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Volumn 44, Issue 32, 2005, Pages 10854-10863

Substrate discrimination by the human GTP fucose pyrophosphorylase

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CATALYSIS; CONDENSATION; LIPIDS; PROTONS; SALVAGING; SUBSTRATES;

EID: 23844527829     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0503605     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker, D. J., and Lowe, J. B. (2003) Fucose: Biosynthesis and biological function in mammals, Glycobiology 13, 41R-53R.
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 2
    • 0025572708 scopus 로고
    • Recognition by ELAM-1 of the sialyl-Lex determinant on myeloid and tumor cells
    • Walz, G., Aruffo, A., Kolanus, W., Bevilacqua, M., and Seed, B. (1990) Recognition by ELAM-1 of the sialyl-Lex determinant on myeloid and tumor cells, Science 250, 1132-1135.
    • (1990) Science , vol.250 , pp. 1132-1135
    • Walz, G.1    Aruffo, A.2    Kolanus, W.3    Bevilacqua, M.4    Seed, B.5
  • 4
    • 0021710314 scopus 로고
    • A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryos, while the free oligosaccharide is ineffective
    • Fenderson, B. A., Zehavi, U., and Hakomori, S. (1984) A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryos, while the free oligosaccharide is ineffective, J. Exp. Med. 160, 1591-1596.
    • (1984) J. Exp. Med. , vol.160 , pp. 1591-1596
    • Fenderson, B.A.1    Zehavi, U.2    Hakomori, S.3
  • 5
    • 0026077444 scopus 로고
    • Structures of mucin-type sugar chains of the galactosyltransferase purified from human milk. Occurrence of the ABO and Lewis blood group determinants
    • Amano, J., Straehl, P., Berger, E. G., Kochibe, N., and Kobata, A. (1991) Structures of mucin-type sugar chains of the galactosyltransferase purified from human milk. Occurrence of the ABO and Lewis blood group determinants, J. Biol. Chem. 266, 11461-11477.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11461-11477
    • Amano, J.1    Straehl, P.2    Berger, E.G.3    Kochibe, N.4    Kobata, A.5
  • 6
    • 0036182235 scopus 로고    scopus 로고
    • Effect of increased concentration of D-glucose or L-fucose on monocyte adhesion to endothelial cell monolayers and activation of nuclear factor-κB
    • Yorek, M. A., and Dunlap, J. A. (2002) Effect of increased concentration of D-glucose or L-fucose on monocyte adhesion to endothelial cell monolayers and activation of nuclear factor-κB, Metabolism 51, 225-234.
    • (2002) Metabolism , vol.51 , pp. 225-234
    • Yorek, M.A.1    Dunlap, J.A.2
  • 7
    • 0034806401 scopus 로고    scopus 로고
    • Identification and characterization of GDP-D-mannose 4,6-dehydratase and GDP-L-fucose snthetase in a GDP-L-fucose biosynthetic gene cluster from Helicobacter pylori, Biochem
    • Wu, B., Zhang, Y., and Wang, P. G. (2001) Identification and characterization of GDP-D-mannose 4,6-dehydratase and GDP-L-fucose snthetase in a GDP-L-fucose biosynthetic gene cluster from Helicobacter pylori, Biochem. Biophys. Res. Commun. 285, 364-371.
    • (2001) Biophys. Res. Commun. , vol.285 , pp. 364-371
    • Wu, B.1    Zhang, Y.2    Wang, P.G.3
  • 8
    • 0033023153 scopus 로고    scopus 로고
    • Decreased availability of GDP-L-fucose in a patient with LAD II with normal GDP-D-mannose dehydratase and FX protein activities
    • Korner, C., Linnebank, M., Koch, H. G., Harms, E., von Figura, K., and Marquardt, T. (1999) Decreased availability of GDP-L-fucose in a patient with LAD II with normal GDP-D-mannose dehydratase and FX protein activities, J. Leukocyte Biol. 66, 95-98.
