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Volumn 20, Issue 8, 2013, Pages 856-863

Polysaccharide-synthesizing glycosyltransferases and carbohydrate binding modules: The case of starch synthase III

Author keywords

Carbohydrate binding modules; Enzymes; Glycosyltransferases; Starch; Starch binding domains; Starch synthase

Indexed keywords

GLYCOSYLTRANSFERASE; GLYCOSYLTRANSFERASE A; GLYCOSYLTRANSFERASE B; GLYCOSYLTRANSFERASE C; POLYSACCHARIDE; STARCH SYNTHASE; STARCH SYNTHASE III; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; GLUCOSYLTRANSFERASE; PROTEIN BINDING; STARCH; STARCH SYNTHASE III, ARABIDOPSIS;

EID: 84882298772     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866511320080003     Document Type: Article
Times cited : (17)

References (82)
  • 2
    • 0000615043 scopus 로고
    • Isolation of the coenzyme of the galactose phosphate-glucose phosphate transformation
    • Caputto, R.; Leloir, L.F.; Cardini, C.E.; Paladini, A.C. Isolation of the coenzyme of the galactose phosphate-glucose phosphate transformation. J. Biol. Chem., 1950, 184, 333-350.
    • (1950) J. Biol. Chem. , vol.184 , pp. 333-350
    • Caputto, R.1    Leloir, L.F.2    Cardini, C.E.3    Paladini, A.C.4
  • 3
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymatic glycosyl transfer
    • Sinnott, M.L. Catalytic mechanisms of enzymatic glycosyl transfer. Chem. Rev., 1990, 90, 1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 4
    • 0034838654 scopus 로고    scopus 로고
    • Structural and functional features of glycosyltransferases
    • Breton, C.; Mucha, J.; Jeanneau, C. Structural and functional features of glycosyltransferases. Biochimie, 2001, 83, 713-718.
    • (2001) Biochimie , vol.83 , pp. 713-718
    • Breton, C.1    Mucha, J.2    Jeanneau, C.3
  • 5
    • 0033787822 scopus 로고    scopus 로고
    • Glycosyltransferase structure and mechanism
    • Unligil, U.M.; Rini, J.M. Glycosyltransferase structure and mechanism. Curr. Opin. Struct. Biol, 2000, 10, 510-517.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 510-517
    • Unligil, U.M.1    Rini, J.M.2
  • 6
    • 0035443118 scopus 로고    scopus 로고
    • Glycoside hydrolases and glycosyltransferases: Families and functional modules
    • Bourne, Y.; Henrissat, B. Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr. Opin. Struct. Biol., 2001, 11, 593-600.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 593-600
    • Bourne, Y.1    Henrissat, B.2
  • 7
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphosphosugar transferase, spsa from bacillus subtilis, in native and nucleotide-complexed forms
    • Charnock, S.J.; Davies, G.J. Structure of the nucleotide-diphosphosugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry, 1999, 38, 6380-6385.
    • (1999) Biochemistry , vol.38 , pp. 6380-6385
    • Charnock, S.J.1    Davies, G.J.2
  • 8
    • 0035824876 scopus 로고    scopus 로고
    • Three-dimensional structures of the mn and mg dtdp complexes of the family gt-2 glycosyltransferase spsa: A comparison with related ndp-sugar glycosyltransferases
    • Tarbouriech, N.; Charnock, S.J.; Davies, G.J. Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT.-2 glycosyltransferase SpsA: a comparison with related NDP.-sugar glycosyltransferases. J. Mol. Biol., 2001, 314, 655-661.
    • (2001) J. Mol. Biol. , vol.314 , pp. 655-661
    • Tarbouriech, N.1    Charnock, S.J.2    Davies, G.J.3
  • 9
    • 0027965664 scopus 로고
    • Crystal structure of the dna modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • Vrielink, A.; Ruger, W.; Driessen, H.P.; Freemont, P.S. Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J., 1994, 13, 3413-3422.
    • (1994) EMBO J. , vol.13 , pp. 3413-3422
    • Vrielink, A.1    Ruger, W.2    Driessen, H.P.3    Freemont, P.S.4
  • 10
    • 4444373841 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase: Homologous enzymes catalyze glycogen synthesis and degradation
    • Buschiazzo, A.; Ugalde, J.E.; Guerin, M.E.; Shepard, W.; Ugalde, R.A.; Alzari, P.M. Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation. EMBO J., 2004, 23, 3196-3205.
