Herschlag D. Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: Implications for mechanism and evolution. Biochemistry 45 (2006) 9788-9803
    • (2006) Biochemistry , vol.45 , pp. 9788-9803
    • Zalatan, J.G.1    Fenn, T.D.2    Brunger, A.T.3    Herschlag, D.4
  • 31
    • 31944441501 scopus 로고    scopus 로고
    • Alkaline phosphatase mono- and diesterase reactions: comparative transition state analysis
    • Zalatan J.G., and Herschlag D. Alkaline phosphatase mono- and diesterase reactions: comparative transition state analysis. Journal of the American Chemical Society 128 (2006) 1293-1303
    • (2006) Journal of the American Chemical Society , vol.128 , pp. 1293-1303
    • Zalatan, J.G.1    Herschlag, D.2
  • 32
    • 0033152549 scopus 로고    scopus 로고
    • Two novel families of ectonucleotidases: molecular structures, catalytic properties and a search for function
    • Zimmermann H. Two novel families of ectonucleotidases: molecular structures, catalytic properties and a search for function. Trends in Pharmacological Sciences 20 (1999) 231-236
    • (1999) Trends in Pharmacological Sciences , vol.20 , pp. 231-236
    • Zimmermann, H.1


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