    • (1999) J. Leukocyte Biol. , vol.66 , pp. 95-98
    • Korner, C.1    Linnebank, M.2    Koch, H.G.3    Harms, E.4    Von Figura, K.5    Marquardt, T.6
  • 9
    • 0023036963 scopus 로고
    • Impairment of glycoprotein fucosylation in rat hippocampus and the consequences on memory formation
    • Jork, R., Grecksch, G., and Matthies, H. (1986) Impairment of glycoprotein fucosylation in rat hippocampus and the consequences on memory formation, Pharmacol. Biochem. Behav. 25, 1137-1144.
    • (1986) Pharmacol. Biochem. Behav. , vol.25 , pp. 1137-1144
    • Jork, R.1    Grecksch, G.2    Matthies, H.3
  • 10
    • 0026794747 scopus 로고
    • The maintenance of hippocampal long-term potentiation is paralleled by a dopamine-dependent increase in glycoprotein fucosylation
    • Angenstein, F., Matthies, H., Jr., Staeck, S., Reymann, K. G., and Staak, S. (1992) The maintenance of hippocampal long-term potentiation is paralleled by a dopamine-dependent increase in glycoprotein fucosylation, Neurochem. Int. 21, 403-408.
    • (1992) Neurochem. Int. , vol.21 , pp. 403-408
    • Angenstein, F.1    Matthies Jr., H.2    Staeck, S.3    Reymann, K.G.4    Staak, S.5
  • 11
    • 0021764439 scopus 로고
    • Study of the conversion of GDP-mannose into GDP-fucose in Nereids: A biochemical marker of oocyte maturation
    • Bulet, P., Hoflack, B., Porchet, M., and Verbert, A. (1984) Study of the conversion of GDP-mannose into GDP-fucose in Nereids: A biochemical marker of oocyte maturation, Eur. J. Biochem. 144, 255-259.
    • (1984) Eur. J. Biochem. , vol.144 , pp. 255-259
    • Bulet, P.1    Hoflack, B.2    Porchet, M.3    Verbert, A.4
  • 12
    • 0001262567 scopus 로고    scopus 로고
    • Purification to apparent homogeneity and properties of pig kidney L-fucose kinase
    • Park, S. H., Pastuszak, I., Drake, R., and Elbein, A. D. (1998) Purification to apparent homogeneity and properties of pig kidney L-fucose kinase, J. Biol. Chem. 273, 5685-5691.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5685-5691
    • Park, S.H.1    Pastuszak, I.2    Drake, R.3    Elbein, A.D.4
  • 14
    • 0032514911 scopus 로고    scopus 로고
    • GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme
    • Pastuszak, I., Ketchum, C., Hermanson, G., Sjoberg, E. J., Drake, R., and Elbein, A. D. (1998) GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme, J. Biol. Chem. 273, 30165-30174.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30165-30174
    • Pastuszak, I.1    Ketchum, C.2    Hermanson, G.3    Sjoberg, E.J.4    Drake, R.5    Elbein, A.D.6
  • 15
    • 0035798395 scopus 로고    scopus 로고
    • Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase
    • Zuccotti, S., Zanardi, D., Rosano, C., Sturla, L., Tonetti, M., and Bolognesi, M. (2001) Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase, J. Mol. Biol. 313, 831-843.
    • (2001) J. Mol. Biol. , vol.313 , pp. 831-843
    • Zuccotti, S.1    Zanardi, D.2    Rosano, C.3    Sturla, L.4    Tonetti, M.5    Bolognesi, M.6
  • 16
    • 0034642186 scopus 로고    scopus 로고
    • The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases
    • Campbell, R. E., Mosimann, S. C., Tanner, M. E., and Strynadka, N. C. (2000) The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases, Biochemistry 39, 14993-15001.
