Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1728 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_149557,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_423128,IEDB_461720,IEDB_983930,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_86,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1730 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153530,IEDB_190606,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1752 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1754 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153530,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1755 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_73,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1757 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153530,IEDB_164174,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_73,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1759 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153530,IEDB_164174,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_73,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1761 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_115136,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_140630,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_143794,IEDB_144983,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_423153,IEDB_983930,SB_137,SB_165,SB_166,SB_187,SB_195,SB_29,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 94
  Gamian A, Katzenellenbogen E, Romanowska E, Fernandez JMG, Pedersen C, Ulrich J, Defaye J "Structure of the Hafnia alvei strain PCM 1188 O-specific polysaccharide" - Carbohydrate Research 277 (1995) 245-255
  

  The lipopolysaccharide was extracted from cells of Hafnia alvei PCM 1188 strain and, after mild acid hydrolysis, the O-specific polysaccharide isolated and characterized. On the basis of sugar and methylation analysis, FAB mass spectrometry and NMR spectroscopy of the polysaccharide and oligosaccharides obtained after Smith degradation, or solvolysis with anhydrous hydrogen fluoride, the repeating unit of the O-specific polysaccharide was shown to be the pentasaccharide: [formula: see text]

  LPS, O-antigen, endotoxin, Hafnia alvei

  NCBI PubMed ID: 8556734
  Publication DOI: 10.1016/0008-6215(95)00200-D
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: gamian@immuno.iitd.pan.wroc.pl
  Institutions: Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland, Universidad de Sevillia, Departamento de Quimica Organica, Facultad de Quimica, Sevillie, Spain, The Technical University of Denmark, Institute of Organic Chemistry, Lyngby, Denmark, CNRS and CEA, Institut de Biologie Structurale, Grenoble, France, CNRS and CEA, Departament de Recherche Fondamentale sur la Matiere Condensee, Grenoble, France
  Methods: methylation, NMR-2D, FAB-MS, NMR, HF solvolysis, sugar analysis, Smith degradation
  
   
  
  Hafnia alvei PCM 1188
  CSDB ID 2201 (all data & tools)

Show legend Show as text

Structure type: monomer
Contained glycoepitopes: IEDB_130701,IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 237
  Garozzo D, Impallomeni G, Spina E, Sturiale L, Cesàro A, Cescutti P "Identification of N-acetylglucosamine and 4-O-[1-carboxyethyl]mannose in the exopolysaccharide from Cyanospira capsulata" - Carbohydrate Research 270(1) (1995) 97-106
  

  No Abstract

  exopolysaccharide, lactylman, Cyanospira capsulata, cianobacterium

  Publication DOI: 10.1016/0008-6215(95)98597-V
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Istituto per la Chimicae e la Technologia dei Materiali Polimerici, Consiglio Nazionale delle Ricerche, Cantania, Italy, Dipartamento di Biochimica, Biofisica e Chimica delle Macromolecole, Universita di Trieste, Trieste, Italy
  Methods: methylation, NMR-2D, NMR, carboxyl reduction, lithium reduction
  
   
  
  Cyanospira capsulata
  CSDB ID 6848 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: CPS
Contained glycoepitopes: IEDB_115136,IEDB_130701,IEDB_140630,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 240
  Gloaguen V, Wieruszeski JM, Strecker G, Hoffmann L, Morvan H "Identification by NMR spectroscopy of oligosaccharides obtained by acidolysis of the capsular polysaccharide of a thermal biomass" - International Journal of Biological Macromolecules 17 (1995) 387-393
  

  This study deals with the chemical characterization of a capsular polysaccharide (CPS) produced by a thermal biomass largely comprising the cyanobacterium Mastigocladus laminosus. The sugar moiety of this polymer is composed of seven neutral monosaccharides (Rha, Fuc, Ara, Xyl, Man, Glc, Gal) and two uronic acids (GalA, GlcA). Proteins represent 18% of the dry weight of the CPS. Organic acid substituents (acetate, pyruvate, succinate) were also detected and estimated by high-performance liquid chromatography. The presence of sulfate groups (5% w/w) was observed, which represents a relatively rare feature for cyanobacteria. Acidic hydrolysis of the purified polysaccharide led to the isolation of four oligosaccharidic fractions. NMR spectroscopy studies of two of the four purified oligosaccharides allowed them to be identified as: α-GlcA-(1→2)-α-GalA-(1→2)-Man and α-GlcA-(1→2)-α-GalA-(1→2)-β-Man-(1→4)-β-Gal-(1→2)-Rha?

