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Volumn 9, Issue 8, 1999, Pages 815-822

Role of a conserved acidic cluster in bovine β1,4 galactosyltransferase-1 probed by mutagenesis of a bacterially expressed recombinant enzyme

Author keywords

1,4 Galactosyltransferase; Expression in E. coli; Mutagenesis; Reaction mechanism

Indexed keywords

GALACTOSYLTRANSFERASE; MUTANT PROTEIN; RECOMBINANT ENZYME;

EID: 0032766699     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/9.8.815     Document Type: Article
Times cited : (19)

References (54)
  • 1
    • 0344706380 scopus 로고    scopus 로고
    • A family of human β4-galactosyltransferases: Cloning and expression of two novel UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferases, β4Gal-T2 and β4Gal-T3
    • Almeida, R., Amado, M., David, L., Levery, S.B., Holmes, E.H., Merkx, G., Kessek, A.G.V., Rygaard, E., Hassan, H., Bennett, E. and Clausen, H. (1997) A family of human β4-galactosyltransferases: cloning and expression of two novel UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferases, β4Gal-T2 and β4Gal-T3. J. Biol Chem., 272, 31979-31991.
    • (1997) J. Biol Chem. , vol.272 , pp. 31979-31991
    • Almeida, R.1    Amado, M.2    David, L.3    Levery, S.B.4    Holmes, E.H.5    Merkx, G.6    Kessek, A.G.V.7    Rygaard, E.8    Hassan, H.9    Bennett, E.10    Clausen, H.11
  • 3
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M.A., Chacon, P., Merelo, J.J. and Moran, F. (1993) Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng., 6, 383-390.
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 4
    • 0025171662 scopus 로고
    • Analysis of the substrate binding sites of human galactosyltransferase by protein engineering
    • Aoki, D., Appert, H.E., Johnson, D., Wong, S.S. and Fukuda, M.N. (1990) Analysis of the substrate binding sites of human galactosyltransferase by protein engineering. EMBO J., 9, 3171-3178.
    • (1990) EMBO J. , vol.9 , pp. 3171-3178
    • Aoki, D.1    Appert, H.E.2    Johnson, D.3    Wong, S.S.4    Fukuda, M.N.5
  • 6
    • 0027942505 scopus 로고
    • A Lymnaeu stagnalis gene, with sequence similarity to that of mammalian β1→4-galactosyltransferases, encodes a novel UDP-GlcNAc:GlcNAcβ-R β1→4-N-acetylglucosaminyltransferase
    • Bakker, H., Agterberg, M., Van Tetering, A., Koeleman, C.A.M., Van den Eijnden, D.H. and Van Die, I. (1994) A Lymnaeu stagnalis gene, with sequence similarity to that of mammalian β1→4-galactosyltransferases, encodes a novel UDP-GlcNAc:GlcNAcβ-R β1→4-N-acetylglucosaminyltransferase. J. Biol. Chem., 269, 30326-30333.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30326-30333
    • Bakker, H.1    Agterberg, M.2    Van Tetering, A.3    Koeleman, C.A.M.4    Van Den Eijnden, D.H.5    Van Die, I.6
  • 7
    • 0024281351 scopus 로고
    • Temporally specific involvement of cell surface β-1,4 galactosyltransferase during mouse embro morula compaction
    • Bayna, E.M., Shaper, J.H. and Shur, B.D. (1988) Temporally specific involvement of cell surface β-1,4 galactosyltransferase during mouse embro morula compaction. Cell, 53, 145-157.
    • (1988) Cell , vol.53 , pp. 145-157
    • Bayna, E.M.1    Shaper, J.H.2    Shur, B.D.3
  • 8
    • 0027522253 scopus 로고
    • Expression of deletion constructs of bovine β-1,4-galactosyltransferase in Escherichia coli: Importance of Cys134 for its activity
    • Boeggeman, E.E., Balaji, P.V., Sethi, N., Masibay, A.S. and Qasba, P.K. (1993) Expression of deletion constructs of bovine β-1,4-galactosyltransferase in Escherichia coli: importance of Cys134 for its activity. Protein Eng., 6, 779-785.