    • (2000) Biochemistry , vol.39 , pp. 14993-15001
    • Campbell, R.E.1    Mosimann, S.C.2    Tanner, M.E.3    Strynadka, N.C.4
  • 17
    • 0031019959 scopus 로고    scopus 로고
    • Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase completed with either UDP-glucose or UDP-galactose: Detailed description of the nucleotide sugar binding site
    • Thoden, J. B., Ruzicka, F. J., Frey, P. A., Rayment, I., and Holden, H. M. (1997) Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase completed with either UDP-glucose or UDP-galactose: Detailed description of the nucleotide sugar binding site, Biochemistry 36, 1212-1222.
    • (1997) Biochemistry , vol.36 , pp. 1212-1222
    • Thoden, J.B.1    Ruzicka, F.J.2    Frey, P.A.3    Rayment, I.4    Holden, H.M.5
  • 19
    • 0037178867 scopus 로고    scopus 로고
    • Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks
    • Thoden, J. B., Henderson, J. M., Fridovich-Keil, J. L., and Holden, H. M. (2002) Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks, J. Biol. Chem. 277, 27528-27534.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27528-27534
    • Thoden, J.B.1    Henderson, J.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 20
    • 0034643813 scopus 로고    scopus 로고
    • The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation
    • Campbell, R. E., Mosimann, S. C., van De Rijn, I., Tanner, M. E., and Strynadka, N. C. (2000) The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation, Biochemistry 39, 7012-7023.
    • (2000) Biochemistry , vol.39 , pp. 7012-7023
    • Campbell, R.E.1    Mosimann, S.C.2    Van De Rijn, I.3    Tanner, M.E.4    Strynadka, N.C.5
  • 21
    • 0034644773 scopus 로고    scopus 로고
    • Probing the catalytic mechanism of GDP-4-keto-6-deoxy-D-mannose epimerase/reductase by kinetic and crystallographic characterization of site-specific mutants
    • Rosano, C., Bisso, A., Izzo, O., Tonetti, M., Sturla, L., De Flora, A., and Bolognesi, M. (2000) Probing the catalytic mechanism of GDP-4-keto-6-deoxy- D-mannose epimerase/reductase by kinetic and crystallographic characterization of site-specific mutants, J. Mol. Biol. 303, 77-91.
    • (2000) J. Mol. Biol. , vol.303 , pp. 77-91
    • Rosano, C.1    Bisso, A.2    Izzo, O.3    Tonetti, M.4    Sturla, L.5    De Flora, A.6    Bolognesi, M.7
  • 22
    • 0034651725 scopus 로고    scopus 로고
    • Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6-dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose
    • Somoza, J. R., Menon, S., Schmidt, H., Joseph-McCarthy, D., Dessen, A., Stahl, M. L., Somers, W. S., and Sullivan, F. X. (2000) Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6-dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose. Structure Fold Des. 8, 123-135.
    • (2000) Structure Fold Des. , vol.8 , pp. 123-135
    • Somoza, J.R.1    Menon, S.2    Schmidt, H.3    Joseph-McCarthy, D.4    Dessen, A.5    Stahl, M.L.6    Somers, W.S.7    Sullivan, F.X.8
  • 23
    • 84982010034 scopus 로고
    • Exploring the active site in UDP-glucose pyrophosphorylase by affinity labelling and site-directed mutagenesis
    • Fukui, T., Kazuta, Y., Katsube, T., Tagaya, M., and Tanizawa, K. (1993) Exploring the active site in UDP-glucose pyrophosphorylase by affinity labelling and site-directed mutagenesis, Biotechnol. Appl. Biochem. 18 (part 2), 209-216.
    • (1993) Biotechnol. Appl. Biochem. , vol.18 , Issue.PART 2 , pp. 209-216
    • Fukui, T.1    Kazuta, Y.2    Katsube, T.3    Tagaya, M.4    Tanizawa, K.5
  • 25
    • 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
  • 26
    • 0037123422 scopus 로고    scopus 로고
    • "Fleximers". Design and synthesis of a new class of novel shape-modified nucleosides
    • Seley, K. L., Zhang, L., Hagos, A., and Quirk, S. (2002) "Fleximers". Design and synthesis of a new class of novel shape-modified nucleosides, J. Org. Chem. 67, 3365-3373.