  Oligosaccharides, capsular polysaccharide, cyanobacteria

  NCBI PubMed ID: 8789345
  Journal NLM ID: 7909578
  Publisher: Butterworth-Heinemann
  Institutions: Laboratoire de Biologie Cellulaire Vegetale et Valorisation des Especes Ligneuses, Université de Limoges, Limoges, France
  Methods: methylation, NMR-2D, NMR, sugar analysis
  
   
  
  Mastigocladus laminosus
  CSDB ID 6858 (all data & tools)

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Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130701,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_151528,IEDB_152206,IEDB_190606,IEDB_983930,SB_44,SB_67,SB_7,SB_72

• Article ID: 283
  Kannenberg EL, Forsberg LS, Carlson RW "Lipopolysaccharide core components of Rhizobium etli reacting with a panel of monoclonal antibodies" - Plant and Soil 186(1) (1996) 161-166
  

  Monoclonal antibodies that react with Rhizobium leguminosarum lipopolysaccharide core antigens (LPS-2) have been used to investigate LPS-2 structure in Rhizobium etli. The panel of antibodies (JIM 32 - JIM 35, JIM 37, JIM 38) specific for LPS-2 of R. leguminosarum strain 3841 and its core components displays similar reactivities towards isolated LPS-2 from R. etli CEI09 (a mutant of wild-type strain R. etli CE3 that displays LPS-2 as its main LPS form on the cell surface). This result suggests the antibodies bind to similar epitopcs on both strains and, hence, that R. legiiminosarum and R. etli have very similar LPS core and lipid A antigen structures. More detailed analysis of the antibody binding sites with isolated LPS-2 and lipid A from R. etli suggests that some of the antibodies (JIM 32, 33, 34, and MASM-I) bind some part of the core oligosaccharidcs, while others (JIM 35 and JIM 38) involve lipid A. These antibodies have already proven useful in the biochemical analysis of the LPS antigen forms. For example, the loss of reactivity of certain LPS forms with antibody JIM 37 has led to the discovery of a hitherto unnoticed form of the LPS antigen in a precipitate formed during the phenol/water extraction procedure. This new form reacts with the JIM 37 antibody. Furthermore, the positive reaction of some of the antibodies with only sonicated wild-type R. etli cells suggests that either an effective way of masking the display of core antigens on whole bacterial cells is occurring or that core forms of the LPSs are never displayed on the surface of the bacterial cells. Either possibility, once confirmed, could be important for our picture of the Rhizobium cell surface and could also have some bearing on symbiotic nodule infection and development.

  LPS, monoclonal, monoclonal antibodies, lipopolysaccharide core, Rhizobium, Rhizobium etli, symbiosis, plant

  Publication DOI: 10.1007/BF00035070
  Journal NLM ID: 9882808
  Publisher: The Hague: M. Nijhoff
  Correspondence: elmark@ccrc.uga.edu
  Institutions: Complex Carbohydrate Research Cento and Department of Biochemistry and Molecular Biology, University of Georgia, 220RiverbendRoad, Athens, GA 30602-4712, USA.
  Methods: immunochemical methods
  
   
  
  Rhizobium etli
  CSDB ID 7185 (all data & tools)

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Structure type: monomer
Trivial name: xanthan
Contained glycoepitopes: IEDB_130701,IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 335
  Nankai H, Hashimoto W, Miki H, Kawai S, Murata K "Microbial system for polysaccharide depolymerization: enzymatic route for xanthan depolymerization by Bacillus sp strain GL1" - Applied and Environmental Microbiology 65(6) (1999) 2520-2526
  

  An enzymatic route for the depolymerization of a heteropolysaccharide (xanthan) in Bacillus sp. strain GL1, which was closely related to Brevibacillus thermoruber, was determined by analyzing the structures of xanthan depolymerization products. The bacterium produces extracellular xanthan lyase catalyzing the cleavage of the glycosidic bond between pyruvylated mannosyl and glucuronyl residues in xanthan side chains (W. Hashimoto et al., Appl. Environ. Microbiol. 64:3765-3768, 1998). The modified xanthan after the lyase reaction was then depolymerized by extracellular β-D-glucanase to a tetrasaccharide, without the terminal mannosyl residue of the side chain in a pentasaccharide, a repeating unit of xanthan. The tetrasaccharide was taken into cells and converted to a trisaccharide (unsaturated glucuronyl-acetylated mannosyl-glucose) by β-D-glucosidase. The trisaccharide was then converted to the unsaturated glucuronic acid and a disaccharide (mannosyl-glucose) by unsaturated glucuronyl hydrolase. Finally, the disaccharide was hydrolyzed to mannose and glucose by α-D-mannosidase. This is the first complete report on xanthan depolymerization by bacteria. Novel β-D-glucanase, one of the five enzymes involved in the depolymerization route, was purified from the culture fluid. This enzyme was a homodimer with a subunit molecular mass of 173 kDa and was most active at pH 6.0 and 45 degrees C. The enzyme specifically acted on xanthan after treatment with xanthan lyase and released the tetrasaccharide.