    • (2004) EMBO J. , vol.23 , pp. 3196-3205
    • Buschiazzo, A.1    Ugalde, J.E.2    Guerin, M.E.3    Shepard, W.4    Ugalde, R.A.5    Alzari, P.M.6
  • 11
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho, P.M.; Deleury, E.; Davies, G.J.; Henrissat, B. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol., 2003, 328, 307-317.
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 12
    • 0038309565 scopus 로고    scopus 로고
    • Three monophyletic superfamilies account for the majority of the known glycosyltransferases
    • Liu, J.; Mushegian, A. Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci., 2003, 12, 1418-1431.
    • (2003) Protein Sci. , vol.12 , pp. 1418-1431
    • Liu, J.1    Mushegian, A.2
  • 13
    • 38049051311 scopus 로고    scopus 로고
    • Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
    • Igura, M.; Maita, N.; Kamishikiryo, J.; Yamada, M.; Obita, T.; Maenaka, K.; Kohda, D. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J., 2008, 27, 234-243.
    • (2008) EMBO J. , vol.27 , pp. 234-243
    • Igura, M.1    Maita, N.2    Kamishikiryo, J.3    Yamada, M.4    Obita, T.5    Maenaka, K.6    Kohda, D.7
  • 14
    • 79952211396 scopus 로고    scopus 로고
    • The c-Terminal domain of the arabinosyltransferase mycobacterium tuberculosis embc is a lectin-like carbohydrate binding module
    • Alderwick, L.J.; Lloyd, G.S.; Ghadbane, H.; May, J.W.; Bhatt, A.; Eggeling, L.; Futterer, K.; Besra, G.S. The C.-Terminal domain of the Arabinosyltransferase Mycobacterium tuberculosis EmbC is a lectin-like carbohydrate binding module. PLoS Pathog., 2011, 7, e1001299.
    • (2011) PLoS Pathog. , vol.7
    • Alderwick, L.J.1    Lloyd, G.S.2    Ghadbane, H.3    May, J.W.4    Bhatt, A.5    Eggeling, L.6    Futterer, K.7    Besra, G.S.8
  • 16
    • 79958835264 scopus 로고    scopus 로고
    • Expression purification and biochemical characterization of gumi, a monotopic membrane gdp-mannose: Glycolipid 4-dmannosyltransferase from xanthomonas campestris pv Campestris
    • Salinas, S.R.; Bianco, M.I.; Barreras, M.; Ielpi, L. Expression, purification and biochemical characterization of GumI, a monotopic membrane GDP.-mannose:glycolipid 4-Dmannosyltransferase from Xanthomonas campestris pv. campestris. Glycobiology, 2011, 21, 903-913.
    • (2011) Glycobiology , vol.21 , pp. 903-913
    • Salinas, S.R.1    Bianco, M.I.2    Barreras, M.3    Ielpi, L.4
  • 17
    • 2942524078 scopus 로고    scopus 로고
    • Chitobiose phosphorylase from vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan gh-l-like (/) barrel fold
    • Hidaka, M.; Honda, Y.; Kitaoka, M.; Nirasawa, S.; Hayashi, K.; Wakagi, T.; Shoun, H.; Fushinobu, S. Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH.-L.-like (/) barrel fold. Structure, 2004, 12, 937-947.
    • (2004) Structure , vol.12 , pp. 937-947
    • Hidaka, M.1    Honda, Y.2    Kitaoka, M.3    Nirasawa, S.4    Hayashi, K.5    Wakagi, T.6    Shoun, H.7    Fushinobu, S.8
  • 18
    • 0026027728 scopus 로고
    • Structure of cyclodextrin glycosyltransferase refined at 2.0 a resolution
    • Klein, C.; Schulz, G.E. Structure of cyclodextrin glycosyltransferase refined at 2.0 A resolution. J. Mol. Biol., 1991, 217, 737-750.
