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Volumn 280, Issue 1, 1998, Pages 153-166

Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 Å resolution

Author keywords

Crystallization; E. coli formycin B; Purine nucleoside phosphorylase; X ray crystallography

Indexed keywords

ARGININE; FORMYCIN B; GLYCINE; INOSINE; PURINE NUCLEOSIDE PHOSPHORYLASE; SERINE;

EID: 0032479324     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1799     Document Type: Article
Times cited : (83)

References (81)
  • 1
    • 8944231024 scopus 로고
    • Immunological aberrations in purine nucleoside deficiencies
    • Ammann A.J. Immunological aberrations in purine nucleoside deficiencies. Ciba Found. Symp. 68:1978;55-57
    • (1978) Ciba Found. Symp. , vol.68 , pp. 55-57
    • Ammann, A.J.1
  • 2
    • 0002411932 scopus 로고
    • Biologically active nucelosides and nucleotides: Conformational features and interactions with enzymes
    • S. Neidle. Macmilian Press. Part 3
    • Birnbaum G.I., Shugar D. Biologically active nucelosides and nucleotides conformational features and interactions with enzymes. Neidle S. Topics in Nucleic Acid Structure. 1987;1-70 Macmilian Press. Part 3
    • (1987) Topics in Nucleic Acid Structure , pp. 1-70
    • Birnbaum, G.I.1    Shugar, D.2
  • 3
    • 0027377493 scopus 로고
    • Cladribine: A review of its pharmacodynamic and pharmacokinetic properties and therapeutic potential in haematological malignances
    • Bryson H.M., Sorkin E.M. Cladribine a review of its pharmacodynamic and pharmacokinetic properties and therapeutic potential in haematological malignances. Drugs. 46:1993;872-894
    • (1993) Drugs , vol.46 , pp. 872-894
    • Bryson, H.M.1    Sorkin, E.M.2
  • 4
    • 0022419375 scopus 로고
    • Aromatic-aromatic interactions: A mechanism of protein structure stabilization
    • Burley S.K., Petsko G.A. Aromatic-aromatic interactions a mechanism of protein structure stabilization. Science. 229:1985;23-28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 5
    • 0019192598 scopus 로고
    • A second purine nucleoside phosphorylase in Escherichia coli K-12. I. Xanthosine phosphorylase regulatory mutants isolated as secondary-site revertants of deoD mutant
    • Buxton R.S., Hammer-Jespersen K., Valentin-Hansen P. A second purine nucleoside phosphorylase in Escherichia coli K-12. I. Xanthosine phosphorylase regulatory mutants isolated as secondary-site revertants of deoD mutant. Mol. Gen. Genet. 179:1980;331-340
    • (1980) Mol. Gen. Genet. , vol.179 , pp. 331-340
    • Buxton, R.S.1    Hammer-Jespersen, K.2    Valentin-Hansen, P.3
  • 6
    • 0028803254 scopus 로고
    • 2-Chloro-2′-deoxyadenosine (cladribine) and its analogues are good substrates and potent selective inhibitors of Escherichia coli purine-nucleoside phosphorylase
    • Bzowska A., Kazimierczuk Z. 2-Chloro-2′-deoxyadenosine (cladribine) and its analogues are good substrates and potent selective inhibitors of Escherichia coli purine-nucleoside phosphorylase. Eur. J. Biochem. 233:1995;886-890
    • (1995) Eur. J. Biochem. , vol.233 , pp. 886-890
    • Bzowska, A.1    Kazimierczuk, Z.2
  • 7
    • 0025069455 scopus 로고
    • Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin
    • Bzowska A., Kulikowska E., Shugar D. Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin. Z. Naturforsch. 45c:1990;59-70
    • (1990) Z. Naturforsch. , vol.45 , pp. 59-70
