메뉴 건너뛰기




Volumn 14, Issue 12, 2004, Pages 1295-1302

Roles of active site tryptophans in substrate binding and catalysis by α-1,3 galactosyltransferase

Author keywords

Catalysis; Crystal structure; Glycosyltransferase; Mutation; Substrate binding

Indexed keywords

ALPHA 1,3 GALACTOSYLTRANSFERASE; GALACTOSYLTRANSFERASE; GLYCINE; THREONINE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GALACTOSE;

EID: 9744229199     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwh119     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 0024508511 scopus 로고
    • Immunogenic Gal α 1-3Gal carbohydrate epitopes are present on pathogenic American Trypanosoma and Leishmania
    • Avila, J.L., Rojas, M., and Galili, U. (1989) Immunogenic Gal α 1-3Gal carbohydrate epitopes are present on pathogenic American Trypanosoma and Leishmania. J. Immunol., 142, 2828-2834.
    • (1989) J. Immunol. , vol.142 , pp. 2828-2834
    • Avila, J.L.1    Rojas, M.2    Galili, U.3
  • 2
    • 0035930576 scopus 로고    scopus 로고
    • Structure of UDP complex of UDP-galactose: β-galactoside-α-1,3-galactosyltransferase at 1.53Å resolution reveals a conformational change in the catalytically important C-terminus
    • Boix, E., Swaminathan, G.J., Zhang, Y., Natesh, R., Brew, K., and Acharya, K.R. (2001) Structure of UDP complex of UDP-galactose: β-galactoside-α-1,3-galactosyltransferase at 1.53Å resolution reveals a conformational change in the catalytically important C-terminus. J. Biol. Chem., 276, 48608-48614.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48608-48614
    • Boix, E.1    Swaminathan, G.J.2    Zhang, Y.3    Natesh, R.4    Brew, K.5    Acharya, K.R.6
  • 3
    • 0037008717 scopus 로고    scopus 로고
    • Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase: α-1,3 galactosyltransferase
    • Boix, E., Zhang, Y., Swaminathan, G.J., Brew, K., and Acharya, K.R. (2002) Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase: α-1,3 galactosyltransferase. J. Biol. Chem., 277, 28310-28318.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28310-28318
    • Boix, E.1    Zhang, Y.2    Swaminathan, G.J.3    Brew, K.4    Acharya, K.R.5
  • 5
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for x-ray protein structure refinement
    • Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for x-ray protein structure refinement. Acta Crystallogr. A47, 392-400.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 6
    • 0025773203 scopus 로고
    • Gene sequences suggest inactivation of α-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys
    • Galili, U. and Swanson, K. (1991) Gene sequences suggest inactivation of α-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc. Natl Acad. Sci. USA, 88 7401-7404.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7401-7404
    • Galili, U.1    Swanson, K.2
  • 7
    • 0024297335 scopus 로고
    • Man, apes and old world monkeys differ from other animals in the expression of α-galactosyl epitopes on nucleated cells
    • Galili, U., Shohet, S.B., Kobrin, E., Stults, C.L., and Macher, B.A. (1988) Man, apes and old world monkeys differ from other animals in the expression of α-galactosyl epitopes on nucleated cells. J. Biol. Chem., 263, 17755-17762.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17755-17762
    • Galili, U.1    Shohet, S.B.2    Kobrin, E.3    Stults, C.L.4    Macher, B.A.5
  • 8
    • 0035865381 scopus 로고    scopus 로고
    • Bovine α1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases
    • Gastinel, L.N., Bignon, C., Misra, A.K., Hindsgaul, O., Shaper, J.H., and Joziasse, D.H. (2001) Bovine α1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases. EMBO J., 20, 638-649.
    • (2001) EMBO J. , vol.20 , pp. 638-649
    • Gastinel, L.N.1    Bignon, C.2    Misra, A.K.3    Hindsgaul, O.4    Shaper, J.H.5    Joziasse, D.H.6
  • 9
    • 0029746154 scopus 로고    scopus 로고
    • Expression cloning of Forssman glycolipid synthetase: A novel member of the histo-blood group ABO family
    • Haslam, D.B. and Baenziger, J.U. (1996) Expression cloning of Forssman glycolipid synthetase: a novel member of the histo-blood group ABO family. Proc. Natl Acad. Sci. USA, 93, 10697-10702.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10697-10702
    • Haslam, D.B.1    Baenziger, J.U.2
  • 10
    • 0037718345 scopus 로고    scopus 로고
    • Molecular modeling of glycosyltransferases involved in the biosynthesis of blood group A, blood group B, Forssman, and igb3 antigens and their interaction with substrates
    • Heissigerová, H., Breton, C., Moravcová, and Imberty, A. (2003) Molecular modeling of glycosyltransferases involved in the biosynthesis of blood group A, blood group B, Forssman, and igb3 antigens and their interaction with substrates. Glycobiology, 13, 377-386.
    • (2003) Glycobiology , vol.13 , pp. 377-386
    • Heissigerová, H.1    Breton, C.2    Moravcová, A.3    Imberty, A.4