    • (1991) J. Mol. Biol. , vol.217 , pp. 737-750
    • Klein, C.1    Schulz, G.E.2
  • 19
    • 0026744021 scopus 로고
    • Catalytic center of cyclodextrin glycosyltransferase derived from x-ray structure analysis combined with site-directed mutagenesis
    • Klein, C.; Hollender, J.; Bender, H.; Schulz, G.E. Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis. Biochemistry, 1992, 31, 8740-8746.
    • (1992) Biochemistry , vol.31 , pp. 8740-8746
    • Klein, C.1    Hollender, J.2    Bender, H.3    Schulz, G.E.4
  • 20
    • 0024277381 scopus 로고
    • Studies of the cellulolytic system of trichoderma reesei qm 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis
    • Tomme, P.; Van Tilbeurgh, H.; Pettersson, G.; Van Damme, J.; Vandekerckhove, J.; Knowles, J.; Teeri, T.; Claeyssens, M. Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. Eur. J. Biochem., 1988, 170, 575-581.
    • (1988) Eur. J. Biochem. , vol.170 , pp. 575-581
    • Tomme, P.1    Van Tilbeurgh, H.2    Pettersson, G.3    Van Damme, J.4    Vandekerckhove, J.5    Knowles, J.6    Teeri, T.7    Claeyssens, M.8
  • 21
    • 0024297010 scopus 로고
    • Precise excision of the cellulose binding domains from two cellulomonas fimi cellulases by a homologous protease and the effect on catalysis
    • Gilkes, N.R.; Warren, R.A.; Miller, Jr. R.C.; Kilburn, D.G. Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J. Biol. Chem., 1988, 263, 10401-10407.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10401-10407
    • Gilkes, N.R.1    Warren, R.A.2    Miller Jr., R.C.3    Kilburn, D.G.4
  • 22
    • 33745161547 scopus 로고    scopus 로고
    • Carbohydrate binding modules: Biochemical properties and novel applications
    • Shoseyov, O.; Shani, Z.; Levy, I. Carbohydrate binding modules: biochemical properties and novel applications. Microbiol. Mol. Biol. Rev., 2006, 70, 283-295.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 283-295
    • Shoseyov, O.1    Shani, Z.2    Levy, I.3
  • 23
    • 27644529698 scopus 로고    scopus 로고
    • A new clan of cbm families based on bioinformatics of starch-binding domains from families cbm20 and cbm21
    • Machovic, M.; Svensson, B.; MacGregor, E.A.; Janecek, S. A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21. FEBS J., 2005, 272, 5497-54513.
    • (2005) FEBS J. , vol.272 , pp. 5497-54513
    • Machovic, M.1    Svensson, B.2    MacGregor, E.A.3    Janecek, S.4
  • 24
    • 33845498615 scopus 로고    scopus 로고
    • Starch-binding domains in the postgenome era
    • Machovic, M.; Janecek, S. Starch-binding domains in the postgenome era. Cell Mol. Life Sci., 2006, 63, 2710-2724.
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 2710-2724
    • Machovic, M.1    Janecek, S.2
  • 25
    • 33750979827 scopus 로고    scopus 로고
    • The evolution of putative starch-binding domains
    • Machovic, M.; Janecek, S. The evolution of putative starch-binding domains. FEBS Lett., 2006, 580, 6349-6356.
    • (2006) FEBS Lett. , vol.580 , pp. 6349-6356
    • Machovic, M.1    Janecek, S.2
  • 26
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-Tuning polysaccharide recognition
    • Boraston, A.B.; Bolam, D.N.; Gilbert, H.J.; Davies, G.J. Carbohydrate-binding modules: fine-Tuning polysaccharide recognition. Biochem. J., 2004, 382, 769-781.
