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Volumn 7, Issue 5, 1997, Pages 652-660

Enzyme-catalyzed formation of glycosidic linkages

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOCONJUGATE; GLYCOPROTEIN; GLYCOSIDASE; GLYCOSIDE; GLYCOSYLTRANSFERASE; MANNOSE; TRISACCHARIDE;

EID: 0030735602     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80074-7     Document Type: Article
Times cited : (65)

References (53)
  • 1
    • 5244279498 scopus 로고
    • Recent progress in O-glycosylation methods and its application to natural products synthesis
    • Toshima K, Tatsuta K. Recent progress in O-glycosylation methods and its application to natural products synthesis. Chem Rev. 93:1993;1503-1531.
    • (1993) Chem Rev , vol.93 , pp. 1503-1531
    • Toshima, K.1    Tatsuta, K.2
  • 2
    • 0001776897 scopus 로고    scopus 로고
    • Enzymatic synthesis of oligosaccharides and glycopeptides
    • D.G. Large, Warren C.D. New York: Marcel Dekker
    • Ichikawa Y. Enzymatic synthesis of oligosaccharides and glycopeptides. Large DG, Warren CD. Glycopeptides and Related Compounds. 1997;79-205 Marcel Dekker, New York.
    • (1997) Glycopeptides and Related Compounds , pp. 79-205
    • Ichikawa, Y.1
  • 3
    • 2642642035 scopus 로고    scopus 로고
    • Recent advances in the chemoenzymatic synthesis of carbohydrates and carbohydrate mimetics
    • Gijsen HJM, Qiao L, Fitz W, Wong C-H. Recent advances in the chemoenzymatic synthesis of carbohydrates and carbohydrate mimetics. Chem Rev. 96:1996;443-473.
    • (1996) Chem Rev , vol.96 , pp. 443-473
    • Gijsen, H.J.M.1    Qiao, L.2    Fitz, W.3    Wong, C.-H.4
  • 4
    • 37049070324 scopus 로고
    • Kinetic control of regioselectivity in glycosidase-catalysed disaccharide synthesis: Preparation of N,N'-diacetylchitobiose and 2-acetamido-6-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-2-deoxy-D- glucopyranose
    • Singh S, Packwood J, Crout DHG. Kinetic control of regioselectivity in glycosidase-catalysed disaccharide synthesis: preparation of N,N'-diacetylchitobiose and 2-acetamido-6-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-2-deoxy-D- glucopyranose. J Chem Soc Chem Commun. 1994;2227-2228.
    • (1994) J Chem Soc Chem Commun , pp. 2227-2228
    • Singh, S.1    Packwood, J.2    Crout, D.H.G.3
  • 5
    • 0003053760 scopus 로고    scopus 로고
    • Glycosidase-catalysed synthesis of oligosaccharides: A two-step synthesis of the core trisaccharide of N-linked glycoproteins using the β-N-acetylhexosaminidase and the β-mannosidase from Aspergillus oryzae
    • An efficient two-step route to the core trisaccharide of N-glycans using a β-mannosidase. This result is important, first, because of the wide abundance of N-linked oligosaccharides and, second, because the chemical synthesis of the β-mannosyl linkage is very difficult. of special interest
    • Singh S, Scigelova M, Crout DHG. Glycosidase-catalysed synthesis of oligosaccharides: a two-step synthesis of the core trisaccharide of N-linked glycoproteins using the β-N-acetylhexosaminidase and the β-mannosidase from Aspergillus oryzae. J Chem Soc Chem Commun. 1996;993-994 An efficient two-step route to the core trisaccharide of N-glycans using a β-mannosidase. This result is important, first, because of the wide abundance of N-linked oligosaccharides and, second, because the chemical synthesis of the β-mannosyl linkage is very difficult. of special interest.