    • Bzowska, A.1    Kulikowska, E.2    Shugar, D.3
  • 8
    • 0026504301 scopus 로고
    • Formycins a and B and some analogues: Selective inhibitors of bacterial Escherichia coli purine nucleoside phosphorylase
    • Bzowska A., Kulikowksa E., Shugar D. Formycins A and B and some analogues selective inhibitors of bacterial Escherichia coli purine nucleoside phosphorylase. Biochem. Biophys. Acta. 1120:1992;239-247
    • (1992) Biochem. Biophys. Acta , vol.1120 , pp. 239-247
    • Bzowska, A.1    Kulikowksa, E.2    Shugar, D.3
  • 9
    • 0027655164 scopus 로고
    • Linear free energy relationship for N(7)-substituted guanosines as substrates of calf spleen purine nucleoside phosphorylase. Possible role of N(7)-protonation as an intermediary in phosphorolysis
    • Bzowska A., Kulikowska E., Shugar D. Linear free energy relationship for N(7)-substituted guanosines as substrates of calf spleen purine nucleoside phosphorylase. Possible role of N(7)-protonation as an intermediary in phosphorolysis. Z. Naturforsch. 48c:1993;803-811
    • (1993) Z. Naturforsch. , vol.48 , pp. 803-811
    • Bzowska, A.1    Kulikowska, E.2    Shugar, D.3
  • 10
    • 0029015603 scopus 로고
    • Calf spleen purine nucleoside phosphorylase: Purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor
    • Bzowska A., Luić M., Schröder W., Shugar D., Saenger W., Koellner G. Calf spleen purine nucleoside phosphorylase purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor. FEBS Letters. 367:1995;214-218
    • (1995) FEBS Letters , vol.367 , pp. 214-218
    • Bzowska, A.1    Luić, M.2    Schröder, W.3    Shugar, D.4    Saenger, W.5    Koellner, G.6
  • 12
    • 0027992738 scopus 로고
    • Purification and characterization of extremely thermophilic thermostable 5′-methylthio-adenosine phosphorylase from the archaeon Sulfolobus solfataricus
    • Cacciapuoti G., Porcelli M., Bertoldo C., de Rosa M., Zappia V. Purification and characterization of extremely thermophilic thermostable 5′-methylthio-adenosine phosphorylase from the archaeon Sulfolobus solfataricus. J. Biol. Chem. 269:1994;24762-24769
    • (1994) J. Biol. Chem. , vol.269 , pp. 24762-24769
    • Cacciapuoti, G.1    Porcelli, M.2    Bertoldo, C.3    De Rosa, M.4    Zappia, V.5
  • 14
    • 0022366823 scopus 로고
    • Crystallization and preliminary X-ray investigation of purine nucleoside phosphorylase from Escherichia coli
    • Cook W.J., Ealick S.E., Krenitsky T.A., Stoeckler J.D., Helliwell J.R., Bugg C.E. Crystallization and preliminary X-ray investigation of purine nucleoside phosphorylase from Escherichia coli. J. Biol. Chem. 260:1985;12968-12969
    • (1985) J. Biol. Chem. , vol.260 , pp. 12968-12969
    • Cook, W.J.1    Ealick, S.E.2    Krenitsky, T.A.3    Stoeckler, J.D.4    Helliwell, J.R.5    Bugg, C.E.6
  • 16
    • 0001364731 scopus 로고
    • Specificity of purine nucleoside phosphorylase from Escherichia coli
    • Doskocil J., Holy A. Specificity of purine nucleoside phosphorylase from Escherichia coli. Collection Czechoslov. Chem. Commun. 42:1977;370-383
    • (1977) Collection Czechoslov. Chem. Commun. , vol.42 , pp. 370-383
    • Doskocil, J.1    Holy, A.2
  • 18
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graphics. 15:1997;132-134
    • (1997) J. Mol. Graphics , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 19
    • 0348050933 scopus 로고
    • Cooperative ligand binding, allosteric interactions and regulation