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 27
    • 0032478833 scopus 로고    scopus 로고
    • Cdna cloning and expression of a family of udp-n-Acetyl-d-galactosamine: Polypeptide n-Acetylgalactosaminyltransferase sequence homologs from caenorhabditis elegans
    • Hagen, F.K.; Nehrke, K. cDNA cloning and expression of a family of UDP.-N.-Acetyl-D.-galactosamine:polypeptide N.-Acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans. J. Biol. Chem., 1998, 273, 8268-8277.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8268-8277
    • Hagen, F.K.1    Nehrke, K.2
  • 28
    • 33646828699 scopus 로고    scopus 로고
    • Dynamic association between the catalytic and lectin domains of human udp-galnac: Polypeptide alpha-n-Acetylgalactosaminyltransferase-2
    • Fritz, T.A.; Raman, J.; Tabak, L.A. Dynamic association between the catalytic and lectin domains of human UDP.-GalNAc: polypeptide alpha-N.-Acetylgalactosaminyltransferase-2. J. Biol. Chem., 2006, 281, 8613-8619.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8613-8619
    • Fritz, T.A.1    Raman, J.2    Tabak, L.A.3
  • 29
    • 0036181524 scopus 로고    scopus 로고
    • Characterization of an archaeal cyclodextrin glucanotransferase with a novel c-Terminal domain
    • Rashid, N.; Cornista, J.; Ezaki, S.; Fukui, T.; Atomi, H.; Imanaka, T. Characterization of an archaeal cyclodextrin glucanotransferase with a novel C.-Terminal domain. J. Bacteriol., 2002, 184, 777-784.
    • (2002) J. Bacteriol. , vol.184 , pp. 777-784
    • Rashid, N.1    Cornista, J.2    Ezaki, S.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 31
    • 57649240496 scopus 로고    scopus 로고
    • Structure-function relationship in cyclodextrin glycosyltransferase from bacillus circulans df 9r
    • Costa, H.; del Canto, S.; Ferrarotti, S.; de Jimenez Bonino, M.B. Structure-function relationship in cyclodextrin glycosyltransferase from Bacillus circulans DF 9R. Carbohydr. Res., 2009, 344, 74-79.
    • (2009) Carbohydr. Res. , vol.344 , pp. 74-79
    • Costa, H.1    Del Canto, S.2    Ferrarotti, S.3    De Jimenez Bonino, M.B.4
  • 32
    • 1642416044 scopus 로고    scopus 로고
    • A cytosolic glucosyltransferase is required for conversion of starch to sucrose in arabidopsis leaves at night
    • Chia, T.; Thorneycroft, D.; Chapple, A.; Messerli, G.; Chen, J.; Zeeman, S.C.; Smith, S.M.; Smith, A.M. A cytosolic glucosyltransferase is required for conversion of starch to sucrose in Arabidopsis leaves at night. Plant J., 2004, 37, 853-863.
    • (2004) Plant J. , vol.37 , pp. 853-863
    • Chia, T.1    Thorneycroft, D.2    Chapple, A.3    Messerli, G.4    Chen, J.5    Zeeman, S.C.6    Smith, S.M.7    Smith, A.M.8
  • 35
    • 40149108056 scopus 로고    scopus 로고
    • Role of the n-Terminal starch-binding domains in the kinetic properties of starch synthase iii from arabidopsis thaliana
    • Valdez, H.A.; Busi, M.V.; Wayllace, N.Z.; Parisi, G.; Ugalde, R.A.; Gomez-Casati, D.F. Role of the N.-Terminal starch-binding domains in the kinetic properties of starch synthase III from Arabidopsis thaliana. Biochemistry, 2008, 47, 3026-3032.
    • (2008) Biochemistry , vol.47 , pp. 3026-3032
    • Valdez, H.A.1    Busi, M.V.2    Wayllace, N.Z.3    Parisi, G.4    Ugalde, R.A.5    Gomez-Casati, D.F.6
  • 37
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-iii cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo, J.; Lamed, R.; Chirino, A.J.; Morag, E.; Bayer, E.A.; Shoham, Y.; Steitz, T.A. Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J., 1996, 15, 5739-5751.
    • (1996) EMBO J. , vol.15 , pp. 5739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morag, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 39
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of aspergillus niger glucoamylase bound to betacyclodextrin
    • Sorimachi, K.; Le Gal-Coeffet, M.F.; Williamson, G.; Archer, D.B.; Williamson, M.P. Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to betacyclodextrin. Structure, 1997, 5, 647-661.
    • (1997) Structure , vol.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffet, M.F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 40
    • 80054683038 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals
    • Janecek, S.; Svensson, B.; MacGregor, E.A. Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enzyme Microb. Technol., 2011, 49, 429-440.
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 429-440
    • Janecek, S.1    Svensson, B.2    MacGregor, E.A.3
  • 42
    • 33846113064 scopus 로고    scopus 로고
    • Recent structural studies of carbohydrate-binding modules
    • Hashimoto, H. Recent structural studies of carbohydrate-binding modules. Cell Mol. Life Sci., 2006, 63, 2954-2967.