    • (1996) J Chem Soc Chem Commun , pp. 993-994
    • Singh, S.1    Scigelova, M.2    Crout, D.H.G.3
  • 6
    • 0040657616 scopus 로고
    • Advances in selective chemical syntheses of complex oligosaccharides
    • Int Ed
    • Paulsen H. Advances in selective chemical syntheses of complex oligosaccharides. Int Ed Angew Chem. 21:1982;155-173.
    • (1982) Angew Chem , vol.21 , pp. 155-173
    • Paulsen, H.1
  • 7
    • 0031013621 scopus 로고    scopus 로고
    • Glycosidase-catalysed synthesis of di- And trisaccharide derivatives related to antigens involved in the hyperacute rejection of xenotransplants
    • A demonstration of the wide substrate specificity possessed by a β-D-galactosidase and an α-D-galactosidase used in turn for the synthesis of α-Gal-1,3-β-Gal-1,4-β-GlcNTeoc-1-SEt. The hydrophobic nature of the Teoc group facilitates the purification of reaction products. of special interest
    • Nilsson KGI. Glycosidase-catalysed synthesis of di- and trisaccharide derivatives related to antigens involved in the hyperacute rejection of xenotransplants. Tetrahedron Lett. 38:1997;133-136 A demonstration of the wide substrate specificity possessed by a β-D-galactosidase and an α-D-galactosidase used in turn for the synthesis of α-Gal-1,3-β-Gal-1,4-β-GlcNTeoc-1-SEt. The hydrophobic nature of the Teoc group facilitates the purification of reaction products. of special interest.
    • (1997) Tetrahedron Lett , vol.38 , pp. 133-136
    • Nilsson, K.G.I.1
  • 8
    • 1542424389 scopus 로고    scopus 로고
    • Glycosidase-catalysed synthesis of oligosaccharides: A one step synthesis of lactosamine and of the linear B type 2 trisaccharide α-D-Gal-(1-3)-β-D-Gal-(1-4)-β-D-GlcNAcSEt involved in the hyperacute rejection response in xenotransplantation from pigs to man and the specific receptor for toxin A from Clostridium difficile
    • Vic G, Tran CH, Scigelova M, Crout DHG. Glycosidase-catalysed synthesis of oligosaccharides: a one step synthesis of lactosamine and of the linear B type 2 trisaccharide α-D-Gal-(1-3)-β-D-Gal-(1-4)-β-D-GlcNAcSEt involved in the hyperacute rejection response in xenotransplantation from pigs to man and the specific receptor for toxin A from Clostridium difficile. J Chem Soc Chem Commun. 1997;169-170.
    • (1997) J Chem Soc Chem Commun , pp. 169-170
    • Vic, G.1    Tran, C.H.2    Scigelova, M.3    Crout, D.H.G.4
  • 9
    • 0030444511 scopus 로고    scopus 로고
    • A practical method for the synthesis of N-acetyl-D-lactosamine derivatives by the tandem use of galactose oxidase and β-galactosidase
    • Int Ed
    • Kimura T, Takayama S, Huang H, Wong C-H. A practical method for the synthesis of N-acetyl-D-lactosamine derivatives by the tandem use of galactose oxidase and β-galactosidase. Int Ed Angew Chem. 35:1996;2348-2350.
    • (1996) Angew Chem , vol.35 , pp. 2348-2350
    • Kimura, T.1    Takayama, S.2    Huang, H.3    Wong, C.-H.4
  • 10
    • 0030200594 scopus 로고    scopus 로고
    • Glycosidase-catalysed synthesis of glycosides by an improved procedure for reverse hydrolysis: Application to the chemoenzymatic synthesis of galacto-(1-4)-α-galacto derivatives
    • Vic G, Hastings JJ, Crout DHG. Glycosidase-catalysed synthesis of glycosides by an improved procedure for reverse hydrolysis: application to the chemoenzymatic synthesis of galacto-(1-4)-α-galacto derivatives. Tetrahedron Asym. 7:1996;1973-1984.