    • New York: W. H. Freeman and Company. chapt. 10
    • Fersht A. Cooperative ligand binding, allosteric interactions and regulation. Enzyme Structure and Mechanism. 1984;263-278 W. H. Freeman and Company, New York. chapt. 10
    • (1984) Enzyme Structure and Mechanism , pp. 263-278
    • Fersht, A.1
  • 20
    • 84919573117 scopus 로고
    • Nucleoside phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity
    • Giblett E.R., Ammann A.J., Wara D.W., Sandman R., Diamond L.K. Nucleoside phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity. Lancet. 1:1975;1010-1013
    • (1975) Lancet , vol.1 , pp. 1010-1013
    • Giblett, E.R.1    Ammann, A.J.2    Wara, D.W.3    Sandman, R.4    Diamond, L.K.5
  • 21
    • 0015217253 scopus 로고
    • Physical and catalytic properties of purine nucleoside phosphorylase from cells and spores of Bacillus cereus T
    • Gilpin R.W., Sadoff H. Physical and catalytic properties of purine nucleoside phosphorylase from cells and spores of Bacillus cereus T. J. Biol. Chem. 246:1971;1475-1480
    • (1971) J. Biol. Chem. , vol.246 , pp. 1475-1480
    • Gilpin, R.W.1    Sadoff, H.2
  • 23
    • 0031080582 scopus 로고    scopus 로고
    • Cloning and expression of nucleoside phosphorylase II gene from Bacillus stearothermophilus TH 6-2 and characterization of its gene product
    • Hamamoto T., Noguchi T., Midorikawa Y. Cloning and expression of nucleoside phosphorylase II gene from Bacillus stearothermophilus TH 6-2 and characterization of its gene product. Biosci. Biotech. Biochem. 61:1997;276-280
    • (1997) Biosci. Biotech. Biochem , vol.61 , pp. 276-280
    • Hamamoto, T.1    Noguchi, T.2    Midorikawa, Y.3
  • 24
    • 0024461035 scopus 로고
    • A new method for the enzymatic synthesis of nucleosides using purine nucleoside phosphorylase
    • Hennen W.J., Wong C.-H. A new method for the enzymatic synthesis of nucleosides using purine nucleoside phosphorylase. J. Org. Chem. 54:1989;4692-4695
    • (1989) J. Org. Chem. , vol.54 , pp. 4692-4695
    • Hennen, W.J.1    Wong, C.-H.2
  • 25
    • 0025784230 scopus 로고
    • Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol
    • Hershfield M.S., Chaffee S., Koro-Johnson L., Mary A., Smith A.A., Short S.A. Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc. Natl Acad. Sci. USA. 88:1991;7185-7189
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7185-7189
    • Hershfield, M.S.1    Chaffee, S.2    Koro-Johnson, L.3    Mary, A.4    Smith, A.A.5    Short, S.A.6
  • 26
    • 0000974868 scopus 로고
    • Purification and characterization of a second thermostable purine nucleoside phosphorylase in Bacillus stearothermophilus JTS 859
    • Hori N., Watanabe M., Yamazaki Y., Mikami Y. Purification and characterization of a second thermostable purine nucleoside phosphorylase in Bacillus stearothermophilus JTS 859. Agric. Biol. Chem. 53:1989;3219-3224
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 3219-3224
    • Hori, N.1    Watanabe, M.2    Yamazaki, Y.3    Mikami, Y.4
  • 27
    • 0029094708 scopus 로고
    • Bystander killing of melanoma cells using the human tyrosinase promoter to express the Escherichia coli purine nucleoside phosphorylase gene
    • Hughes B.W., Wells A.H., Bebok Z., Gadi V.K., Garver R.I. Jr, Parker W.B., Sorscher E.J. Bystander killing of melanoma cells using the human tyrosinase promoter to express the Escherichia coli purine nucleoside phosphorylase gene. Cancer Res. 55:1995;3339-3345