    • (1993) Protein Eng. , vol.6 , pp. 779-785
    • Boeggeman, E.E.1    Balaji, P.V.2    Sethi, N.3    Masibay, A.S.4    Qasba, P.K.5
  • 9
    • 0031749203 scopus 로고    scopus 로고
    • Sequence-function relationships of prokaryotic and eukaryotic galactosyltransferases
    • Breton, C., Bettler, E., Joziasse, D.H., Geremia, R.A. and Imberty, A. (1998) Sequence-function relationships of prokaryotic and eukaryotic galactosyltransferases. J. Biochem., 123, 1000-1009.
    • (1998) J. Biochem. , vol.123 , pp. 1000-1009
    • Breton, C.1    Bettler, E.2    Joziasse, D.H.3    Geremia, R.A.4    Imberty, A.5
  • 10
    • 0014251737 scopus 로고
    • The role of α-lactalbumin and the A protein in lactose synthesis: A unique mechanism for the control of a biological reaction
    • Brew, K., Vanaman, T.C. and Hill, R.L. (1968) The role of α-lactalbumin and the A protein in lactose synthesis: a unique mechanism for the control of a biological reaction. Proc. Natl. Acad. Sci., USA, 59, 491-497.
    • (1968) Proc. Natl. Acad. Sci., USA , vol.59 , pp. 491-497
    • Brew, K.1    Vanaman, T.C.2    Hill, R.L.3
  • 11
    • 0015935205 scopus 로고
    • The charge relay system in chymotrypsin and chymotrypsinogen
    • Fersht, A.R. and Sperling, J. (1973) The charge relay system in chymotrypsin and chymotrypsinogen. J. Mol. Biol., 74, 137-149
    • (1973) J. Mol. Biol. , vol.74 , pp. 137-149
    • Fersht, A.R.1    Sperling, J.2
  • 12
    • 0016790384 scopus 로고
    • Circular diochroism changes in galactosyltransferase upon substrate binding
    • Geren, C.R., Magee, S.C. and Ebner, K.E. (1975) Circular diochroism changes in galactosyltransferase upon substrate binding. Biochemistry, 14, 1461-1463.
    • (1975) Biochemistry , vol.14 , pp. 1461-1463
    • Geren, C.R.1    Magee, S.C.2    Ebner, K.E.3
  • 13
    • 0028148991 scopus 로고
    • Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipooligosaccharide
    • Gotschlich, E.C. (1994) Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipooligosaccharide. J. Exp. Med., 180, 2181-2190.
    • (1994) J. Exp. Med. , vol.180 , pp. 2181-2190
    • Gotschlich, E.C.1
  • 14
    • 0028095491 scopus 로고
    • Study by mutagenesis of the role of two aromatic clusters of α-lactalbumin in aspects of its action in the lactose synthase system
    • Grobler, J.A., Wang, M., Pike, A.C.W. and Brew, K. (1994) Study by mutagenesis of the role of two aromatic clusters of α-lactalbumin in aspects of its action in the lactose synthase system. J. Biol. Chem., 269, 5106-5114.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5106-5114
    • Grobler, J.A.1    Wang, M.2    Pike, A.C.W.3    Brew, K.4
  • 15
    • 0031105795 scopus 로고    scopus 로고
    • A chemoenzymatic synthesis of UDP-(2-deoxy-2-fluoro)-galactose and evaluation of its interaction with galactosyltransferase
    • Hayashi, T., Murray, B.W., Wang, R. and Wong, C.H. (1997) A chemoenzymatic synthesis of UDP-(2-deoxy-2-fluoro)-galactose and evaluation of its interaction with galactosyltransferase. Bioorg. Med. Chem., 5, 497-500.
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 497-500
    • Hayashi, T.1    Murray, B.W.2    Wang, R.3    Wong, C.H.4
  • 18
    • 0030824330 scopus 로고    scopus 로고
    • Mutational study of the amino-terminal domain of human tissue inhibitor of metalloproteinases 1 (TIMP-1) locates an inhibitory region for matrix metalloproteinases
    • Huang, W., Meng, Q., Suzuki, K., Nagase, H. and Brew, K. (1997) Mutational study of the amino-terminal domain of human tissue inhibitor of metalloproteinases 1 (TIMP-1) locates an inhibitory region for matrix metalloproteinases. J. Biol. Chem., 272, 22086-22091.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22086-22091
    • Huang, W.1    Meng, Q.2    Suzuki, K.3    Nagase, H.4    Brew, K.5
  • 19
    • 0026655074 scopus 로고
    • Enzyme-catalyzed oligosaccharide synthesis
    • Ichikawa, Y., Look, G.C. and Wong, C.-H. (1992) Enzyme-catalyzed oligosaccharide synthesis. (Review). Anal. Biochem., 202, 215-239.