    • (1996) Tetrahedron Asym , vol.7 , pp. 1973-1984
    • Vic, G.1    Hastings, J.J.2    Crout, D.H.G.3
  • 11
    • 0030580312 scopus 로고    scopus 로고
    • Microwave radiation can increase the rate of enzyme-catalysed reactions in organic media
    • Parker M-C, Besson T, Lamare S, Legoy M. Microwave radiation can increase the rate of enzyme-catalysed reactions in organic media. Tetrahedron Lett. 37:1996;8383-8386.
    • (1996) Tetrahedron Lett , vol.37 , pp. 8383-8386
    • Parker, M.-C.1    Besson, T.2    Lamare, S.3    Legoy, M.4
  • 13
    • 0029056255 scopus 로고
    • Enhanced transglycosylation activity of Arthrobacter protophormiae endo-β-D-acetylglucosaminidase in media containing organic solvents
    • Fan J, Takegawa K, Iwahara S, Kondo A, Kato I, Abeygunawardana C, Lee YC. Enhanced transglycosylation activity of Arthrobacter protophormiae endo-β-D-acetylglucosaminidase in media containing organic solvents. J Biol Chem. 270:1995;17723-17729.
    • (1995) J Biol Chem , vol.270 , pp. 17723-17729
    • Fan, J.1    Takegawa, K.2    Iwahara, S.3    Kondo, A.4    Kato, I.5    Abeygunawardana, C.6    Lee, Y.C.7
  • 15
    • 0029023104 scopus 로고
    • Synthesis of neoglycoconjugates by transglycosylation with Arthrobacter protophormiae endo-β-N-acetylglucosaminidase
    • Fan J-Q, Quesenberry MS, Takegawa K, Iwahara S, Kondo A, Kato I, Lee YC. Synthesis of neoglycoconjugates by transglycosylation with Arthrobacter protophormiae endo-β-N-acetylglucosaminidase. J Biol Chem. 270:1995;17730-17735.
    • (1995) J Biol Chem , vol.270 , pp. 17730-17735
    • Fan, J.-Q.1    Quesenberry, M.S.2    Takegawa, K.3    Iwahara, S.4    Kondo, A.5    Kato, I.6    Lee, Y.C.7
  • 16
    • 0029914514 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of a high-mannose-type N-glycopeptide analog with C-glycosidic linkage
    • 2-Asn containing peptide to yield a complex high-mannose-type N-glycopeptide analogue. of outstanding interest
    • 2-Asn containing peptide to yield a complex high-mannose-type N-glycopeptide analogue. of outstanding interest.
    • (1996) Tetrahedron Lett , vol.37 , pp. 1975-1978
    • Wang, L.1    Fan, J.2    Lee, Y.C.3
  • 17
    • 0028343530 scopus 로고
    • Glycosyltransferases in glycobiology
    • Palcic MM. Glycosyltransferases in glycobiology. Methods Enzymol. 230:1994;300-360.
    • (1994) Methods Enzymol , vol.230 , pp. 300-360
    • Palcic, M.M.1
  • 18
    • 0030445043 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of a sialylated undecasaccharide-asparagine conjugate
    • This paper describes an effective use of two glycosyltransferases in turn to finish off a chemical synthesis, which would be difficult to do by chemical means. The glycosyltransfer steps are carried out successively in high yield. of special interest. Int Ed
    • Unverzagt C. Chemoenzymatic synthesis of a sialylated undecasaccharide-asparagine conjugate. Int Ed Angew Chem. 35:1996;2350-2353 This paper describes an effective use of two glycosyltransferases in turn to finish off a chemical synthesis, which would be difficult to do by chemical means. The glycosyltransfer steps are carried out successively in high yield. of special interest.
    • (1996) Angew Chem , vol.35 , pp. 2350-2353
    • Unverzagt, C.1
  • 19
    • 0029736391 scopus 로고    scopus 로고
    • Mechanism and specificity of human α-1,3-fucosyltransferase V
    • Murray BW, Takayama S, Schultz J, Wong C-H. Mechanism and specificity of human α-1,3-fucosyltransferase V. Biochemistry. 35:1996;11183-11195.