    • (1995) Cancer Res. , vol.55 , pp. 3339-3345
    • Hughes, B.W.1    Wells, A.H.2    Bebok, Z.3    Gadi, V.K.4    Garver Jr., R.I.5    Parker, W.B.6    Sorscher, E.J.7
  • 28
    • 0030039296 scopus 로고    scopus 로고
    • Promotif: A program to identify and analyze structural motifs in proteins
    • Hutchinson E.G., Thornton J.M. Promotif a program to identify and analyze structural motifs in proteins. Protein Sci. 5:1996;212-220
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 29
    • 0017892225 scopus 로고
    • Two purine nucleoside phosphorylases in Bacillus subtilis. Purification and some properties of the adenosine-specific phosphorylase
    • Jensen K.F. Two purine nucleoside phosphorylases in Bacillus subtilis. Purification and some properties of the adenosine-specific phosphorylase. Biochim. Biophys. Acta. 525:1978;346-356
    • (1978) Biochim. Biophys. Acta , vol.525 , pp. 346-356
    • Jensen, K.F.1
  • 30
    • 0017229698 scopus 로고
    • Purine nucleoside phosphorylase from Salmonella typhimurium and Escherichia coli. Initial velocity kinetics, ligand binding and reaction mechanism
    • Jensen K.J. Purine nucleoside phosphorylase from Salmonella typhimurium and Escherichia coli. Initial velocity kinetics, ligand binding and reaction mechanism. Eur. J. Biochem. 61:1976;377-386
    • (1976) Eur. J. Biochem. , vol.61 , pp. 377-386
    • Jensen, K.J.1
  • 31
    • 0016427543 scopus 로고
    • Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium
    • Jensen K.J., Nygaard P. Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Eur. J. Biochem. 51:1975;253-265
    • (1975) Eur. J. Biochem. , vol.51 , pp. 253-265
    • Jensen, K.J.1    Nygaard, P.2
  • 32
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones T.A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11:1978;268-272
    • (1978) J. Appl. Crystallog. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjieldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjieldgaard, M.4
  • 34
    • 84873792925 scopus 로고
    • The enzymatic synthesis of purine-ribosides
    • Kalckar H.M. The enzymatic synthesis of purine-ribosides. J. Biol. Chem. 167:1947;429-443
    • (1947) J. Biol. Chem. , vol.167 , pp. 429-443
    • Kalckar, H.M.1
  • 36
    • 0343765811 scopus 로고    scopus 로고
    • Binding of phosphate and sulphate anions by purine nucleoside phosphorylase from E. coli: Ligand-dependent quenching of enzyme intrinsic fluorescence
    • Kierdaszuk B., Modrak-Wojcik A., Shugar D. Binding of phosphate and sulphate anions by purine nucleoside phosphorylase from E. coli ligand-dependent quenching of enzyme intrinsic fluorescence. Biophys. Chem. 63:1997;107-118
    • (1997) Biophys. Chem. , vol.63 , pp. 107-118
    • Kierdaszuk, B.1    Modrak-Wojcik, A.2    Shugar, D.3
  • 37
    • 0014429481 scopus 로고
    • Purine nucleoside phosphorylase from human erythrocytes. Kinetic analysis and substrate-binding studies
    • Kim B.K., Cha S., Parks R.E. Jr. Purine nucleoside phosphorylase from human erythrocytes. Kinetic analysis and substrate-binding studies. J. Biol. Chem. 243:1968;1771-1776
    • (1968) J. Biol. Chem. , vol.243 , pp. 1771-1776
    • Kim, B.K.1    Cha, S.2    Parks Jr., R.E.3
  • 38
    • 0026690264 scopus 로고
    • Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity
    • Kline P.C., Schramm V.L. Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity. Biochemistry. 31:1992;5964-5973
