Found 51 structures.
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1. Compound ID: 47
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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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2. Compound ID: 48
Structure type: oligomer
Aglycon: p-nitrophenyl
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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3. Compound ID: 49
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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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4. Compound ID: 71
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-D-GlcNAc |
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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_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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5. Compound ID: 72
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-D-Man |
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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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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6. Compound ID: 73
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-D-Man |
Show graphically |
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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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7. Compound ID: 74
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-D-GlcNAc |
Show graphically |
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_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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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8. Compound ID: 75
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-D-Man |
Show graphically |
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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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9. Compound ID: 76
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-D-GlcNAc |
Show graphically |
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_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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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10. Compound ID: 77
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-D-Man |
Show graphically |
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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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11. Compound ID: 78
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-D-GlcNAc |
Show graphically |
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_153530,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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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12. Compound ID: 79
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-D-Man |
Show graphically |
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
The structure is contained in the following publication(s):
- Article ID: 16
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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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13. Compound ID: 15178
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-+
|
{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=6/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ {{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=3/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| | |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=7/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/Asn-X-Ser/Thr/ |
Show graphically |
Structure type: structural motif or average structure
Aglycon: Asn-X-Ser/Thr
Trivial name: poly-LacNAc-containing N-glycan
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158550,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5913
Damerow M, Graalfs F, Guther MLS, Mehlert A, Izquierdo L, Ferguson MA "A Gene of the beta3-Glycosyltransferase Family Encodes N-Acetylglucosaminyltransferase II Function in Trypanosoma brucei" -
Journal of Biological Chemistry 291(26) (2016) 13834-13845
The bloodstream form of the human pathogen Trypanosoma brucei expresses oligomannose, paucimannose, and complex N-linked glycans, including some exceptionally large poly-N-acetyllactosamine-containing structures. Despite the presence of complex N-glycans in this organism, no homologues of the canonical N-acetylglucosaminyltransferase I or II genes can be found in the T. brucei genome. These genes encode the activities that initiate the elaboration of the Manα1-3 and Manα1-6 arms, respectively, of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans. Previously, we identified a highly divergent T. brucei N-acetylglucosaminyltransferase I (TbGnTI) among a set of putative T. brucei glycosyltransferase genes belonging to the β3-glycosyltransferase superfamily (Damerow, M., Rodrigues, J. A., Wu, D., Güther, M. L., Mehlert, A., and Ferguson, M. A. (2014) J. Biol. Chem. 289, 9328-9339). Here, we demonstrate that TbGT15, another member of the same β3-glycosyltransferase family, encodes an equally divergent N-acetylglucosaminyltransferase II (TbGnTII) activity. In contrast to multicellular organisms, where GnTII activity is essential, TbGnTII null mutants of T. brucei grow in culture and are still infectious to animals. Characterization of the large poly-N-acetyllactosamine containing N-glycans of the TbGnTII null mutants by methylation linkage analysis suggests that, in wild-type parasites, the Manα1-6 arm of the conserved trimannosyl core may carry predominantly linear poly-N-acetyllactosamine chains, whereas the Manα1-3 arm may carry predominantly branched poly-N-acetyllactosamine chains. These results provide further detail on the structure and biosynthesis of complex N-glycans in an important human pathogen and provide a second example of the adaptation by trypanosomes of β3-glycosyltransferase family members to catalyze β1-2 glycosidic linkages.
