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Literature summary for 2.4.99.19 extracted from
- From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni (2007), Biochemistry, 46, 5579-5585.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mn2+ | activates | Campylobacter jejuni |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | Campylobacter jejuni | - |
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Campylobacter jejuni | - |
gene pglB | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | peptide substrate library construction, based on the known glycosylation site 88DFNVS92 from the Campylobacter jejuni glycoprotein PEB3, and assessment of the amino acids at each position of the consensus glycosylation sequence for their impact on glycosylation efficiency using a quantitative radioactivity-based in vitro assay, and glycosylation sequences specificity, overview. Circular dichroism spectra of acceptor proteins. PglB is inactive with glycosyl donors such as dolichyl-pyrophosphatechitobiose | Campylobacter jejuni | ? | - |
? | |
| tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | - |
Campylobacter jejuni | tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? | |
| tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline, sequence DQNAT is the optimal acceptor substrate | Campylobacter jejuni | tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| oligosaccharyl transferase | - |
Campylobacter jejuni |
| OT | - |
Campylobacter jejuni |
| PglB | - |
Campylobacter jejuni |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Campylobacter jejuni |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | PglB is involved in the Campylobacter jejuni general N-linked protein glycosylation pathway, overview | Campylobacter jejuni |
| physiological function | PglB catalyzes the transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline | Campylobacter jejuni |
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Release 2023.1 (January 2023)
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