    • (1992) Biochemistry , vol.31 , pp. 5964-5973
    • Kline, P.C.1    Schramm, V.L.2
  • 39
    • 0027729453 scopus 로고
    • Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction
    • Kline P.C., Schramm V.L. Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction. Biochemistry. 32:1993;13212-13219
    • (1993) Biochemistry , vol.32 , pp. 13212-13219
    • Kline, P.C.1    Schramm, V.L.2
  • 40
    • 0031575420 scopus 로고    scopus 로고
    • Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 Å resolution
    • Koellner G., Luić M., Shugar W., Saenger W., Bzowska A. Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 Å resolution. J. Mol. Biol. 265:1997;202-216
    • (1997) J. Mol. Biol. , vol.265 , pp. 202-216
    • Koellner, G.1    Luić, M.2    Shugar, W.3    Saenger, W.4    Bzowska, A.5
  • 41
    • 0023690299 scopus 로고
    • Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12
    • Koszalka G.W., Vanhooke J., Short S.A., Hall W.W. Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12. J. Bacteriol. 170:1988;3493-3498
    • (1988) J. Bacteriol. , vol.170 , pp. 3493-3498
    • Koszalka, G.W.1    Vanhooke, J.2    Short, S.A.3    Hall, W.W.4
  • 42
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 43
    • 0019876093 scopus 로고
    • Purine nucleoside synthesis: An efficient method employing nucleoside phosphorylases
    • Krenistky T.A., Koszalka G.W., Tuttle J.V. Purine nucleoside synthesis an efficient method employing nucleoside phosphorylases. Biochemistry. 20:1981;3615-3621
    • (1981) Biochemistry , vol.20 , pp. 3615-3621
    • Krenistky, T.A.1    Koszalka, G.W.2    Tuttle, J.V.3
  • 44
    • 0022979207 scopus 로고
    • Properties of two unusual and fluorescent substrates of purine nucleosides phosphorylase: 7-methylguanosine and 7-methylinosine
    • Kulikowska E., Bzowska A., Wierzchowski J., Shugar D. Properties of two unusual and fluorescent substrates of purine nucleosides phosphorylase 7-methylguanosine and 7-methylinosine. Biochim. Biophys. Acta. 874:1986;355-363
    • (1986) Biochim. Biophys. Acta , vol.874 , pp. 355-363
    • Kulikowska, E.1    Bzowska, A.2    Wierzchowski, J.3    Shugar, D.4
  • 45
    • 0025668822 scopus 로고
    • Purification and characterization of a novel nucleoside phosphorylase from a Klebsiella sp. and its use in the enzymatic production of adenine arabinose
    • Ling F., Inoue Y., Kimura A. Purification and characterization of a novel nucleoside phosphorylase from a Klebsiella sp. and its use in the enzymatic production of adenine arabinose. Appl. Envir. Microbiol. 56:1990;3830-3834
    • (1990) Appl. Envir. Microbiol. , vol.56 , pp. 3830-3834
    • Ling, F.1    Inoue, Y.2    Kimura, A.3
  • 46
    • 0028112373 scopus 로고
    • Induction, purification and utilization of purine nucleoside phosphorylase and uridine phosphorylase from Klebsiella sp
    • Ling F., Inoue Y., Kimura A. Induction, purification and utilization of purine nucleoside phosphorylase and uridine phosphorylase from Klebsiella sp. Proc. Biochem. 29:1994;355-361
    • (1994) Proc. Biochem. , vol.29 , pp. 355-361
    • Ling, F.1    Inoue, Y.2    Kimura, A.3
  • 47
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la détermination des structures cristallines. Acta. Crystallog. 5:1952;802-810
    • (1952) Acta. Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 48