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 2954-2967
    • Hashimoto, H.1
  • 44
    • 26944490008 scopus 로고    scopus 로고
    • Mutations affecting starch synthase iii in arabidopsis alter leaf starch structure and increase the rate of starch synthesis
    • Zhang, X.; Myers, A.M.; James, M.G. Mutations affecting starch synthase III in Arabidopsis alter leaf starch structure and increase the rate of starch synthesis. Plant Physiol., 2005, 138, 663-674.
    • (2005) Plant Physiol. , vol.138 , pp. 663-674
    • Zhang, X.1    Myers, A.M.2    James, M.G.3
  • 45
    • 77952466937 scopus 로고    scopus 로고
    • Starch: Its metabolism, evolution, and biotechnological modification in plants
    • Zeeman, S.C.; Kossmann, J.; Smith, A.M. Starch: its metabolism, evolution, and biotechnological modification in plants. Annu. Rev. Plant Biol., 2010, 61, 209-234.
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 209-234
    • Zeeman, S.C.1    Kossmann, J.2    Smith, A.M.3
  • 47
    • 0034089676 scopus 로고    scopus 로고
    • The structure and expression of the wheat starch synthase iii gene. Motifs in the expressed gene define the lineage of the starch synthase iii gene family
    • Li, Z.; Mouille, G.; Kosar-Hashemi, B.; Rahman, S.; Clarke, B.; Gale, K.R.; Appels, R.; Morell, M.K. The structure and expression of the wheat starch synthase III gene. Motifs in the expressed gene define the lineage of the starch synthase III gene family. Plant Physiol., 2000, 123, 613-624.
    • (2000) Plant Physiol. , vol.123 , pp. 613-624
    • Li, Z.1    Mouille, G.2    Kosar-Hashemi, B.3    Rahman, S.4    Clarke, B.5    Gale, K.R.6    Appels, R.7    Morell, M.K.8
  • 49
    • 74549189480 scopus 로고    scopus 로고
    • The starch-binding capacity of the noncatalytic sbd2 region and the interaction between the n-And c-Terminal domains are involved in the modulation of the activity of starch synthase iii from arabidopsis thaliana
    • Wayllace, N.Z.; Valdez, H.A.; Ugalde, R.A.; Busi, M.V.; Gomez-Casati, D.F. The starch-binding capacity of the noncatalytic SBD2 region and the interaction between the N.-And C.-Terminal domains are involved in the modulation of the activity of starch synthase III from Arabidopsis thaliana. FEBS J., 2010, 277, 428-440.
    • (2010) FEBS J. , vol.277 , pp. 428-440
    • Wayllace, N.Z.1    Valdez, H.A.2    Ugalde, R.A.3    Busi, M.V.4    Gomez-Casati, D.F.5
  • 50
    • 80051514068 scopus 로고    scopus 로고
    • Preferential binding of sbd from arabidopsis thaliana ssiii to polysaccharides. Study of amino acid residues involved
    • Valdez, H.A.; Peralta, D.A.; Wayllace, N.Z.; Grisolía, M.J.; Gomez-Casati, D.F.; Busi, M.V. Preferential binding of SBD from Arabidopsis thaliana SSIII to polysaccharides. Study of amino acid residues involved. Starch/Stärke, 2011, 63, 451-460.