glycosyltransferase, N-acetylglucosamine, glycobiology, Parasite, Trypanosoma brucei, post-translational modification (PTM)
NCBI PubMed ID: 27189951Publication DOI: 10.1074/jbc.M116.733246Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: From the Division of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
Methods: methylation, GC-MS, DNA techniques, glycosyltransferase assays, ESI-MS, Western blotting, composition analysis, genetic methods, Southern blotting, RT-PCR, HPTLC, LC-MS, NaBD4 reduction, lectin blotting, RNA extraction, SEM
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14. Compound ID: 15179
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ {{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=3/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-+ | a-D-Manp-(1-6)-+
| | | |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-}}}/n=4/-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/Asn-X-Ser/Thr/ |
Show graphically |
Structure type: structural motif or average structure
Aglycon: Asn-X-Ser/Thr
Trivial name: poly-LacNAc-containing N-glycan
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158550,IEDB_190606,IEDB_423128,IEDB_540672,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_173,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5913
Damerow M, Graalfs F, Guther MLS, Mehlert A, Izquierdo L, Ferguson MA "A Gene of the beta3-Glycosyltransferase Family Encodes N-Acetylglucosaminyltransferase II Function in Trypanosoma brucei" -
Journal of Biological Chemistry 291(26) (2016) 13834-13845
The bloodstream form of the human pathogen Trypanosoma brucei expresses oligomannose, paucimannose, and complex N-linked glycans, including some exceptionally large poly-N-acetyllactosamine-containing structures. Despite the presence of complex N-glycans in this organism, no homologues of the canonical N-acetylglucosaminyltransferase I or II genes can be found in the T. brucei genome. These genes encode the activities that initiate the elaboration of the Manα1-3 and Manα1-6 arms, respectively, of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans. Previously, we identified a highly divergent T. brucei N-acetylglucosaminyltransferase I (TbGnTI) among a set of putative T. brucei glycosyltransferase genes belonging to the β3-glycosyltransferase superfamily (Damerow, M., Rodrigues, J. A., Wu, D., Güther, M. L., Mehlert, A., and Ferguson, M. A. (2014) J. Biol. Chem. 289, 9328-9339). Here, we demonstrate that TbGT15, another member of the same β3-glycosyltransferase family, encodes an equally divergent N-acetylglucosaminyltransferase II (TbGnTII) activity. In contrast to multicellular organisms, where GnTII activity is essential, TbGnTII null mutants of T. brucei grow in culture and are still infectious to animals. Characterization of the large poly-N-acetyllactosamine containing N-glycans of the TbGnTII null mutants by methylation linkage analysis suggests that, in wild-type parasites, the Manα1-6 arm of the conserved trimannosyl core may carry predominantly linear poly-N-acetyllactosamine chains, whereas the Manα1-3 arm may carry predominantly branched poly-N-acetyllactosamine chains. These results provide further detail on the structure and biosynthesis of complex N-glycans in an important human pathogen and provide a second example of the adaptation by trypanosomes of β3-glycosyltransferase family members to catalyze β1-2 glycosidic linkages.
glycosyltransferase, N-acetylglucosamine, glycobiology, Parasite, Trypanosoma brucei, post-translational modification (PTM)
NCBI PubMed ID: 27189951Publication DOI: 10.1074/jbc.M116.733246Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson@dundee.ac.uk
Institutions: From the Division of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
Methods: methylation, GC-MS, DNA techniques, glycosyltransferase assays, ESI-MS, Western blotting, composition analysis, genetic methods, Southern blotting, RT-PCR, HPTLC, LC-MS, NaBD4 reduction, lectin blotting, RNA extraction, SEM
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15. Compound ID: 15196
|
a-D-Manp-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/Asn263 N-terminal N-glycosylation site NET peptide/ |
Show graphically |
Structure type: oligomer
; 809.3 [M+H+Na]2+
Aglycon: Asn263 N-terminal N-glycosylation site NET peptide
Trivial name: sVSG, soluble-form VSG, variant surface glycoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,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_153212,IEDB_190606,IEDB_423128,IEDB_548907,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5917
Denton H, Fyffe S, Smith TK "GDP-mannose pyrophosphorylase is essential in the bloodstream form of Trypanosoma brucei" -
Biochemical Journal 425(3) (2010) 603-614
A putative GDP-Man PP (guanidine diphosphomannose pyrophosphorylase) gene from Trypanosoma brucei (TbGDP-Man PP) was identified in the genome and subsequently cloned, sequenced and recombinantly expressed, and shown to be a catalytically active dimer. Kinetic analysis revealed a Vmax of 0.34 μmol/min per mg of protein and Km values of 67 μM and 12 μM for GTP and mannose 1-phosphate respectively. Further kinetic studies showed GDP-Man was a potent product feedback inhibitor. RNAi (RNA interference) of the cytosolic TbGDP-Man PP showed that mRNA levels were reduced to ~20% of wild-type levels, causing the cells to die after 3-4 days, demonstrating that TbGDP-Man PP is essential in the bloodstream form of T. brucei and thus a potential drug target. The RNAi-induced parasites have a greatly reduced capability to form GDP-Man, leading ultimately to a reduction in their ability to synthesize their essential GPI (glycosylphosphatidylinositol) anchors. The RNAi-induced parasites also showed aberrant N-glycosylation of their major cell-surface glycoprotein, variant surface glycoprotein, with loss of the high-mannose Man9GlcNAc2 N-glycosylation at Asn428 and formation of complex N-glycans at Asn263.
Glycosylphosphatidylinositol, N-glycosylation, Trypanosoma brucei, variant surface glycoprotein, essentiality, guanidine diphosphomannose pyrophosphorylase
NCBI PubMed ID: 19919534Publication DOI: 10.1042/BJ20090896Journal NLM ID: 2984726RPublisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
Correspondence: tks1@st-andrews.ac.uk
Institutions: Biomolecular Sciences Research Complex, The North Haugh, The University, St Andrews, Fife KY16 9ST, Scotland, UK
Methods: gel filtration, ESI-MS, ESI-MS/MS, genetic methods, HPLC, enzymatic digestion, Southern blotting, RT-PCR, HPTLC, cloning, enzymatic assay
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