    • (1996) Biochemistry , vol.35 , pp. 11183-11195
    • Murray, B.W.1    Takayama, S.2    Schultz, J.3    Wong, C.-H.4
  • 20
    • 0031039932 scopus 로고    scopus 로고
    • Mechanism of human α-1,3-fucosyltransferase V: Glycosidic cleavage occurs prior to nucleophilic attack
    • Murray BW, Wittmann V, Burkart MD, Hung S, Wong C-H. Mechanism of human α-1,3-fucosyltransferase V: glycosidic cleavage occurs prior to nucleophilic attack. Biochemistry. 36:1997;823-831.
    • (1997) Biochemistry , vol.36 , pp. 823-831
    • Murray, B.W.1    Wittmann, V.2    Burkart, M.D.3    Hung, S.4    Wong, C.-H.5
  • 21
    • 0030956956 scopus 로고    scopus 로고
    • 1H-tetrazole as a catalyst in phosphomorpholidate coupling reactions: Efficient synthesis of GDP-fucose, GDP-mannose, and UDP-galactose
    • 1H-tetrazole as a catalyst in phosphomorpholidate coupling reactions: efficient synthesis of GDP-fucose, GDP-mannose, and UDP-galactose. J Org Chem. 62:1997;2144-2147.
    • (1997) J Org Chem , vol.62 , pp. 2144-2147
    • Wittmann, V.1    Wong, C.-H.2
  • 22
    • 0030922424 scopus 로고    scopus 로고
    • Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferases boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes
    • A human glycosyltransferase is overexpressed in E. coli and used for the preparative-scale synthesis of the human blood group A antigen. Kinetic characterization of this enzyme and of mutants provide some structure/function relationships which may pave the way for further understanding of factors that determine the mechanism and specificity of glycosyltransferases. of special interest
    • Seto NOL, Palcic MM, Compston CA, Li H, Bundle DR, Narang SA. Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferases boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes. J Biol Chem. 272:1997;14133-14138 A human glycosyltransferase is overexpressed in E. coli and used for the preparative-scale synthesis of the human blood group A antigen. Kinetic characterization of this enzyme and of mutants provide some structure/function relationships which may pave the way for further understanding of factors that determine the mechanism and specificity of glycosyltransferases. of special interest.
    • (1997) J Biol Chem , vol.272 , pp. 14133-14138
    • Seto, N.O.L.1    Palcic, M.M.2    Compston, C.A.3    Li, H.4    Bundle, D.R.5    Narang, S.A.6
  • 23
    • 0030294016 scopus 로고    scopus 로고
    • Acceptor hydroxyl group mapping for human milk α1-3 and α1-3/4 fucosyltransferases
    • Two fucosyltransferases from human milk are isolated to map their acceptor-binding sites. The results of kinetic studies using monodeoxygenated derivatives are analogous to those of cloned fucosyltransferases III-V. of special interest
    • Gosselin S, Palcic MM. Acceptor hydroxyl group mapping for human milk α1-3 and α1-3/4 fucosyltransferases. Bioorg Med Chem. 4:1996;2023-2028 Two fucosyltransferases from human milk are isolated to map their acceptor-binding sites. The results of kinetic studies using monodeoxygenated derivatives are analogous to those of cloned fucosyltransferases III-V. of special interest.
    • (1996) Bioorg Med Chem , vol.4 , pp. 2023-2028
    • Gosselin, S.1    Palcic, M.M.2
  • 24
    • 0028969419 scopus 로고
    • Acceptor specificity of different length constructs of human recombinant alpha-1,3/4-fucosyl-transferases - replacement of the stem region and the transmembrane domain of fucosyl-transferase-V by protein-A results in an enzyme with GDP-fucosyl hydrolysing activity
    • De Vries T, Srnka C, Palcic MM, Swiedler S, Vandeneijungen D, Macher B. Acceptor specificity of different length constructs of human recombinant alpha-1,3/4-fucosyl-transferases - replacement of the stem region and the transmembrane domain of fucosyl-transferase-V by protein-A results in an enzyme with GDP-fucosyl hydrolysing activity. J Biol Chem. 270:1995;8712-8722.