  xanthan, strain, polysaccharide, enzymatic, Bacillus, depolymerization

  NCBI PubMed ID: 10347037
  Journal NLM ID: 7605801
  Publisher: American Society for Microbiology
  Correspondence: hasimoto@food2.food.kyoto-u.ac.jp
  Institutions: Research Institute for Food Science, Kyoto University, Uji 611-0011, Japan
  Methods: SDS-PAGE, ESI-MS, enzymatic degradation, RNA analysis
  
   
  
  Bacillus sp. GL1
  CSDB ID 7848 (all data & tools)

Show legend Show as text

Structure type: monomer
Contained glycoepitopes: IEDB_130701,IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 396
  Tian XX, Li AF, Farrugia IV, Mo XS, Crich D, Groves MJ "Isolation and identification of poly-a-(1→4)-linked 3-O-methyl-D-mannopyranose from a hot-water extract of Mycobacterium vaccae" - Carbohydrate Research 324(1) (2000) 38-44
  

  A polysaccharide around 3.6 kDa has been identified as the major carbohydrate moiety of a antineoplastic protein-polysaccharide complex (PS4A) obtained by boiling intact cells of Mycobacterium vaccae in water. 1H and 13C NMR spectra of this polysaccharide suggested it was a highly homogeneous polymer composed substantially of one monomer, probably an α-linked O-methylated mannose. Comparison of the COSY spectra of the original and acetylated polymer indicated that the glycosidic linkage and the methyl ether were interchangeable, at O-3 and O-4. Further study demonstrated that the benzyolated hydrolysate of the polymer was 1,2,4,6-tetra-O-benzoyl-3-O-methyl-β-mannopyranose. The hydrolysate was 3-O-methyl-α, β-mannopyranose and the polymer was therefore poly-α-(1→4)-linked 3-O-methyl-D-mannopyranose. This conclusion was further confirmed with an authentic sample of the monomer, which had spectral data identical to those of the hydrolyzate and co-eluted from an ion-exchange HPLC with the major sugar in the hydrolysate.

  synthesis, Protein-polysaccharide complex, Poly-α-(1-4)-3-O-methyl mannopyranose, Mycobacterium vaccae

  NCBI PubMed ID: 10723610
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: groves@uic.edu
  Institutions: Institute for Tuberculosis Research (M:C 964), University of Illinois at Chicago, Chicago Technology Park, 2201W. Campbell Park Dr., c 217, Chicago, IL 60612, USA, Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL 60607, USA
  Methods: NMR-2D, NMR
  
   
  
  Mycobacterium vaccae ATCC 15483
  CSDB ID 8410 (all data & tools)

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Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_153755,IEDB_190606,IEDB_983930,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 631
  Becker BU, Kosch K, Parniske M, Müller P "Exopolysaccharide (EPS) synthesis in Bradyrhizobium japonicum: sequence, operon structure and mutational analysis of an exo gene cluster" - Molecular and General Genetics 259(2) (1998) 161-171
  

  The nucleotide sequence of a 8330-bp DNA fragment from Bradyrhizobium japonicum 110spc4 was determined. Sequence analysis revealed that six ORFs were present and the deduced amino acid sequences were homologous to enzymes involved in exopolysaccharide (EPS) biosynthesis. The genes appear to be organized into at least four different operons. One gene was found to be homologous to exoB, which encodes a UDP-galactose 4'-epimerase. Other ORFs were homologous to UDP-hexose transferases and one ORF showed similarity to Sinorhizobium (Rhizobium) meliloti ExoP, which has been suggested to be involved in EPS chain-length determination. A set of deletion and insertion mutants was constructed and the resulting B. japonicum strains were tested for their symbiotic traits. Deletion mutant DP22, which lacks the C-terminal part of ExoP, the UDP-hexose transferase ExoT and the N-terminal part of ExoB, shows a delayed nodulation phenotype and induces symptoms of plant defense reactions; its EPS does not contain galactose and no high molecular weight fraction is synthesized. In contrast, insertion mutant EH3, which expresses an exoP gene product that is truncated in its putative periplasmic domain, produced an EPS containing both HMW and LMW fractions. However, the interaction of EH3 with soybeans was severely perturbed. As a rule, only the initial steps of nodule formation were observed.

  synthesis, structure, gene, analysis, cluster, gene cluster, exopolysaccharide, symbiosis, sequence, EPS, operon, Bradyrhizobium japonicum, Bradyrhizobium, gene fusion, nodule development, transcriptional reporter

  NCBI PubMed ID: 9747707
  Journal NLM ID: 0125036
  Publisher: Berlin; New York: Springer
  Correspondence: muellerp@mailer.uni-marburg.de
  Institutions: The Sainsbury Laboratory, Norwich Research Park, Colney, Norwich NR4 7UH, UK
  Methods: DNA sequencing, plant assays
  
   
  
  Bradyrhizobium japonicum
  CSDB ID 94 (all data & tools)