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Volumn 259, Issue 3, 1999, Pages 770-775

Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli

Author keywords

Blood groups; Carbohydrate antigens; Enzyme kinetics; Glycosyltransferases; Recombinant

Indexed keywords

GLYCOSYLTRANSFERASE;

EID: 0033083847     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00086.x     Document Type: Article
Times cited : (88)

References (25)
  • 2
    • 0027742093 scopus 로고
    • The molecular and cell biology of glycosyltransferases
    • 2. Kleene, R. & Berger, E.G. (1993) The molecular and cell biology of glycosyltransferases. Biochim. Biophys. Acta 1154, 283-325.
    • (1993) Biochim. Biophys. Acta , vol.1154 , pp. 283-325
    • Kleene, R.1    Berger, E.G.2
  • 3
    • 0018895005 scopus 로고
    • Biochemistry and genetics of the ABO, Lewis and P blood group systems
    • 3. Watkins, W.M. (1980) Biochemistry and genetics of the ABO, Lewis and P blood group systems. Adv. Hum. Genet. 10, 1-136.
    • (1980) Adv. Hum. Genet. , vol.10 , pp. 1-136
    • Watkins, W.M.1
  • 4
    • 0025101066 scopus 로고
    • Cloning and characterization of DNA complementary to human UDP-GalNAc: Fucα1-2Galα1-3GalNAc transferase (histo-blood group A transferase) mRNA
    • 4. Yamamoto, F.-I., Marken, J., Tsuju, T., White, T., Clausen, H. & Hakomori, S.-I. (1990) Cloning and characterization of DNA complementary to human UDP-GalNAc: Fucα1-2Galα1-3GalNAc transferase (histo-blood group A transferase) mRNA. J. Biol. Chem. 265, 1146-1151.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1146-1151
    • Yamamoto, F.-I.1    Marken, J.2    Tsuju, T.3    White, T.4    Clausen, H.5    Hakomori, S.-I.6
  • 5
    • 0025270738 scopus 로고
    • Molecular genetic basis of the histo-blood group ABO system
    • 5. Yamamoto, F.-I., Clausen, H., White, T., Marken, J. & Hakomori, S.-I. (1990) Molecular genetic basis of the histo-blood group ABO system. Nature 345, 229-233.
    • (1990) Nature , vol.345 , pp. 229-233
    • Yamamoto, F.-I.1    Clausen, H.2    White, T.3    Marken, J.4    Hakomori, S.-I.5
  • 6
    • 0025010879 scopus 로고
    • Sugar-nucleotide donor specificity to histo-blood group A and B transferases is based on amino acid substitutions
    • 6. Yamamoto, F.-I. & Hakomori, S. (1990) Sugar-nucleotide donor specificity to histo-blood group A and B transferases is based on amino acid substitutions. J. Biol. Chem. 265, 19257-19262.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19257-19262
    • Yamamoto, F.-I.1    Hakomori, S.2
  • 9
    • 0029960005 scopus 로고    scopus 로고
    • Amino acid residue at codon 268 determines both activity and nucleotide-sugar donor substrate specificity of human histo-blood group A and B transferases
    • 9. Yamamoto, F.-I. & McNeill, P.D. (1996) Amino acid residue at codon 268 determines both activity and nucleotide-sugar donor substrate specificity of human histo-blood group A and B transferases. J. Biol. Chem. 271, 10515-10520.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10515-10520
    • Yamamoto, F.-I.1    McNeill, P.D.2
  • 10
    • 0028824151 scopus 로고
    • Expression of a recombinant human glycosyltransferase from a synthetic gene and its utilization for synthesis of the human blood group B trisaccharide
    • 10. Seto, N.O.L., Palcic, M.M., Hindsgaul, O., Bundle, D.R. & Narang, S.A. (1995) Expression of a recombinant human glycosyltransferase from a synthetic gene and its utilization for synthesis of the human blood group B trisaccharide. Eur. J. Biochem. 234, 323-328.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 323-328
    • Seto, N.O.L.1    Palcic, M.M.2    Hindsgaul, O.3    Bundle, D.R.4    Narang, S.A.5
  • 11
    • 0030922424 scopus 로고    scopus 로고
    • Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes
    • 11. Seto, N.O.L., Palcic, M.M., Compston, C.A., Li, H., Bundle, D.R. & Narang, S.A. (1997) Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes. J. Biol. Chem. 272, 14133-14138.
    • (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
  • 13
    • 0028278660 scopus 로고
    • Detection of 100 molecules of product formed in a fucosyltransferase reaction