    • (1995) J Biol Chem , vol.270 , pp. 8712-8722
    • De Vries, T.1    Srnka, C.2    Palcic, M.M.3    Swiedler, S.4    Vandeneijungen, D.5    Macher, B.6
  • 25
    • 0029960003 scopus 로고    scopus 로고
    • Enzymatic galactosylation of non-natural glucosamide acceptors
    • Baisch G, Ohrlein R, Ernst B. Enzymatic galactosylation of non-natural glucosamide acceptors. Bioorg Med Chem Lett. 6:1996;749-754.
    • (1996) Bioorg Med Chem Lett , vol.6 , pp. 749-754
    • Baisch, G.1    Ohrlein, R.2    Ernst, B.3
  • 26
    • 0030008018 scopus 로고    scopus 로고
    • Enzymatic α-2,3-sialylation of non-natural disaccharides with cloned sialyltransferase
    • Baisch G, Ohrlein R, Streiff M, Ernst B. Enzymatic α-2,3-sialylation of non-natural disaccharides with cloned sialyltransferase. Bioorg Med Chem Lett. 6:1996;755-758.
    • (1996) Bioorg Med Chem Lett , vol.6 , pp. 755-758
    • Baisch, G.1    Ohrlein, R.2    Streiff, M.3    Ernst, B.4
  • 27
    • 0029915224 scopus 로고    scopus 로고
    • Enzymatic fucosylation of non-natural trisaccharides with cloned fucosyltransferase VI
    • Baisch G, Ohrlein R, Katopodis A, Ernst B. Enzymatic fucosylation of non-natural trisaccharides with cloned fucosyltransferase VI. Bioorg Med Chem Lett. 6:1996;759-762.
    • (1996) Bioorg Med Chem Lett , vol.6 , pp. 759-762
    • Baisch, G.1    Ohrlein, R.2    Katopodis, A.3    Ernst, B.4
  • 28
    • 0029065414 scopus 로고
    • Chemical-enzymatic synthesis and bioactivity of mono-6[Gal-β-1,4-GlcNAc-β-1,6-hexyl]-amido-6-deoxy-cycloheptaamylose
    • Leray E, Parrot-Lopez H, Auge C, Coleman AW, Finance C, Bonaly R. Chemical-enzymatic synthesis and bioactivity of mono-6[Gal-β-1,4-GlcNAc-β-1,6-hexyl]-amido-6-deoxy-cycloheptaamylose. J Chem Soc Chem Comm. 1995;1019-1020.
    • (1995) J Chem Soc Chem Comm , pp. 1019-1020
    • Leray, E.1    Parrot-Lopez, H.2    Auge, C.3    Coleman, A.W.4    Finance, C.5    Bonaly, R.6
  • 29
    • 0028941855 scopus 로고
    • Chemical and enzymatic synthesis of glycoconjugates 1. Enzymatic galactosylation of conduritol
    • Yu L, Cabrera R, Ramirez J, Malinovskii VA, Brew K, Wang PG. Chemical and enzymatic synthesis of glycoconjugates 1. Enzymatic galactosylation of conduritol. Tetrahedron Lett. 36:1995;2897-2900.
    • (1995) Tetrahedron Lett , vol.36 , pp. 2897-2900
    • Yu, L.1    Cabrera, R.2    Ramirez, J.3    Malinovskii, V.A.4    Brew, K.5    Wang, P.G.6
  • 31
    • 0028672815 scopus 로고
    • Regeneration of sugar nucleotide for enzymatic oligosaccharide synthesis
    • Ichikawa Y, Wang R, Wong C-H. Regeneration of sugar nucleotide for enzymatic oligosaccharide synthesis. Methods Enzymol. 247:1994;107-127.