    • (1992) Anal. Biochem. , vol.202 , pp. 215-239
    • Ichikawa, Y.1    Look, G.C.2    Wong, C.-H.3
  • 20
    • 0029564106 scopus 로고
    • Molecular analysis of a locus for the biosynthesis and phase-variable expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis
    • Jennings, M.P., Hood, D.M., Peak, I.R.A., Virji, M. and Moxon, E.R. (1995) Molecular analysis of a locus for the biosynthesis and phase-variable expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis. Mol. Microbiol., 18, 729-740.
    • (1995) Mol. Microbiol. , vol.18 , pp. 729-740
    • Jennings, M.P.1    Hood, D.M.2    Peak, I.R.A.3    Virji, M.4    Moxon, E.R.5
  • 21
    • 0016220517 scopus 로고
    • Some kinetic properties of human milk galactosyltransferase
    • Khatra, B.S., Herries, D.G. and Brew, K. (1974) Some kinetic properties of human milk galactosyltransferase. Eur. J. Biochem., 44, 537-560.
    • (1974) Eur. J. Biochem. , vol.44 , pp. 537-560
    • Khatra, B.S.1    Herries, D.G.2    Brew, K.3
  • 22
    • 0024165727 scopus 로고
    • An analysis of the galactosyltransferase reaction mechanism by positional isotope exchange and secondary deuterium effects
    • Kim, S.C., Singh, A.N. and Raushel, F.M. (1988) An analysis of the galactosyltransferase reaction mechanism by positional isotope exchange and secondary deuterium effects. Arch. Biochem. Biophys., 267, 54-59.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 54-59
    • Kim, S.C.1    Singh, A.N.2    Raushel, F.M.3
  • 23
    • 0031972692 scopus 로고    scopus 로고
    • Cloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3 β-galactosyltransferase catalyzing the formation of type 1 chains
    • Kolbinger, F., Streiff, M.B. and Katopodis, A.G. (1998) Cloning of a human UDP-galactose:2-acetamido-2-deoxy-D-glucose 3 β-galactosyltransferase catalyzing the formation of type 1 chains. J. Biol. Chem., 273, 433-440.
    • (1998) J. Biol. Chem. , vol.273 , pp. 433-440
    • Kolbinger, F.1    Streiff, M.B.2    Katopodis, A.G.3
  • 24
    • 0027533272 scopus 로고
    • Purification and characterization of recombinant human β-1,4-galactosyltransferase expressed in Saccharomyces cerevisiae
    • Krezdorn, C.H., Watzele, G., Kleene, R.B., Ivanov, S.X. and Berger, E.G. (1993) Purification and characterization of recombinant human β-1,4-galactosyltransferase expressed in Saccharomyces cerevisiae. Eur. J. Biochem., 212, 113-120.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 113-120
    • Krezdorn, C.H.1    Watzele, G.2    Kleene, R.B.3    Ivanov, S.X.4    Berger, E.G.5
  • 25
    • 0031777054 scopus 로고    scopus 로고
    • The expanding β4-galactosyltransferase gene family: Message from the databanks
    • Lo, N.W., Shaper, J.H., Pevsner, J. and Shaper, N.L. (1998) The expanding β4-galactosyltransferase gene family: message from the databanks. Glycobiology, 8, 517-526.
    • (1998) Glycobiology , vol.8 , pp. 517-526
    • Lo, N.W.1    Shaper, J.H.2    Pevsner, J.3    Shaper, N.L.4
  • 26
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficients of tryptonphan and tyrosine in native proteins
    • Mach, H., Middaugh, C.R. and Lewis, R.V. (1992) Statistical determination of the average values of the extinction coefficients of tryptonphan and tyrosine in native proteins. Anal. Biochem., 200, 74-80.