    • (2002) J. Org. Chem. , vol.67 , pp. 3365-3373
    • Seley, K.L.1    Zhang, L.2    Hagos, A.3    Quirk, S.4
  • 27
    • 0038101536 scopus 로고    scopus 로고
    • Unexpected inhibition of S-adenosyl-L-homocysteine hydrolase by a guanosine nucleoside
    • Seley, K. L., Quirk, S., Salim, S., Zhang, L., and Hagos, A. (2003) Unexpected inhibition of S-adenosyl-L-homocysteine hydrolase by a guanosine nucleoside, Bioorg. Med. Chem. Lett. 13, 1985-1988.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 1985-1988
    • Seley, K.L.1    Quirk, S.2    Salim, S.3    Zhang, L.4    Hagos, A.5
  • 28
    • 0037180395 scopus 로고    scopus 로고
    • Synthesis of nucleotide analogues that potently and selectively inhibit human DNA primase
    • Moore, C. L., Chiaramonte, M., Higgins, T., and Kuchta, R. D. (2002) Synthesis of nucleotide analogues that potently and selectively inhibit human DNA primase, Biochemistry 41, 14066-14075.
    • (2002) Biochemistry , vol.41 , pp. 14066-14075
    • Moore, C.L.1    Chiaramonte, M.2    Higgins, T.3    Kuchta, R.D.4
  • 29
    • 0033689049 scopus 로고    scopus 로고
    • Syntheses of nucleoside triphosphates
    • Burgess, K., and Cook, D. (2000) Syntheses of nucleoside triphosphates, Chem. Rev. 100, 2047-2060.
    • (2000) Chem. Rev. , vol.100 , pp. 2047-2060
    • Burgess, K.1    Cook, D.2
  • 32
    • 0031860314 scopus 로고    scopus 로고
    • Occurrence of reducing terminal N-acetylglucosamine 3-sulfate and fucosylated outer chains in acidic N-glycans of porcine zona pellucida glycoproteins
    • Mori, E., Hedrick, J. L., Wardrip, N. J., Mori, T., and Takasaki, S. (1998) Occurrence of reducing terminal N-acetylglucosamine 3-sulfate and fucosylated outer chains in acidic N-glycans of porcine zona pellucida glycoproteins, Glycoconjate J. 15, 447-456.
    • (1998) Glycoconjate J. , vol.15 , pp. 447-456
    • Mori, E.1    Hedrick, J.L.2    Wardrip, N.J.3    Mori, T.4    Takasaki, S.5
  • 33
    • 0027338125 scopus 로고
    • Le(y) antigen expression is correlated with apoptosis (programmed cell death)
    • Hiraishi, K., Suzuki, K., Hakomori, S., and Adachi, M. (1993) Le(y) antigen expression is correlated with apoptosis (programmed cell death), Glycobiology 3, 381-390.
    • (1993) Glycobiology , vol.3 , pp. 381-390
    • Hiraishi, K.1    Suzuki, K.2    Hakomori, S.3    Adachi, M.4
  • 35
    • 0037363278 scopus 로고    scopus 로고
    • Characterization of the ugpG gene encoding a UDP-glucose pyrophosphorylase from the gellan gum producer Sphingomonas paucimobilis ATCC 31461
    • Marques, A. R., Ferreira, P. B., Sa-Correia, I., and Fialho, A. M. (2003) Characterization of the ugpG gene encoding a UDP-glucose pyrophosphorylase from the gellan gum producer Sphingomonas paucimobilis ATCC 31461, Mol. Genet. Genomics 268, 816-824.
    • (2003) Mol. Genet. Genomics , vol.268 , pp. 816-824
    • Marques, A.R.1    Ferreira, P.B.2    Sa-Correia, I.3    Fialho, A.M.4
  • 36
    • 0038653402 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis, Microbiol
    • table of contents
    • Ballicora, M. A., Iglesias, A. A., and Preiss, J. (2003) ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis, Microbiol. Mol. Biol. Rev. 67, 213-225, table of contents.