    • (1994) Methods Enzymol , vol.247 , pp. 107-127
    • Ichikawa, Y.1    Wang, R.2    Wong, C.-H.3
  • 32
    • 0029137069 scopus 로고
    • A multienzyme system for a one-pot synthesis of sialyl T-antigen
    • Int Ed
    • Kren V, Thiem J. A multienzyme system for a one-pot synthesis of sialyl T-antigen. Int Ed Angew Chem. 34:1995;893-895.
    • (1995) Angew Chem , vol.34 , pp. 893-895
    • Kren, V.1    Thiem, J.2
  • 33
    • 0028847233 scopus 로고
    • Application of sucrose phosphorylase reaction in one-pot enzymatic galactosylation: Scavenger of phosphate and generation of glucose 1-phosphate in situ
    • Ichikawa M, Schnaar RL, Ichikawa Y. Application of sucrose phosphorylase reaction in one-pot enzymatic galactosylation: scavenger of phosphate and generation of glucose 1-phosphate in situ. Tetrahedron Lett. 36:1995;8731-8732.
    • (1995) Tetrahedron Lett , vol.36 , pp. 8731-8732
    • Ichikawa, M.1    Schnaar, R.L.2    Ichikawa, Y.3
  • 34
    • 0027951227 scopus 로고
    • Solid-phase chemical-enzymatic synthesis of glycopeptides and oligosaccharides
    • Schuster M, Wang P, Paulson JC, Wong C-H. Solid-phase chemical-enzymatic synthesis of glycopeptides and oligosaccharides. J Am Chem Soc. 116:1994;1135-1136.
    • (1994) J Am Chem Soc , vol.116 , pp. 1135-1136
    • Schuster, M.1    Wang, P.2    Paulson, J.C.3    Wong, C.-H.4
  • 35
    • 0028587090 scopus 로고
    • Solution- And solid-phase synthesis of inhibitors of H. pylori attachment and E-selectin-mediated leukocyte adhesion
    • Halcomb RL, Huang H, Wong C-H. Solution- and solid-phase synthesis of inhibitors of H. pylori attachment and E-selectin-mediated leukocyte adhesion. J Am Chem Soc. 116:1994;11315-11322.
    • (1994) J Am Chem Soc , vol.116 , pp. 11315-11322
    • Halcomb, R.L.1    Huang, H.2    Wong, C.-H.3
  • 36
    • 37049067264 scopus 로고
    • A PEGA resin for use in the solid-phase chemical-enzymatic synthesis of glycopeptides
    • Meldal M, Auzanneau F-I, Hindsgaul O, Palcic MM. A PEGA resin for use in the solid-phase chemical-enzymatic synthesis of glycopeptides. J Chem Soc Chem Commun. 1994;1849-1850.
    • (1994) J Chem Soc Chem Commun , pp. 1849-1850
    • Meldal, M.1    Auzanneau, F.-I.2    Hindsgaul, O.3    Palcic, M.M.4
  • 37
    • 0028761774 scopus 로고
    • Polymer-supported enzymic synthesis on a preparative scale
    • Köpper S. Polymer-supported enzymic synthesis on a preparative scale. Carbohydr Res. 265:1994;161-166.
    • (1994) Carbohydr Res , vol.265 , pp. 161-166
    • Köpper, S.1
  • 38
    • 0028001271 scopus 로고
    • Chemoenzymatic oligosaccharide synthesis on a soluble polymeric carrier
    • Nishimura S-I, Matsuoka K, Lee YC. Chemoenzymatic oligosaccharide synthesis on a soluble polymeric carrier. Tetrahedron Lett. 35:1994;5657-5660.
    • (1994) Tetrahedron Lett , vol.35 , pp. 5657-5660
    • Nishimura, S.-I.1    Matsuoka, K.2    Lee, Y.C.3
  • 39
    • 0029609447 scopus 로고
    • An efficient synthesis of sialoglycoconjugates on a peptidase-sensitive polymer support
    • Yamada K, Nishimura S-I. An efficient synthesis of sialoglycoconjugates on a peptidase-sensitive polymer support. Tetrahedron Lett. 36:1995;9493-9496.