    • (1992) Anal. Biochem. , vol.200 , pp. 74-80
    • Mach, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 27
    • 0029764535 scopus 로고    scopus 로고
    • Functional site in alpha-lactalbumin encompasses a region corresponding to a subsite in lysozyme and parts of two adjacent flexible substructures
    • Malinovskii, V.A., Tian, J., Grobler, J.A. and Brew, K. (1996) Functional site in alpha-lactalbumin encompasses a region corresponding to a subsite in lysozyme and parts of two adjacent flexible substructures. Biochemistry, 35, 9710-9715.
    • (1996) Biochemistry , vol.35 , pp. 9710-9715
    • Malinovskii, V.A.1    Tian, J.2    Grobler, J.A.3    Brew, K.4
  • 29
    • 0026611050 scopus 로고
    • Complementarity between sperm surface β-1,4 galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding
    • Miller, D.J., Macek, M.B. and Shur,B.D. (1992) Complementarity between sperm surface β-1,4 galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding. Nature, 357, 589-593.
    • (1992) Nature , vol.357 , pp. 589-593
    • Miller, D.J.1    Macek, M.B.2    Shur, B.D.3
  • 30
    • 0027161319 scopus 로고
    • Kinetic study of human beta-1,4-galactosyltransferase expressed in E.coli
    • Nakazawa, K., Furukawa, K., Narimatsu, H. and Kobata, A. (1993) Kinetic study of human beta-1,4-galactosyltransferase expressed in E.coli. J. Biochem. (Tokyo), 113, 747-753.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 747-753
    • Nakazawa, K.1    Furukawa, K.2    Narimatsu, H.3    Kobata, A.4
  • 31
    • 0022542290 scopus 로고
    • Cloning and sequencing of cDNA of bovine N-acetylglucosamine β-1,4 galactosyltransferase
    • Narimatsu, H., Sinha, S., Brew, K., Okayama, H. and Qasba, P.K. (1986) Cloning and sequencing of cDNA of bovine N-acetylglucosamine β-1,4 galactosyltransferase. Proc. Natl. Acad. Sci. USA, 83, 4720-4724.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4720-4724
    • Narimatsu, H.1    Sinha, S.2    Brew, K.3    Okayama, H.4    Qasba, P.K.5
  • 32
    • 0027052199 scopus 로고
    • Galactosylation of non-natural glycosides with human β-D-galactosyltransferase on a preparative scale
    • Öhrlein, R., Ernst, B. and Berger, E.G. (1992) Galactosylation of non-natural glycosides with human β-D-galactosyltransferase on a preparative scale. Carbohydr. Res., 26, 335-338.
    • (1992) Carbohydr. Res. , vol.26 , pp. 335-338
    • Öhrlein, R.1    Ernst, B.2    Berger, E.G.3
  • 33
    • 0025971614 scopus 로고
    • Flexibility in the donor substrate specificity of β, 1,4-galactosyltransferase: Application in the synthesis of complex carbohydrates
    • Palcic, M.M. and Hindsgaul, O. (1991) Flexibility in the donor substrate specificity of β, 1,4-galactosyltransferase: application in the synthesis of complex carbohydrates. Glycobiology, 1, 205-209.
    • (1991) Glycobiology , vol.1 , pp. 205-209
    • Palcic, M.M.1    Hindsgaul, O.2
  • 34
    • 0024431691 scopus 로고
    • Glycosyltransferases. Structure, localization and control of cell type-specific glycosylation
    • Paulson, J.C. and Colley, K.J. (1989) Glycosyltransferases. Structure, localization and control of cell type-specific glycosylation. J. Biol. Chem., 264, 17615-17618.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 35
    • 0016232295 scopus 로고
    • Isolation and characterization of two forms of bovine galactosyltransferase
    • Powell, J.T. and Brew, K. (1974) Isolation and characterization of two forms of bovine galactosyltransferase. Eur. J. Biochem., 48, 217-228.