    • (2003) Mol. Biol. Rev. , vol.67 , pp. 213-225
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 37
    • 0034713876 scopus 로고    scopus 로고
    • GDP-mannose mannosyl hydrolase catalyzes nucleophilic substitution at carbon, unlike all other Nudix hydrolases
    • Legler, P. M., Massiah, M. A., Bessman, M. J., and Mildvan, A. S. (2000) GDP-mannose mannosyl hydrolase catalyzes nucleophilic substitution at carbon, unlike all other Nudix hydrolases, Biochemistry 39, 8603-8608.
    • (2000) Biochemistry , vol.39 , pp. 8603-8608
    • Legler, P.M.1    Massiah, M.A.2    Bessman, M.J.3    Mildvan, A.S.4
  • 38
    • 0017769609 scopus 로고
    • Equilibration of fucosyl glycoprotein pools in HeLa cells
    • Yurchenco, P. D., and Atkinson, P. H. (1977) Equilibration of fucosyl glycoprotein pools in HeLa cells, Biochemistry 16, 944-953.
    • (1977) Biochemistry , vol.16 , pp. 944-953
    • Yurchenco, P.D.1    Atkinson, P.H.2
  • 39
    • 1642458114 scopus 로고    scopus 로고
    • Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose
    • Niittymaki, J., Mattila, P., Roos, C., Huopaniemi, L., Sjoblom, S., and Renkonen, R. (2004) Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose, Eur. J. Biochem. 271, 78-86.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 78-86
    • Niittymaki, J.1    Mattila, P.2    Roos, C.3    Huopaniemi, L.4    Sjoblom, S.5    Renkonen, R.6
  • 40
    • 0031023919 scopus 로고    scopus 로고
    • Cloning, purification, and characterization of the Shigella boydii dGTP triphosphohydrolase
    • Quirk, S., and Do, B. T. (1997) Cloning, purification, and characterization of the Shigella boydii dGTP triphosphohydrolase, J. Biol. Chem. 272, 332-336.
    • (1997) J. Biol. Chem. , vol.272 , pp. 332-336
    • Quirk, S.1    Do, B.T.2
  • 41
    • 0037407940 scopus 로고    scopus 로고
    • Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing
    • Burton, R. E., Baker, T. A., and Sauer, R. T. (2003) Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing, Protein Sci. 12, 893-902.
    • (2003) Protein Sci. , vol.12 , pp. 893-902
    • Burton, R.E.1    Baker, T.A.2    Sauer, R.T.3
  • 42
    • 0032705126 scopus 로고    scopus 로고
    • Nucleotide binding to creatine kinase: An isothermal titration microcalorimetry study
    • Forstner, M., Berger, C., and Wallimann, T. (1999) Nucleotide binding to creatine kinase: An isothermal titration microcalorimetry study, FEBS Lett. 461, 111-114.
    • (1999) FEBS Lett. , vol.461 , pp. 111-114
    • Forstner, M.1    Berger, C.2    Wallimann, T.3
  • 43
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant, J. M. (1977) Heat capacity and entropy changes in processes involving proteins, Proc. Natl. Acad. Sci. U.S.A. 74, 2236-2240.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 44
    • 0032874671 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to NBS-I of the Bacillus subtilis preprotein translocase subunit SecA
    • den Blaauwen, T., van der Wolk, J. P., van der Does, C., van Wely, K. H., and Driessen, A. J. (1999) Thermodynamics of nucleotide binding to NBS-I of the Bacillus subtilis preprotein translocase subunit SecA, FEBS Lett. 458, 145-150.
    • (1999) FEBS Lett. , vol.458 , pp. 145-150
    • Den Blaauwen, T.1    Van Der Wolk, J.P.2    Van Der Does, C.3    Van Wely, K.H.4    Driessen, A.J.5


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