    • (1995) Tetrahedron Lett , vol.36 , pp. 9493-9496
    • Yamada, K.1    Nishimura, S.-I.2
  • 40
    • 0028417390 scopus 로고
    • Enzymic synthesis of N-acetyllactosamine on a soluble light-sensitive polymer
    • Wiemann T, Taubken N, Zehavi U, Thiem J. Enzymic synthesis of N-acetyllactosamine on a soluble light-sensitive polymer. Carbohydr Res. 257:1994;C1-C6.
    • (1994) Carbohydr Res , vol.257
    • Wiemann, T.1    Taubken, N.2    Zehavi, U.3    Thiem, J.4
  • 41
    • 0031500827 scopus 로고    scopus 로고
    • Solid-phase enzymatic synthesis of a Lewis A trisaccharide using an acceptor reversibly bound to sepharose
    • Blixt O, Norberg T. Solid-phase enzymatic synthesis of a Lewis A trisaccharide using an acceptor reversibly bound to sepharose. J Carbohydr Chem. 16:1997;143-154.
    • (1997) J Carbohydr Chem , vol.16 , pp. 143-154
    • Blixt, O.1    Norberg, T.2
  • 42
    • 0030090601 scopus 로고    scopus 로고
    • Chemical and biological approaches to glycoprotein synthesis
    • Bill RM, Flitsch SL. Chemical and biological approaches to glycoprotein synthesis. Chem Biol. 3:1996;145-149.
    • (1996) Chem Biol , vol.3 , pp. 145-149
    • Bill, R.M.1    Flitsch, S.L.2
  • 43
    • 0029610991 scopus 로고
    • Asparagine-linked glycosylation: Specificity and function of oligosaccharyl transferase
    • Imperiali B, Hendrickson TL. Asparagine-linked glycosylation: specificity and function of oligosaccharyl transferase. Bioorg Med Chem. 3:1995;1565-1578.
    • (1995) Bioorg Med Chem , vol.3 , pp. 1565-1578
    • Imperiali, B.1    Hendrickson, T.L.2
  • 44
    • 0029991763 scopus 로고    scopus 로고
    • Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase
    • The most recent review of oligosaccharyltransferase, including a summary of mechanistic studies. of special interest
    • Silberstein S, Gilmore R. Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase. FASEB J. 10:1996;849-858 The most recent review of oligosaccharyltransferase, including a summary of mechanistic studies. of special interest.
    • (1996) FASEB J , vol.10 , pp. 849-858
    • Silberstein, S.1    Gilmore, R.2
  • 45
    • 0029618326 scopus 로고
    • Investigation of the active site of oligosaccharyltransferase from pig liver using synthetic tripeptides as tools
    • Bause E, Breuer W, Peters S. Investigation of the active site of oligosaccharyltransferase from pig liver using synthetic tripeptides as tools. Biochem J. 312:1995;979-985.
    • (1995) Biochem J , vol.312 , pp. 979-985
    • Bause, E.1    Breuer, W.2    Peters, S.3
  • 46
    • 0028806665 scopus 로고
    • Synthesis and evaluation of synthetic analogues of dolichyl-P-P-chitobiose as oligosaccharyltransferase substrates
    • Fang X, Gibbs BS, Coward JK. Synthesis and evaluation of synthetic analogues of dolichyl-P-P-chitobiose as oligosaccharyltransferase substrates. Bioorg Med Chem Lett. 5:1995;2701-2706.
    • (1995) Bioorg Med Chem Lett , vol.5 , pp. 2701-2706
    • Fang, X.1    Gibbs, B.S.2    Coward, J.K.3
  • 47
    • 0030656964 scopus 로고    scopus 로고
    • Efficient enzymatic synthesis of the core trisaccharide of N-glycans using a recombinant β-mannosyltransferase
    • Int Ed in press
    • Watt GM, Revers L, Webberley MC, Wilson IBH, Flitsch SL. Efficient enzymatic synthesis of the core trisaccharide of N-glycans using a recombinant β-mannosyltransferase. Int Ed Angew Chem. 36:1997;. in press.