    • 13. Zhao, J.Y., Dovichi, N.J., Hindsgaul, O., Gosselin, S. & Palcic, M.M. (1994) Detection of 100 molecules of product formed in a fucosyltransferase reaction. Glycobiology 4, 239-242.
    • (1994) Glycobiology , vol.4 , pp. 239-242
    • Zhao, J.Y.1    Dovichi, N.J.2    Hindsgaul, O.3    Gosselin, S.4    Palcic, M.M.5
  • 14
    • 0026568167 scopus 로고
    • Enzyme-linked immunosorbent assays for the measurement of blood group A and B glycosyltransferase activities
    • 14. Keshvara, L.M., Newton, E.M., Good, A.H., Hindsgaul, O. & Palcic, M.M. (1992) Enzyme-linked immunosorbent assays for the measurement of blood group A and B glycosyltransferase activities. Glycoconjugate J. 9, 16-20.
    • (1992) Glycoconjugate J. , vol.9 , pp. 16-20
    • Keshvara, L.M.1    Newton, E.M.2    Good, A.H.3    Hindsgaul, O.4    Palcic, M.M.5
  • 15
    • 0025688727 scopus 로고
    • A new forced-field program for the calculation of glycopeptides and its application to a heptacosapeptide-decasaccharide of immunoglobulin Gl. Importance of 1-6 glycosidic linkages in carbohydrate-peptide interactions
    • 15. Suike-Prill, R. & Meyer, B. (1991) A new forced-field program for the calculation of glycopeptides and its application to a heptacosapeptide-decasaccharide of immunoglobulin Gl. Importance of 1-6 glycosidic linkages in carbohydrate-peptide interactions. Eur. J. Biochem. 194, 903-919.
    • (1991) Eur. J. Biochem. , vol.194 , pp. 903-919
    • Suike-Prill, R.1    Meyer, B.2
  • 17
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • 17. Evans, S.V. (1993) SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 18
    • 0000390128 scopus 로고    scopus 로고
    • Glycine residues provide flexibility for enzyme active sites
    • 18. Van, B.X. & Sun, Y.Q. (1997) Glycine residues provide flexibility for enzyme active sites. J. Biol. Chem. 272, 3190-3194.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3190-3194
    • Van, B.X.1    Sun, Y.Q.2
  • 19
    • 0031749203 scopus 로고    scopus 로고
    • Sequence-function relationships of prokaryotic and eukaryotic galactosyltransferases
    • 19. Breton, C., Bettler, E., Joziasse, D.H., Geremia, R.A. & 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
  • 20
    • 0027965664 scopus 로고
    • Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • 20. Vrielink, A., Rüger, W., Driessen, H.P.C. & Freemont, P.S. (1994) Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J. 13, 3413-3422.
    • (1994) EMBO J. , vol.13 , pp. 3413-3422
    • Vrielink, A.1    Rüger, W.2    Driessen, H.P.C.3    Freemont, P.S.4
  • 21
    • 0029683858 scopus 로고    scopus 로고
    • Sequence alignment and fold recognition of fucosyltransferases
    • 21. Breton, C., Oriol, R. & Imberty, A. (1996) Sequence alignment and fold recognition of fucosyltransferases. Glycobiology 6, vii-xii.
    • (1996) Glycobiology , vol.6
    • Breton, C.1    Oriol, R.2    Imberty, A.3
  • 22
    • 0027169638 scopus 로고
    • Improved prediction of protein secondary structure by use of sequence profiles and neural networks
    • 22. Rost, B. & Sander, C. (1993) Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc. Natl Acad. Sci. USA 90, 7558-7562.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7558-7562
    • Rost, B.1    Sander, C.2
  • 23
    • 0027477526 scopus 로고
    • Protein classification by stochastic modeling and optimal filtering of amino-acid sequences
    • 23. Stultz, C.M., White, J.V. & Smith, T.F. (1993) Protein classification by stochastic modeling and optimal filtering of amino-acid sequences. Protein Sci. 2, 305-314.
    • (1993) Protein Sci. , vol.2 , pp. 305-314
    • Stultz, C.M.1    White, J.V.2    Smith, T.F.3
  • 24
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by prediction from multiple alignments
    • 24. Geourjon, C. & Deleage, G. (1995) SOPMA: Significant improvements in protein secondary structure prediction by prediction from multiple alignments. Comput. Appl. Biosci. 11, 681-684.
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 25
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • 25. Farber, G.K. & Petsko, G.A. (1990) The evolution of α/β barrel enzymes. Trends Biochem. Sci. 15, 228-234.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.