    • 0031572855 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli purine nucleoside phosphorylase: A comparison with the human reveals a conserved topology
    • Mao C., Cook W.J., Zhou M., Koszalka G.W., Krenitsky T.A., Ealick S.E. Crystal structure of Escherichia coli purine nucleoside phosphorylase a comparison with the human reveals a conserved topology. Structure. 5:1997;1373-1383
    • (1997) Structure , vol.5 , pp. 1373-1383
    • Mao, C.1    Cook, W.J.2    Zhou, M.3    Koszalka, G.W.4    Krenitsky, T.A.5    Ealick, S.E.6
  • 50
    • 0030887917 scopus 로고    scopus 로고
    • Refined structure of purine nucleoside phosphorylase at 2.75 Å resolution
    • Narayana S.V.L., Bugg C.E., Ealick S.E. Refined structure of purine nucleoside phosphorylase at 2.75 Å resolution. Acta Crystallog. sect. D. 53:1997;131-142
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 131-142
    • Narayana, S.V.L.1    Bugg, C.E.2    Ealick, S.E.3
  • 51
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navazza J. AMoRe an automated package for molecular replacement. Acta. Crystallog. sect. B. 50:1994;157-163
    • (1994) Acta. Crystallog. Sect. B , vol.50 , pp. 157-163
    • Navazza, J.1
  • 54
    • 0015935354 scopus 로고
    • Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium
    • Robertson B.C., Hoffee P.A. Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium. J. Biol. Chem. 248:1973;2040-2043
    • (1973) J. Biol. Chem. , vol.248 , pp. 2040-2043
    • Robertson, B.C.1    Hoffee, P.A.2
  • 55
    • 0025823991 scopus 로고
    • Purine nucleoside phosphorylase. Allosteric regulation of a dissociating enzyme
    • Ropp P.A., Traut Th.W. Purine nucleoside phosphorylase. Allosteric regulation of a dissociating enzyme. J. Biol. Chem. 266:1991;7682-7687
    • (1991) J. Biol. Chem. , vol.266 , pp. 7682-7687
    • Ropp, P.A.1    Traut, Th.W.2
  • 56
    • 0025895545 scopus 로고
    • Allosteric regulation of purine nucleoside phosphorylase
    • Ropp P.A., Traut Th.W. Allosteric regulation of purine nucleoside phosphorylase. Arch. Biochem. Biophys. 288:1991;614-620
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 614-620
    • Ropp, P.A.1    Traut, Th.W.2
  • 57
    • 0003458038 scopus 로고
    • C.E. Cantor. New York, Berlin, Heidelberg, Tokyo: Springer Verlag
    • Saenger W. Cantor C.E. Principles of Nucleic Acids Structure. 1984;107-110 Springer Verlag, New York, Berlin, Heidelberg, Tokyo
    • (1984) Principles of Nucleic Acids Structure , pp. 107-110
    • Saenger, W.1
  • 60
    • 0014286887 scopus 로고
    • Purine nucleoside phosphorylase from human erythrocytes III. Inhibition by the inosine analogue formycin B of the isolated enzyme and of nucleoside metabolism in intact erythrocytes and sarcoma 180 cells
    • Sheen M.R., Kim B.K., Parks R.E. Jr. Purine nucleoside phosphorylase from human erythrocytes III. Inhibition by the inosine analogue formycin B of the isolated enzyme and of nucleoside metabolism in intact erythrocytes and sarcoma 180 cells. Mol. Pharmacol. 4:1968;293-302
    • (1968) Mol. Pharmacol. , vol.4 , pp. 293-302
    • Sheen, M.R.1    Kim, B.K.2    Parks Jr., R.E.3
  • 61
    • 0026184268 scopus 로고
    • Purifications and properties of orotidine-phosphorylyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992
    • Shirae H., Yokozeki K. Purifications and properties of orotidine-phosphorylyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992. Agric. Biol. Chem. 55:1991;1849-1857