    • (2011) Starch/Stärke , vol.63 , pp. 451-460
    • Valdez, H.A.1    Peralta, D.A.2    Wayllace, N.Z.3    Grisolía, M.J.4    Gomez-Casati, D.F.5    Busi, M.V.6
  • 51
    • 0041422391 scopus 로고    scopus 로고
    • Structure of the tdp-epi-vancosaminyltransferase gtfa from the chloroeremomycin biosynthetic pathway
    • Mulichak, A.M.; Losey, H.C.; Lu, W.; Wawrzak, Z.; Walsh, C.T.; Garavito, R.M. Structure of the TDP.-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway. Proc. Natl. Acad. Sci. USA, 2003, 100, 9238-9243.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9238-9243
    • Mulichak, A.M.1    Losey, H.C.2    Lu, W.3    Wawrzak, Z.4    Walsh, C.T.5    Garavito, R.M.6
  • 53
    • 80053917641 scopus 로고    scopus 로고
    • The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications
    • Zheng, Y.; Anderson, S.; Zhang, Y.; Garavito, R.M. The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. J. Biol. Chem., 2011, 286, 36108-36118.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36108-36118
    • Zheng, Y.1    Anderson, S.2    Zhang, Y.3    Garavito, R.M.4
  • 54
    • 0035865381 scopus 로고    scopus 로고
    • Bovine.1,3-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.; Joziasse, D.H. Bovine.1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases. EMBO J., 2001, 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
  • 55
    • 77952024581 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of drosophila.1, 4-galactosyltransferase-7
    • Ramakrishnan, B.; Qasba, P.K. Crystal structure of the catalytic domain of Drosophila.1,4-Galactosyltransferase-7. J. Biol. Chem., 2010, 285, 15619-15626.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15619-15626
    • Ramakrishnan, B.1    Qasba, P.K.2
  • 56
    • 84855502662 scopus 로고    scopus 로고
    • Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis
    • Chaikuad, A.; Froese, D.S.; Berridge, G.; von Delft, F.; Oppermann, U.; Yue, W.W. Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis. Proc. Natl. Acad. Sci. USA, 2011, 108, 21028-21033.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 21028-21033
    • Chaikuad, A.1    Froese, D.S.2    Berridge, G.3    Von Delft, F.4    Oppermann, U.5    Yue, W.W.6
  • 57
    • 0034675845 scopus 로고    scopus 로고
    • X-ray crystal structure of rabbit nacetylglucosaminyltransferase i: Catalytic mechanism and a new protein superfamily
    • Unligil, U.M.; Zhou, S.; Yuwaraj, S.; Sarkar, M.; Schachter, H.; Rini, J.M. X-ray crystal structure of rabbit Nacetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily. EMBO J., 2000, 19, 5269-5280.
    • (2000) EMBO J. , vol.19 , pp. 5269-5280
    • Unligil, U.M.1    Zhou, S.2    Yuwaraj, S.3    Sarkar, M.4    Schachter, H.5    Rini, J.M.6
  • 58
    • 33748756443 scopus 로고    scopus 로고
    • X-ray crystal structure of leukocyte type core 2 beta1, 6-n-Acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism
    • Pak, J.E.; Arnoux, P.; Zhou, S.; Sivarajah, P.; Satkunarajah, M.; Xing, X.; Rini, J.M. X-ray crystal structure of leukocyte type core 2 beta1,6-N.-Acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism. J. Biol. Chem., 2006, 281, 26693-26701.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26693-26701
    • Pak, J.E.1    Arnoux, P.2    Zhou, S.3    Sivarajah, P.4    Satkunarajah, M.5    Xing, X.6    Rini, J.M.7
  • 59
    • 2342420346 scopus 로고    scopus 로고
    • Structure of kre2p/mnt1p: A yeast.1, 2-mannosyltransferase involved in mannoprotein biosynthesis
    • Lobsanov, Y.D.; Romero, P.A.; Sleno, B.; Yu, B.; Yip, P.; Herscovics, A.; Howell, P.L. Structure of Kre2p/Mnt1p: a yeast.1,2-mannosyltransferase involved in mannoprotein biosynthesis. J. Biol. Chem., 2004, 279, 17921-17931.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17921-17931
    • Lobsanov, Y.D.1    Romero, P.A.2    Sleno, B.3    Yu, B.4    Yip, P.5    Herscovics, A.6    Howell, P.L.7
  • 60
    • 0036909547 scopus 로고    scopus 로고
    • Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase otsa
    • Gibson, R.P.; Turkenburg, J.P.; Charnock, S.J.; Lloyd, R.; Davies, G.J. Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA. Chem. Biol., 2002, 9, 1337-1346.
    • (2002) Chem. Biol. , vol.9 , pp. 1337-1346
    • Gibson, R.P.1    Turkenburg, J.P.2    Charnock, S.J.3    Lloyd, R.4    Davies, G.J.5
  • 61
    • 35348893812 scopus 로고    scopus 로고
    • High-resolution structure of nodz fucosyltransferase involved in the biosynthesis of the nodulation factor
    • Brzezinski, K.; Stepkowski, T.; Panjikar, S.; Bujacz, G.; Jaskolski, M. High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor. Acta Biochim. Pol., 2007, 54, 537-549.