  • 11
    • 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., and Kjeldgaard M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., A47 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 12
    • 0034682757 scopus 로고    scopus 로고
    • Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids
    • Keusch, J.J., Manzella, S.M., Nyame, K.A., Cummings, R.D., and Baenziger, J.U. (2000) Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids. J. Biol. Chem., 275 25308-25314.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25308-25314
    • Keusch, J.J.1    Manzella, S.M.2    Nyame, K.A.3    Cummings, R.D.4    Baenziger, J.U.5
  • 13
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 14
    • 0036263750 scopus 로고    scopus 로고
    • The importance of CH/pi interactions to the function of carbohydrate binding proteins
    • Muraki, M. (2002) The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept. Lett., 9, 195-209.
    • (2002) Protein Pept. Lett. , vol.9 , pp. 195-209
    • Muraki, M.1
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 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
  • 18
    • 9744229464 scopus 로고    scopus 로고
    • Ordered Bi Bi Enzyme Mechanism
    • Academic Press, San Diego, CA
    • Purich, D.L. and Allison, R.D. (2000) Ordered Bi Bi Enzyme Mechanism. In Handbook of Biochemical Kinetics. Academic Press, San Diego, CA, pp 524-525.
    • (2000) Handbook of Biochemical Kinetics , pp. 524-525
    • Purich, D.L.1    Allison, R.D.2
  • 19
    • 0033083847 scopus 로고    scopus 로고
    • Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli
    • Seto, N.O.L., Compston, C.A., Evans, S.V., Bundle, D.R., Narang, S.A., and Palcic, M.M. (1999) Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli. Eur J. Biochem., 259, 770-775.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 770-775
    • Seto, N.O.L.1    Compston, C.A.2    Evans, S.V.3    Bundle, D.R.4    Narang, S.A.5    Palcic, M.M.6
  • 20
    • 0034951022 scopus 로고    scopus 로고
    • The structural basis for carbohydrate recognition by lectins
    • Sharon, N. and Lis, H. (2001) The structural basis for carbohydrate recognition by lectins. Adv. Exp. Med. Biol., 491 1-16.
    • (2001) Adv. Exp. Med. Biol. , vol.491 , pp. 1-16
    • Sharon, N.1    Lis, H.2
  • 21
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High resolution refinement
    • Sheldrick, G.M. and Schneider, T.R. (1997) SHELXL: high resolution refinement. Methods Enzymol., 277, 319-343.
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 23
    • 0021104749 scopus 로고
    • Identification and characterization of an UDP-gal: N-acetyllactosaminide α1,3-D-galactosyltransferase in calf thymus
    • van den Eijnden, D.H., Blanken, W.M., Winterwerp, H., and Schiphorst, W.E.C.M. (1983) Identification and characterization of an UDP-gal: N-acetyllactosaminide α1,3-D-galactosyltransferase in calf thymus. Eur J. Biochem., 134, 523-530.
    • (1983) Eur J. Biochem. , vol.134 , pp. 523-530
    • van den Eijnden, D.H.1    Blanken, W.M.2    Winterwerp, H.3    Schiphorst, W.E.C.M.4
  • 24
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weiss, W.I. and Drickamer, K. (1996) Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem., 65, 441-473.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 441-473
    • Weiss, W.I.1    Drickamer, K.2
  • 25
    • 0025270738 scopus 로고
    • Molecular genetic basis of the histo-blood group ABO system
    • Yamamato, F.-I., Clausen, H., White, T., Marken, J., and Hakamori, S.-I. (1990) Molecular genetic basis of the histo-blood group ABO system. Nature, 345, 229-233.
    • (1990) Nature , vol.345 , pp. 229-233
    • Yamamato, F.-I.1    Clausen, H.2    White, T.3    Marken, J.4    Hakamori, S.-I.5
  • 26
    • 0035853670 scopus 로고    scopus 로고
    • Specificity and mechanism of metal ion activation in UDP-galactose β-galactoside α-1,3-galactosyltransferase
    • Zhang, Y., Wang, P.G., and Brew, K. (2001) Specificity and mechanism of metal ion activation in UDP-galactose β-galactoside α-1,3-galactosyltransferase. J. Biol. Chem., 276, 11567-11574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11567-11574
    • Zhang, Y.1    Wang, P.G.2    Brew, K.3
  • 27
    • 0345254937 scopus 로고    scopus 로고
    • Roles of individual enzyme-substrate interactions by α-1,3 galactosyltransferase in catalysis and specificity
    • Zhang, Y., Swaminanthan, G.J., Deshpande, A., Natesh, R., Boix, E., Xie, Z., Acharya, K.R., and Brew, K. (2003) Roles of individual enzyme-substrate interactions by α-1,3 galactosyltransferase in catalysis and specificity. Biochemistry, 42, 13512-13521.
    • (2003) Biochemistry , vol.42 , pp. 13512-13521
    • Zhang, Y.1    Swaminanthan, G.J.2    Deshpande, A.3    Natesh, R.4    Boix, E.5    Xie, Z.6    Acharya, K.R.7    Brew, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.