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1849-1857
    • Shirae, H.1    Yokozeki, K.2
  • 62
    • 0028264426 scopus 로고
    • Cladribine in treatment of chronic progressive multiple sclerosis
    • Sipe J.C., Romine J.S., Koziol J.A., McMillian R., Beutler E. Cladribine in treatment of chronic progressive multiple sclerosis. Lancet. 344:1994;9-13
    • (1994) Lancet , vol.344 , pp. 9-13
    • Sipe, J.C.1    Romine, J.S.2    Koziol, J.A.3    McMillian, R.4    Beutler, E.5
  • 63
    • 0028465423 scopus 로고
    • Tumor cell bystander killing in colonic carcinoma utilizing the Eschrichia coli DeoD gene to generate toxic purines
    • Sorscher E.J., Peng S., Bebok Z., Allan P.W., Bennett L.L. Jr, Parker W.B. Tumor cell bystander killing in colonic carcinoma utilizing the Eschrichia coli DeoD gene to generate toxic purines. Gene Ther. 1:1994;233-238
    • (1994) Gene Ther. , vol.1 , pp. 233-238
    • Sorscher, E.J.1    Peng, S.2    Bebok, Z.3    Allan, P.W.4    Bennett Jr., L.L.5    Parker, W.B.6
  • 64
    • 0025879501 scopus 로고
    • In a Staphyloccocal nuclease mutant the side-chain of lysine replacing Val66 is fully buried in the hydrophobic core
    • Stites W.E., Gitts A.G., Lattman E.E., Shortle D. In a Staphyloccocal nuclease mutant the side-chain of lysine replacing Val66 is fully buried in the hydrophobic core. J. Mol. Biol. 221:1991;7-14
    • (1991) J. Mol. Biol. , vol.221 , pp. 7-14
    • Stites, W.E.1    Gitts, A.G.2    Lattman, E.E.3    Shortle, D.4
  • 65
    • 0001157528 scopus 로고
    • Purine nucleoside phosphorylase: A target for chemotherapy
    • R.I. Glazer. Boca Raton, USA, FL: CRC Press Inc
    • Stoeckler J.D. Purine nucleoside phosphorylase a target for chemotherapy. Glazer R.I. Developments in Cancer Chemotherapy. 1984;35-60 CRC Press Inc, Boca Raton, USA, FL
    • (1984) Developments in Cancer Chemotherapy , pp. 35-60
    • Stoeckler, J.D.1
  • 66
    • 0018100276 scopus 로고
    • Purine nucleoside phosphorylase from human erythrocytes: Physicochemical properties of the crystalline enzyme
    • Stoeckler J.D., Agarwal R.P., Agarwal K.C., Schmid K., Parks R.E. Jr. Purine nucleoside phosphorylase from human erythrocytes physicochemical properties of the crystalline enzyme. Biochemistry. 17:1978;278-283
    • (1978) Biochemistry , vol.17 , pp. 278-283
    • Stoeckler, J.D.1    Agarwal, R.P.2    Agarwal, K.C.3    Schmid, K.4    Parks Jr., R.E.5
  • 68
    • 0019203755 scopus 로고
    • Purine nucleoside phosphorylase inhibitors as potential chemotherapeutic and immunosuppressive agents
    • Stoeckler J.D., Cambor C., Burgess F.W., Erban S.B., Parks R.E. Jr. Purine nucleoside phosphorylase inhibitors as potential chemotherapeutic and immunosuppressive agents. Pharmacologist. 22:1980;99-105
    • (1980) Pharmacologist , vol.22 , pp. 99-105
    • Stoeckler, J.D.1    Cambor, C.2    Burgess, F.W.3    Erban, S.B.4    Parks Jr., R.E.5
  • 69
    • 0018879146 scopus 로고
    • Human erythrocytic purine nucleoside phosphorylase: Reaction with sugar-modified nucleoside substrates
    • Stoeckler J.D., Cambor C., Parks R.E. Jr. Human erythrocytic purine nucleoside phosphorylase reaction with sugar-modified nucleoside substrates. Biochemistry. 19:1980;102-107
    • (1980) Biochemistry , vol.19 , pp. 102-107
    • Stoeckler, J.D.1    Cambor, C.2    Parks Jr., R.E.3
  • 71
    • 0025423593 scopus 로고