    • (2007) Acta Biochim. Pol. , vol.54 , pp. 537-549
    • Brzezinski, K.1    Stepkowski, T.2    Panjikar, S.3    Bujacz, G.4    Jaskolski, M.5
  • 62
    • 0033623762 scopus 로고    scopus 로고
    • The 1.9 a crystal structure of escherichia coli murg, a membrane-Associated glycosyltransferase involved in peptidoglycan biosynthesis
    • Ha, S.; Walker, D.; Shi, Y.; Walker, S. The 1.9 A crystal structure of Escherichia coli MurG, a membrane-Associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci., 2000, 9, 1045-1052.
    • (2000) Protein Sci. , vol.9 , pp. 1045-1052
    • Ha, S.1    Walker, D.2    Shi, Y.3    Walker, S.4
  • 65
    • 33749526524 scopus 로고    scopus 로고
    • Structural insights into the notch-modifying glycosyltransferase fringe
    • Jinek, M.; Chen, Y.W.; Clausen, H.; Cohen, S.M.; Conti, E. Structural insights into the Notch-modifying glycosyltransferase Fringe. Nat. Struct. Mol. Biol., 2006, 13, 945-956.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 945-956
    • Jinek, M.1    Chen, Y.W.2    Clausen, H.3    Cohen, S.M.4    Conti, E.5
  • 66
    • 0031956876 scopus 로고    scopus 로고
    • The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 a resolution and 100 k: The role of the water structure and its contribution to binding
    • Gregoriou, M.; Noble, M.E.; Watson, K.A.; Garman, E.F.; Krulle, T.M.; de la Fuente, C.; Fleet, G.W.; Oikonomakos, N.G.; Johnson, L.N. The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding. Protein Sci., 1998, 7, 915-927.
    • (1998) Protein Sci. , vol.7 , pp. 915-927
    • Gregoriou, M.1    Noble, M.E.2    Watson, K.A.3    Garman, E.F.4    Krulle, T.M.5    De La Fuente, C.6    Fleet, G.W.7    Oikonomakos, N.G.8    Johnson, L.N.9
  • 67
    • 80055095714 scopus 로고    scopus 로고
    • Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein
    • Kawai, F.; Grass, S.; Kim, Y.; Choi, K.J.; St Geme, J.W.; Yeo, H.J. Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C.-like protein. J. Biol. Chem., 2011, 286, 38546-38557.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38546-38557
    • Kawai, F.1    Grass, S.2    Kim, Y.3    Choi, K.J.4    St Geme, J.W.5    Yeo, H.J.6
  • 68
    • 34250829050 scopus 로고    scopus 로고
    • Structural analysis of the-2,3-sialyltransferase cst-i from campylobacter jejuni in apo and substrate-Analogue bound forms
    • Chiu, C.P.; Lairson, L.L.; Gilbert, M.; Wakarchuk, W.W.; Withers, S.G.; Strynadka, N.C. Structural analysis of the-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-Analogue bound forms. Biochemistry, 2007, 46, 7196-7204.
    • (2007) Biochemistry , vol.46 , pp. 7196-7204
    • Chiu, C.P.1    Lairson, L.L.2    Gilbert, M.3    Wakarchuk, W.W.4    Withers, S.G.5    Strynadka, N.C.6
  • 69
    • 0034602394 scopus 로고    scopus 로고
    • Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I
    • Pedersen, L.C.; Tsuchida, K.; Kitagawa, H.; Sugahara, K.; Darden, T.A.; Negishi, M. Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. J. Biol. Chem., 2000, 275, 34580-34585.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34580-34585
    • Pedersen, L.C.1    Tsuchida, K.2    Kitagawa, H.3    Sugahara, K.4    Darden, T.A.5    Negishi, M.6
  • 73
    • 0012784535 scopus 로고    scopus 로고
    • Crystal structure of an alpha 1,4-n-Acetylhexosaminyltransferase (extl2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
    • Pedersen, L.C.; Dong, J.; Taniguchi, F.; Kitagawa, H.; Krahn, J.M.; Pedersen, L.G.; Sugahara, K.; Negishi, M. Crystal structure of an alpha 1,4-N.-Acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. J. Biol. Chem., 2003, 278, 14420-14428.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14420-14428
    • Pedersen, L.C.1    Dong, J.2    Taniguchi, F.3    Kitagawa, H.4    Krahn, J.M.5    Pedersen, L.G.6    Sugahara, K.7    Negishi, M.8
  • 75
    • 84861400022 scopus 로고    scopus 로고
    • Crystal structure of the cterminal globular domain of oligosaccharyltransferase from archaeoglobus fulgidus at 1.75 a resolution
    • Matsumoto, S.; Igura, M.; Nyirenda, J.; Matsumoto, M.; Yuzawa, S.; Noda, N.; Inagaki, F.; Kohda, D. Crystal structure of the Cterminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 A resolution. Biochemistry, 2012, 51, 4157-4166.