    • (1974) Eur. J. Biochem. , vol.48 , pp. 217-228
    • Powell, J.T.1    Brew, K.2
  • 36
    • 0017159511 scopus 로고
    • Metal ion activation of galactosyltrasferase
    • Powell, J.T. and Brew, K. (1976) Metal ion activation of galactosyltrasferase. J. Biol. Chem., 251, 3645-3652.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3645-3652
    • Powell, J.T.1    Brew, K.2
  • 37
    • 0027166035 scopus 로고
    • Cell surface β1,4 galactosyltransferase on primary spermatocytes facilitates their initial adhesion to Sertoli cells in vitro
    • Pratt, S.A., Scully, N.F. and Shur, B.D. (1993) Cell surface β1,4 galactosyltransferase on primary spermatocytes facilitates their initial adhesion to Sertoli cells in vitro. Biol. Reprod., 49, 470-482.
    • (1993) Biol. Reprod. , vol.49 , pp. 470-482
    • Pratt, S.A.1    Scully, N.F.2    Shur, B.D.3
  • 38
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarker, G. and Sommer, S.S. (1990) The "megaprimer" method of site-directed mutagenesis. BioTechniques, 8, 404-407.
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarker, G.1    Sommer, S.S.2
  • 39
    • 0014940419 scopus 로고
    • Galactosyltransferase acceptor specificity of lactose synthetase A protein
    • Schanbacher, F.L. and Ebner, K.E. (1970) Galactosyltransferase acceptor specificity of lactose synthetase A protein. J. Biol. Chem., 245, 5057-5061.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5057-5061
    • Schanbacher, F.L.1    Ebner, K.E.2
  • 40
    • 0032491511 scopus 로고    scopus 로고
    • Cloning of a novel member of the UDP-galactose:Beta-N-acetylglucosamine beta1,4-galactosyltransferase family, beta4Gal-T4, involved in glycosphingolipid biosynthesis
    • Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. (1998) Cloning of a novel member of the UDP-galactose:beta-N-acetylglucosamine beta1,4-galactosyltransferase family, beta4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem., 273, 29331-29340.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29331-29340
    • Schwientek, T.1    Almeida, R.2    Levery, S.B.3    Holmes, E.H.4    Bennett, E.5    Clausen, H.6
  • 41
    • 0345009059 scopus 로고
    • Bovine galactosyltransferase: Identification of a clone by direct immunological screening of a cDNA expression library
    • Shaper, N.L., Shaper, J.H., Meuth, J.L., Fox, J.L., Chang, H., Kirsch, I.R. and Hollis, G.F. (1986) Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library. Proc. Natl. Acad. Sci. USA, 83, 1537-1577.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1537-1577
    • Shaper, N.L.1    Shaper, J.H.2    Meuth, J.L.3    Fox, J.L.4    Chang, H.5    Kirsch, I.R.6    Hollis, G.F.7
  • 42
    • 0023713645 scopus 로고
    • Characterization of the full length cDNA for murine β-1,4 galactosyltransferase. Novel features at the 5′ end predict two translational start sites at two in-frame AUGs
    • Shaper, N.L., Hollis, G.G., Douglas, J.G., Kirsch, I.R. and Shaper, J.H. (1988) Characterization of the full length cDNA for murine β-1,4 galactosyltransferase. Novel features at the 5′ end predict two translational start sites at two in-frame AUGs. J. Biol. Chem., 263, 10420-10428.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10420-10428
    • Shaper, N.L.1    Hollis, G.G.2    Douglas, J.G.3    Kirsch, I.R.4    Shaper, J.H.5
  • 43
    • 0031454414 scopus 로고    scopus 로고
    • The chicken genome contains two functional nonallelic β-1,4-galactosyltransferase genes: Chromosomal assignment to syntenic regions tracks fate of the two gene lineages in the human genome
    • Shaper, N.L., Meurer, J.A., Joziasse, J.H., Chou, T.-D.D., Smith, E.J., Schnaar, R.L. and Shaper, J.H. (1997) the chicken genome contains two functional nonallelic β-1,4-galactosyltransferase genes: chromosomal assignment to syntenic regions tracks fate of the two gene lineages in the human genome. J. Biol. Chem., 272, 31389-31399.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31389-31399
    • Shaper, N.L.1    Meurer, J.A.2    Joziasse, J.H.3    Chou, T.-D.D.4    Smith, E.J.5    Schnaar, R.L.6    Shaper, J.H.7
  • 44
    • 0021065907 scopus 로고
    • Embryonal carcinoma cell adhesion: The role of surface galactosyltransferase and its 90K lactosaminoglycan substrate
    • Shur, B.D. (1983) Embryonal carcinoma cell adhesion: the role of surface galactosyltransferase and its 90K lactosaminoglycan substrate. Dev. Biol., 99, 360-372.