    • Purification and characterization of purine nucleoside phsophorylase from Proteus vulgaris
    • Surette M., Gill T., MacLean S. Purification and characterization of purine nucleoside phsophorylase from Proteus vulgaris. Appl. Envir. Microbiol. 56:1990;1435-1439
    • (1990) Appl. Envir. Microbiol. , vol.56 , pp. 1435-1439
    • Surette, M.1    Gill, T.2    MacLean, S.3
  • 72
    • 0029384078 scopus 로고
    • Molecular cloning und nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp
    • Takehara M., Ling F., Izawa S., Inoue Y., Kimura A. Molecular cloning und nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp. Biosci. Biotech. Biochem. 59:1995;1987-1990
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 1987-1990
    • Takehara, M.1    Ling, F.2    Izawa, S.3    Inoue, Y.4    Kimura, A.5
  • 73
    • 0009684747 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylase (PNP) from Cellulomonas sp., a third class of PNP different from both 'low-molecular weight' mammalian and 'high-molecular weight' bacterial PNPs
    • Tebbe J., Wielgus-Kutrowska B., Schröder W., Luić M., Shugar D., Saenger W., Koellner G., Bzowska A. Purine nucleoside phosphorylase (PNP) from Cellulomonas sp., a third class of PNP different from both 'low-molecular weight' mammalian and 'high-molecular weight' bacterial PNPs. Protein Eng. 10:(Suppl.):1997;90
    • (1997) Protein Eng. , vol.10 , Issue.SUPPL. , pp. 90
    • Tebbe, J.1    Wielgus-Kutrowska, B.2    Schröder, W.3    Luić, M.4    Shugar, D.5    Saenger, W.6    Koellner, G.7    Bzowska, A.8
  • 74
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud D.E., Ten EyckL.F., Matthews B.W. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A. 43:1987;489-501
    • (1987) Acta Crystallog. Sect. a , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten, EyckL.F.2    Matthews, B.W.3
  • 76
    • 0028876808 scopus 로고
    • Coincidences, decarboxylation and electrostatic effects
    • Westheimer F.H. Coincidences, decarboxylation and electrostatic effects. Tetrahedron. 51:1995;3-30
    • (1995) Tetrahedron , vol.51 , pp. 3-30
    • Westheimer, F.H.1
  • 79
    • 0020030603 scopus 로고
    • Luminisence studies of formycin, its aglycone, and their N-methyl derivatives: Tautomerismn, sites of protonation and phototautomerismn
    • Wierzchowski J., Shugar D. Luminisence studies of formycin, its aglycone, and their N-methyl derivatives tautomerismn, sites of protonation and phototautomerismn. Photochem. Photobiol. 35:1982;445-458
    • (1982) Photochem. Photobiol. , vol.35 , pp. 445-458
    • Wierzchowski, J.1    Shugar, D.2
  • 80
    • 0021770772 scopus 로고
    • Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization
    • Williams S.R., Goddard J.M., Martin D.W. Jr. Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucl. Acids Res. 12:1984;5779-5787
    • (1984) Nucl. Acids Res. , vol.12 , pp. 5779-5787
    • Williams, S.R.1    Goddard, J.M.2    Martin Jr., D.W.3
  • 81
    • 0014961477 scopus 로고
    • Kinetics and mechanism of the acid catalysed hydrolysis of some purine nucleosides
    • Zoltewicz J.A., Clark D.F., Sharpless T.W., Grahe G. Kinetics and mechanism of the acid catalysed hydrolysis of some purine nucleosides. J. Am. Chem. Soc. 92:1970;1741-1750
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 1741-1750
    • Zoltewicz, J.A.1    Clark, D.F.2    Sharpless, T.W.3    Grahe, G.4


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