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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
additional information
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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
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one N-acetylgalactosamine is linked to the polyisoprenepyrophosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und
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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
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additional information
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starting from UDP-GalNAc, UDP-Glc, Und-P and chemically synthesized UDP-Bac-2,4-NAc, the reactions of recombinant PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel to synthesize the bacterial glycan heptasaccharide, overview. Presence of GST-PglF, PglE and PglD in the same reaction vessel does not inhibit the downstream reactions. In N-linked glycoproteins the heptasaccharide is covalently attached at the N,N'-diacetylbacillosamine through a beta-linkage to the amide nitrogen of an asparagine side chain in the canonical sequence Asn-Xaa-Ser/Thr motif, where Xaa can be any amino acid except proline
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additional information
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development and optimization of an assay method to monitor the transfer of GalNAc from the hydrophilic UDP-linked carrier to the lipophilic UndPP-diNAcBac, i.e. 2,4-diacetamido-2,4,6-trideoxyglucose
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additional information
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starting from UDP-GalNAc, UDP-Glc, Und-P and chemically synthesized UDP-Bac-2,4-NAc, the reactions of recombinant PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel to synthesize the bacterial glycan heptasaccharide, overview. Presence of GST-PglF, PglE and PglD in the same reaction vessel does not inhibit the downstream reactions. In N-linked glycoproteins the heptasaccharide is covalently attached at the N,N'-diacetylbacillosamine through a beta-linkage to the amide nitrogen of an asparagine side chain in the canonical sequence Asn-Xaa-Ser/Thr motif, where Xaa can be any amino acid except proline
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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
additional information
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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
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one N-acetylgalactosamine is linked to the polyisoprenepyrophosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und
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UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
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additional information
?
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starting from UDP-GalNAc, UDP-Glc, Und-P and chemically synthesized UDP-Bac-2,4-NAc, the reactions of recombinant PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel to synthesize the bacterial glycan heptasaccharide, overview. Presence of GST-PglF, PglE and PglD in the same reaction vessel does not inhibit the downstream reactions. In N-linked glycoproteins the heptasaccharide is covalently attached at the N,N'-diacetylbacillosamine through a beta-linkage to the amide nitrogen of an asparagine side chain in the canonical sequence Asn-Xaa-Ser/Thr motif, where Xaa can be any amino acid except proline
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?
additional information
?
-
-
starting from UDP-GalNAc, UDP-Glc, Und-P and chemically synthesized UDP-Bac-2,4-NAc, the reactions of recombinant PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel to synthesize the bacterial glycan heptasaccharide, overview. Presence of GST-PglF, PglE and PglD in the same reaction vessel does not inhibit the downstream reactions. In N-linked glycoproteins the heptasaccharide is covalently attached at the N,N'-diacetylbacillosamine through a beta-linkage to the amide nitrogen of an asparagine side chain in the canonical sequence Asn-Xaa-Ser/Thr motif, where Xaa can be any amino acid except proline
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physiological function
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the enzyme is involved in a general N-linked glycosylation system that plays a role in pathogenicity
metabolism
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a general N-linked glycosylation pathway, encoded by the pgl gene cluster, culminates in the transfer of a heptasaccharide: GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcalpha1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac, where Bac is bacillosamine, i.e. 2,4-diacetamido-2,4,6-trideoxyglucose, from a membrane-anchored undecaprenylpyrophosphate (Und-PP)-linked donor to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif. For biosynthesis of Und-PP-linked heptasaccharide, PglA and PglJ add the first two GalNAc residues on to the isoprenoid-linked Bac carrier, respectively. Elongation of the trisaccharide with PglH results in a hexasaccharide revealing the polymerase activity of PglH. The final branching glucose is then added by PglI, which prefers native lipids for optimal activity. Pathway overview
metabolism
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PglF, PglE, PglD, PglC and PglA are the enzymes involved in the biosynthesis of an undecaprenyl diphosphate-linked disaccharide
metabolism
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the enzyme is involved in the biosynthesis of the sugar 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose, termed N,N'-diacetylbacillosamine or Bac2,4diNAc, the first carbohydrate in the glycoprotein N-linked heptasaccharide, in vitro biosynthesis of the complete heptasaccharide lipid-linked donor by coupling the action of eight enzymes, PglF, PglE, PglD, PglC, PglA, PglJ, PglH, and PglI, in the Pgl pathway
metabolism
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the enzyme is part of the enzyme system catalyzing the synthesis of the Und-PP-linked heptasaccharide GalNAc-alpha1,4- GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-Gal-NAc-alpha1,4-GalNAc-R1,3-Bac-R1,PP-Und, where Bac is the unusual sugar bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucose) that is only found in specific bacterial systems
metabolism
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the enzyme is involved in the biosynthesis of the sugar 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose, termed N,N'-diacetylbacillosamine or Bac2,4diNAc, the first carbohydrate in the glycoprotein N-linked heptasaccharide, in vitro biosynthesis of the complete heptasaccharide lipid-linked donor by coupling the action of eight enzymes, PglF, PglE, PglD, PglC, PglA, PglJ, PglH, and PglI, in the Pgl pathway
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metabolism
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a general N-linked glycosylation pathway, encoded by the pgl gene cluster, culminates in the transfer of a heptasaccharide: GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcalpha1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac, where Bac is bacillosamine, i.e. 2,4-diacetamido-2,4,6-trideoxyglucose, from a membrane-anchored undecaprenylpyrophosphate (Und-PP)-linked donor to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif. For biosynthesis of Und-PP-linked heptasaccharide, PglA and PglJ add the first two GalNAc residues on to the isoprenoid-linked Bac carrier, respectively. Elongation of the trisaccharide with PglH results in a hexasaccharide revealing the polymerase activity of PglH. The final branching glucose is then added by PglI, which prefers native lipids for optimal activity. Pathway overview
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Olivier, N.B.; Chen, M.M.; Behr, J.R.; Imperiali, B.
In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system
Biochemistry
45
13659-13669
2006
Campylobacter jejuni, Campylobacter jejuni NCTC 11168
brenda
Morrison, J.P.; Troutman, J.M.; Imperiali, B.
Development of a multicomponent kinetic assay of the early enzymes in the Campylobacter jejuni N-linked glycosylation pathway
Bioorg. Med. Chem.
18
8167-8171
2010
Campylobacter jejuni
brenda
Weerapana, E.; Glover, K.J.; Chen, M.M.; Imperiali, B.
Investigating bacterial N-linked glycosylation: synthesis and glycosyl acceptor activity of the undecaprenyl pyrophosphate-linked bacillosamine
J. Am. Chem. Soc.
127
13766-13767
2005
Campylobacter jejuni
brenda
Glover, K.J.; Weerapana, E.; Imperiali, B.
In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation
Proc. Natl. Acad. Sci. USA
102
14255-14259
2005
Campylobacter jejuni, Campylobacter jejuni NCTC 11168
brenda
Enzyme Nomenclature
2.4.1.290 N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
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