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Literature summary extracted from
- In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system (2006), Biochemistry, 45, 13659-13669.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.3.1.203 | expressed in Escherichia coli BL21 (DE3) pLysS cells | Campylobacter jejuni |
| 2.4.1.290 | gene pglA, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS | Campylobacter jejuni |
| 2.6.1.34 | expression in Escherichia coli | Campylobacter jejuni |
| 4.2.1.135 | full-length PglF is overexpressed as a GST-fusion protein | Campylobacter jejuni |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.2.1.135 | DELTA1-129 | a truncated form of pglF coding for residues M130-V590 is generated omitting the transmembrane domain which expressed well in Escherichia coli. Substrate turnover is not observed in a reaction coupling the deletion construct DELTA1-129 and PglE suggesting the involvement of the PglF transmembrane domain in preventing the inhibitory reaction | Campylobacter jejuni |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.3.1.203 | 0.41 | - |
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine | at 37°C, pH 7.7 | Campylobacter jejuni |  |
| 4.2.1.135 | 7 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.7, 37°C, full-length GST-PglF | Campylobacter jejuni | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 2.4.1.293 | cell envelope | - |
Campylobacter jejuni | 30313 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 2.3.1.203 | 23500 | - |
x * 23500, His-tagged enzyme, SDS-PAGE | Campylobacter jejuni |
| 4.2.1.135 | 93000 | - |
SDS-PAGE, GST-PglF | Campylobacter jejuni |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.289 | dTDP-6-deoxy-beta-L-mannose + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | Campylobacter jejuni | - |
dTDP + alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | - |
? | |
| 2.4.1.289 | dTDP-6-deoxy-beta-L-mannose + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | Campylobacter jejuni NCTC 11168 | - |
dTDP + alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | - |
? | |
| 2.4.1.290 | additional information | Campylobacter jejuni | 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 | ? | - |
? | |
| 2.4.1.290 | additional information | Campylobacter jejuni NCTC 11168 | 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 | ? | - |
? | |
| 2.4.1.290 | UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | Campylobacter jejuni | 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 | UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.291 | UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | Campylobacter jejuni | the sugar 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose, termed N,N'-diacetylbacillosamine, i.e Bac2,4diNAc, is 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 in a single reaction vessel, overview | UDP + N-acetyl-D-galactosaminyl-alpha-(1->4)-N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.292 | 3 UDP-N-acetyl-alpha-D-galactosamine + GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | Campylobacter jejuni | - |
3 UDP + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.293 | UDP-alpha-D-glucose + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | Campylobacter jejuni | - |
UDP + [GalNAc-alpha-(1->4)]2-[Glc-beta-(1->3)]-[GalNAc-alpha-(1->4)]2-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.6.1.34 | UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate | Campylobacter jejuni | - |
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate | - |
? | |
| 2.6.1.34 | UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate | Campylobacter jejuni NCTC 11168 | - |
UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.3.1.203 | Campylobacter jejuni | - |
- |
- |
| 2.3.1.203 | Campylobacter jejuni NCTC 11168 | - |
- |
- |
| 2.4.1.289 | Campylobacter jejuni | - |
gene pglA, cj1125c | - |
| 2.4.1.289 | Campylobacter jejuni NCTC 11168 | - |
gene pglA, cj1125c | - |
| 2.4.1.290 | Campylobacter jejuni | - |
gene Cj1125c or pglA | - |
| 2.4.1.290 | Campylobacter jejuni NCTC 11168 | - |
gene Cj1125c or pglA | - |
| 2.4.1.291 | Campylobacter jejuni | - |
gene pglJ | - |
| 2.4.1.291 | Campylobacter jejuni NCTC 11168 | - |
gene pglJ | - |
| 2.4.1.292 | Campylobacter jejuni | - |
gene pglH | - |
| 2.4.1.292 | Campylobacter jejuni NCTC 11168 | - |
gene pglH | - |
| 2.4.1.293 | Campylobacter jejuni | - |
gene pglI | - |
| 2.4.1.293 | Campylobacter jejuni NCTC 11168 | - |
gene pglI | - |
| 2.6.1.34 | Campylobacter jejuni | - |
- |
- |
| 4.2.1.135 | Campylobacter jejuni | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 2.3.1.203 | Ni-NTA resin column chromatography | Campylobacter jejuni |
| 2.4.1.290 | recombinant His-tagged PglA from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography | Campylobacter jejuni |
| 2.6.1.34 | - |
Campylobacter jejuni |
| 4.2.1.135 | purified in the presence of detergent | Campylobacter jejuni |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.3.1.203 | acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine | - |
Campylobacter jejuni | CoA + UDP-N,N'-diacetylbacillosamine | i.e. UDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose | ? | |
| 2.3.1.203 | acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine | - |
Campylobacter jejuni NCTC 11168 | CoA + UDP-N,N'-diacetylbacillosamine | i.e. UDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose | ? | |
| 2.4.1.289 | dTDP-6-deoxy-beta-L-mannose + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | - |
Campylobacter jejuni | dTDP + alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | - |
? | |
| 2.4.1.289 | dTDP-6-deoxy-beta-L-mannose + N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | - |
Campylobacter jejuni NCTC 11168 | dTDP + alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol | - |
? | |
| 2.4.1.289 | additional information | in vitro transfer of N,N'-diacetylbacillosamine phosphate onto Und-P and the in vitro enzymatic synthesis of the heptasacccharide using a chemically synthesized undecaprenyl diphosphate-linked N,N'-diacetylbacillosamine. The reactions of PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel, NMR spectrometric product analysis | Campylobacter jejuni | ? | - |
? | |
| 2.4.1.289 | additional information | in vitro transfer of N,N'-diacetylbacillosamine phosphate onto Und-P and the in vitro enzymatic synthesis of the heptasacccharide using a chemically synthesized undecaprenyl diphosphate-linked N,N'-diacetylbacillosamine. The reactions of PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel, NMR spectrometric product analysis | Campylobacter jejuni NCTC 11168 | ? | - |
? | |
| 2.4.1.290 | 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 | Campylobacter jejuni | ? | - |
? | |
| 2.4.1.290 | 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 | Campylobacter jejuni NCTC 11168 | ? | - |
? | |
| 2.4.1.290 | UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
Campylobacter jejuni | UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.290 | UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | 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 | Campylobacter jejuni | UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.291 | additional information | in vitro transfer of N,N'-diacetylbacillosamine phosphate onto Und-P and the in vitro enzymatic synthesis of the heptasacccharide using a chemically synthesized undecaprenyl diphosphate-linked N,N'-diacetylbacillosamine. The reactions of PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel, NMR spectrometric product analysis | Campylobacter jejuni | ? | - |
? | |
| 2.4.1.291 | UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
Campylobacter jejuni | UDP + N-acetyl-D-galactosaminyl-alpha-(1->4)-N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.291 | UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | the sugar 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose, termed N,N'-diacetylbacillosamine, i.e Bac2,4diNAc, is 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 in a single reaction vessel, overview | Campylobacter jejuni | UDP + N-acetyl-D-galactosaminyl-alpha-(1->4)-N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.292 | 3 UDP-N-acetyl-alpha-D-galactosamine + GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | - |
Campylobacter jejuni | 3 UDP + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.4.1.292 | additional information | in vitro transfer of N,N'-diacetylbacillosamine phosphate onto undecaprenyl-phosphate and the in vitro enzymatic synthesis of the heptasacccharide using a chemically synthesized undecaprenyl diphosphate-linked N,N'-diacetylbacillosamine. The reactions of PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel, NMR spectrometric product analysis | Campylobacter jejuni | ? | - |
? | |
| 2.4.1.293 | additional information | in vitro transfer of N,N'-diacetylbacillosamine phosphate onto undecaprenyl phosphate and the in vitro enzymatic synthesis of the heptasacccharide using a chemically synthesized undecaprenyl pyrophosphatelinked N,N'-diacetylbacillosamine. The reactions of PglC, PglA, PglH, PglJ and PglI are coupled in a single reaction vessel, NMR spectrometric product analysis | Campylobacter jejuni | ? | - |
? | |
| 2.4.1.293 | UDP-alpha-D-glucose + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | - |
Campylobacter jejuni | UDP + [GalNAc-alpha-(1->4)]2-[Glc-beta-(1->3)]-[GalNAc-alpha-(1->4)]2-GalNAc-alpha-(1->3)-Bac2,4diNAc-diphospho-tritrans,heptacis-undecaprenol | - |
? | |
| 2.6.1.34 | UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate | - |
Campylobacter jejuni | UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate | - |
? | |
| 2.6.1.34 | UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate | - |
Campylobacter jejuni NCTC 11168 | UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate | - |
? | |