    • (1983) Dev. Biol. , vol.99 , pp. 360-372
    • Shur, B.D.1
  • 45
    • 0026318061 scopus 로고
    • Cell surface β1,4 galactosyltransferases: Twenty years later
    • Shur, B.D. (1991) Cell surface β1,4 galactosyltransferases: twenty years later. Glycobiology, 1, 563-575.
    • (1991) Glycobiology , vol.1 , pp. 563-575
    • Shur, B.D.1
  • 46
    • 0015150656 scopus 로고
    • The purification and properties of the A protein of lactose synthetase
    • Trayer, I.P. and Hill, R.L. (1971) The purification and properties of the A protein of lactose synthetase. J. Biol. Chem., 246, 6666-6675.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6666-6675
    • Trayer, I.P.1    Hill, R.L.2
  • 47
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theries are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theries are correct. Glycobiology, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 48
    • 0032493440 scopus 로고    scopus 로고
    • Activity of the yeast MNN1 α-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases
    • Wiggins, C.A.R. and Munro, S. (1998) Activity of the yeast MNN1 α-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc. Natl. Acad. Sci. USA, 95, 7945-7950.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7945-7950
    • Wiggins, C.A.R.1    Munro, S.2
  • 49
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R.W. (1995) Circular dichroism. Methods Enzymol., 246, 34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 50
    • 0025042557 scopus 로고
    • Identification of a region of UDP-galactose: N-acetylglucosamine β-4 galactosyltransferase involved in UDP-galactose binding by differential labeling
    • Yadav, S.P. and Brew, K. (1990) Identification of a region of UDP-galactose: N-acetylglucosamine β-4 galactosyltransferase involved in UDP-galactose binding by differential labeling. J. Biol. Chem., 265, 14163-14169.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14163-14169
    • Yadav, S.P.1    Brew, K.2
  • 51
    • 0026069501 scopus 로고
    • Structure and function in galactosyltransferase: Sequence locations of α-lactalbumin binding site, thiol groups and disulfide bond
    • Yadav, S.P. and Brew, K. (1991) Structure and function in galactosyltransferase: sequence locations of α-lactalbumin binding site, thiol groups and disulfide bond. J. Biol. Chem., 266, 698-703.
    • (1991) J. Biol. Chem. , vol.266 , pp. 698-703
    • Yadav, S.P.1    Brew, K.2
  • 52
    • 0028941855 scopus 로고
    • Chemical and enzymatic synthesis of glycoconjugates. I. Enzymatic galactosylation of conduritol B. (1995)
    • Yu, L., Cabrera, R., Ramirez, J., Wang, P., Malinovskii, V.A. and Brew, K. (1995) Chemical and enzymatic synthesis of glycoconjugates. I. Enzymatic galactosylation of conduritol B. (1995) Tetrahedron Lett., 36, 2897-2900.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 2897-2900
    • Yu, L.1    Cabrera, R.2    Ramirez, J.3    Wang, P.4    Malinovskii, V.A.5    Brew, K.6
  • 53
    • 0031561502 scopus 로고    scopus 로고
    • Secreted Fringe-like signaling molecules may be glycosyltransferases
    • Yuan, Y.P., Schultz, J., Moldzik, M. and Bork, P. (1997) Secreted Fringe-like signaling molecules may be glycosyltransferases. Cell, 88, 9-11.
    • (1997) Cell , vol.88 , pp. 9-11
    • Yuan, Y.P.1    Schultz, J.2    Moldzik, M.3    Bork, P.4
  • 54
    • 0028815836 scopus 로고
    • Use of site-directed mutagenesis to identify the galactosyltransferase binding sites for UDP-galactose
    • Zu, H., Fukuda, M.N., Wong, S.S., Wang, Y. Liu, Z., Tang, Q. and Appert, H.E. (1995) Use of site-directed mutagenesis to identify the galactosyltransferase binding sites for UDP-galactose. Biochem. Biophys. Res. Commun., 206, 362-369.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 362-369
    • Zu, H.1    Fukuda, M.N.2    Wong, S.S.3    Wang, Y.4    Liu, Z.5    Tang, Q.6    Appert, H.E.7


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