    • (1997) Angew Chem , vol.36
    • Watt, G.M.1    Revers, L.2    Webberley, M.C.3    Wilson, I.B.H.4    Flitsch, S.L.5
  • 48
    • 0030936614 scopus 로고    scopus 로고
    • Enzymatic glycoprotein synthesis: Preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation
    • The synthesis of a novel glycoprotein is described utilising purified glycosyltransferases and a peptide ligase. It is shown that glycosyltransferases can recognize unnatural glycoprotein acceptors and that glycopeptides can be ligated under thermodynamic conditions to give full length proteins. of outstanding interest
    • Witte K, Sears P, Martin R, Wong C-H. Enzymatic glycoprotein synthesis: preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation. J Am Chem Soc. 119:1997;2114-2118 The synthesis of a novel glycoprotein is described utilising purified glycosyltransferases and a peptide ligase. It is shown that glycosyltransferases can recognize unnatural glycoprotein acceptors and that glycopeptides can be ligated under thermodynamic conditions to give full length proteins. of outstanding interest.
    • (1997) J Am Chem Soc , vol.119 , pp. 2114-2118
    • Witte, K.1    Sears, P.2    Martin, R.3    Wong, C.-H.4
  • 49
    • 0029743320 scopus 로고    scopus 로고
    • Firefly luciferase: Alteration of the color of emitted light resulting from substitutions at position 286
    • The first example of the site-specific incorporation of a glycosylated amino acid into a protein via the techniques of unnatural amino acid mutagenesis and in vitro translation. of outstanding interest
    • Mamaev SV, Laikhter AL, Arslan T, Hecht SM. Firefly luciferase: alteration of the color of emitted light resulting from substitutions at position 286. J Am Chem Soc. 118:1996;7243-7244 The first example of the site-specific incorporation of a glycosylated amino acid into a protein via the techniques of unnatural amino acid mutagenesis and in vitro translation. of outstanding interest.
    • (1996) J Am Chem Soc , vol.118 , pp. 7243-7244
    • Mamaev, S.V.1    Laikhter, A.L.2    Arslan, T.3    Hecht, S.M.4
  • 50
    • 0029108642 scopus 로고
    • Probing protein structure and function with an expanded genetic code
    • Int Ed
    • Cornish VW, Mendel D, Schultz PG. Probing protein structure and function with an expanded genetic code. Int Ed Angew Chem. 34:1995;621-633.
    • (1995) Angew Chem , vol.34 , pp. 621-633
    • Cornish, V.W.1    Mendel, D.2    Schultz, P.G.3
  • 51
    • 0028011302 scopus 로고
    • Recombinant whole cells as catalysts for the enzymatic synthesis of oligosaccharides and glycopeptides
    • Int Ed
    • Herrmann GF, Wang P, Shen G-J, Wong C-H. Recombinant whole cells as catalysts for the enzymatic synthesis of oligosaccharides and glycopeptides. Int Ed Angew Chem. 33:1994;1241-1242.
    • (1994) Angew Chem , vol.33 , pp. 1241-1242
    • Herrmann, G.F.1    Wang, P.2    Shen, G.-J.3    Wong, C.-H.4
  • 53
    • 0028964058 scopus 로고
    • Use of transformed whole yeast cells expressing β-1,4-galactosyltransferase for the synthesis of N-acetyllactosamine
    • Herrmann GF, Elling L, Krezdorn CH, Kleene R, Berger EG, Wandrey C. Use of transformed whole yeast cells expressing β-1,4-galactosyltransferase for the synthesis of N-acetyllactosamine. Biorg Med Chem Lett. 5:1995;673-676.
    • (1995) Biorg Med Chem Lett , vol.5 , pp. 673-676
    • Herrmann, G.F.1    Elling, L.2    Krezdorn, C.H.3    Kleene, R.4    Berger, E.G.5    Wandrey, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.