| 4.2.1.135 | UDP-N-acetyl-alpha-D-glucosamine | PglF performs a cofactor-dependent hydride transfer from the C4 position of UDP-GlcNAc to C6, in conjunction with the elimination of water across the glucosyl C5 and C6 bond | Campylobacter jejuni | UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 2.3.1.203 | ? | x * 23500, His-tagged enzyme, SDS-PAGE | Campylobacter jejuni |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.3.1.203 | Cj1123c | - |
Campylobacter jejuni |
| 2.3.1.203 | PglD | - |
Campylobacter jejuni |
| 2.4.1.289 | Cj1125c | - |
Campylobacter jejuni |
| 2.4.1.289 | PglA | - |
Campylobacter jejuni |
| 2.4.1.290 | Cj1125c | - |
Campylobacter jejuni |
| 2.4.1.290 | PglA | - |
Campylobacter jejuni |
| 2.4.1.291 | PglJ | - |
Campylobacter jejuni |
| 2.4.1.292 | PglH | - |
Campylobacter jejuni |
| 2.4.1.293 | PglI | - |
Campylobacter jejuni |
| 2.6.1.34 | PglE | - |
Campylobacter jejuni |
| 4.2.1.135 | Cj1120c | - |
Campylobacter jejuni |
| 4.2.1.135 | PglF | - |
Campylobacter jejuni |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.289 | 22 | - |
assay at room temperature | Campylobacter jejuni |
| 4.2.1.135 | 37 | - |
assay at | Campylobacter jejuni |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.3.1.203 | 8050 | - |
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine | at 37°C, pH 7.7 | Campylobacter jejuni | |
| 4.2.1.135 | 0.118 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.7, 37°C, full-length GST-PglF | Campylobacter jejuni | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.289 | 7 | - |
assay at | Campylobacter jejuni |
| 4.2.1.135 | 7.7 | - |
assay at | Campylobacter jejuni |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.135 | NAD+ | catalytic activity by GST-PglF is enhanced in the presence of additional NAD+ but not NADP+ | Campylobacter jejuni | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 2.3.1.203 | metabolism | the enzyme catalyzes the final step in N,N'-diacetylbacillosamine synthesis by N-acetylation of UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine at the C4 position | Campylobacter jejuni |
| 2.4.1.289 | metabolism | the Pgl pathway produces the N-linked glycan heptasaccharide GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac2,4diNAc-_1-Asn. The pathway begins with diphosphate bond formation between the Bac2,4diNAc phosphate and undecaprenylphosphate (Und-P) by Cj1124c (PglC) to form Bac2,4diNAc-alpha1-PP-Und. One N-acetylgalactosamine (GalNAc) is linked to the polyisoprenediphosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und. Next, four additional GalNAc and one branching glucose are added sequentially to the isoprene-linked disaccharide by PglJ, PglH, and PglI, to form the heptasaccharide, overview | Campylobacter jejuni |
| 2.4.1.290 | metabolism | 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 | Campylobacter jejuni |
| 2.4.1.291 | metabolism | the Pgl pathway produces the N-linked glycan heptasaccharide GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac2,4diNAc-_1-Asn. The pathway begins with diphosphate bond formation between the Bac2,4diNAc phosphate and undecaprenylphosphate (Und-P) by Cj1124c (PglC) to form Bac2,4diNAc-alpha1-PP-Und. One N-acetylgalactosamine is linked to the polyisoprenediphosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und. Next, four additional GalNAc and one branching glucose are added sequentially to the isoprene-linked disaccharide by PglJ, PglH, and PglI, to form the heptasaccharide, overview | Campylobacter jejuni |
| 2.4.1.292 | metabolism | the Pgl pathway produces the N-linked glycan heptasaccharide GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac2,4diNAc-1-Asn. The pathway begins with pyrophosphate bond formation between the Bac2,4diNAc phosphate and undecaprenylphosphate by Cj1124c (PglC) to form Bac2,4diNAc-alpha1-PP-Und. One N-acetylgalactosamine is linked to the polyisoprenediphosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und. Next, four additional GalNAc and one branching glucose are added sequentially to the isoprene-linked disaccharide by PglJ, PglH, and PglI, to form the heptasaccharide, overview | Campylobacter jejuni |
| 2.4.1.293 | metabolism | the Pgl pathway produces the N-linked glycan heptasaccharide GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac2,4diNAc-1-Asn. The pathway begins with diphosphate bond formation between the Bac2,4diNAc phosphate and undecaprenylphosphate by Cj1124c (PglC) to form Bac2,4diNAc-alpha1-PP-Und. One N-acetylgalactosamine is linked to the polyisoprenediphosphate-bound N,N'-diacetylbacillosamine by Cj1125c (PglA) to form GalNAc-alpha1,3-Bac2,4diNAc-alpha1-PP-Und. Next, four additional GalNAc and one branching glucose are added sequentially to the isoprene-linked disaccharide by PglJ, PglH, and PglI, to form the heptasaccharide, overview | Campylobacter jejuni |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.3.1.203 | 20000 | - |
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine | at 37°C, pH 7.7 | Campylobacter jejuni | |
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Release 2023.1 (January 2023)
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