    • (2012) Biochemistry , vol.51 , pp. 4157-4166
    • Matsumoto, S.1    Igura, M.2    Nyirenda, J.3    Matsumoto, M.4    Yuzawa, S.5    Noda, N.6    Inagaki, F.7    Kohda, D.8
  • 76
    • 84864149706 scopus 로고    scopus 로고
    • Structure of human pofut2: Insights into thrombospondin type 1 repeat fold and o-fucosylation
    • Chen, C.I.; Keusch, J.J.; Klein, D.; Hess, D.; Hofsteenge, J.; Gut, H. Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O.-fucosylation. EMBO J., 2012, 31, 3183-3197.
    • (2012) EMBO J. , vol.31 , pp. 3183-3197
    • Chen, C.I.1    Keusch, J.J.2    Klein, D.3    Hess, D.4    Hofsteenge, J.5    Gut, H.6
  • 77
    • 53249107961 scopus 로고    scopus 로고
    • Structure and mechanism of gumk, a membrane-Associated glucuronosyltransferase
    • Barreras, M.; Salinas, S.R.; Abdian, P.L.; Kampel, M.A.; Ielpi, L. Structure and mechanism of GumK, a membrane-Associated glucuronosyltransferase. J. Biol. Chem., 2008, 283, 25027-25035.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25027-25035
    • Barreras, M.1    Salinas, S.R.2    Abdian, P.L.3    Kampel, M.A.4    Ielpi, L.5
  • 78
    • 23944471080 scopus 로고    scopus 로고
    • Structural evidence of a passive base-flipping mechanism for agt, an unusual gt-b glycosyltransferase
    • Lariviere, L.; Sommer, N.; Morera, S. Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT.-B glycosyltransferase. J. Mol. Biol., 2005, 352, 139-150.
    • (2005) J. Mol. Biol. , vol.352 , pp. 139-150
    • Lariviere, L.1    Sommer, N.2    Morera, S.3
  • 80
    • 34249674955 scopus 로고    scopus 로고
    • Crystal structures of pasteurella multocida sialyltransferase complexes with acceptor and donor analogues reveal substrate binding sites and catalytic mechanism
    • Ni, L.; Chokhawala, H.A.; Cao, H.; Henning, R.; Ng, L.; Huang, S.; Yu, H.; Chen, X.; Fisher, A.J. Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogues reveal substrate binding sites and catalytic mechanism. Biochemistry, 2007, 46, 6288-6298.
    • (2007) Biochemistry , vol.46 , pp. 6288-6298
    • Ni, L.1    Chokhawala, H.A.2    Cao, H.3    Henning, R.4    Ng, L.5    Huang, S.6    Yu, H.7    Chen, X.8    Fisher, A.J.9
  • 81
    • 56649112704 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: Structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis
    • Pereira, P.J.; Empadinhas, N.; Albuquerque, L.; Sa-Moura, B.; da Costa, M.S.; Macedo-Ribeiro, S. Mycobacterium tuberculosis glucosyl-3-phosphoglycerate synthase: structure of a key enzyme in methylglucose lipopolysaccharide biosynthesis. PLoS ONE, 2008, 3, e3748.
    • (2008) PLoS ONE , vol.3
    • Pereira, P.J.1    Empadinhas, N.2    Albuquerque, L.3    Sa-Moura, B.4    Da Costa, M.S.5    Macedo-Ribeiro, S.6


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