Application | Comment | Organism |
---|---|---|
medicine | PglB-mediated transfer of poylsaccharides might be valuable for in vivo production of O-polysaccharides-protein congugates for use as antibacterial vaccines | Campylobacter jejuni |
medicine | the relaxed specificity of the PglB oligosaccharyltransferase toward the glycan structure is exploited to create novel N-glycan structures containing two distinct Escherichia coli or Pseudomonas aeruginosa O antigens. PglB-mediated transfer of polysaccharides might be valuable for in vivo production of O polysaccharides-protein conjugates for use as antibacterial vaccines | Campylobacter jejuni |
Cloned (Comment) | Organism |
---|---|
- |
Campylobacter jejuni |
expression in Escherichia coli | Campylobacter jejuni |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dolichyl diphosphooligosaccharide + [protein]-L-asparagine | Campylobacter jejuni | PglB, the key enzyme of the Campylobacter jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an accept or protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer | dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine | - |
? | |
additional information | Campylobacter jejuni | key enzyme of Campylobacter jejuni N-glycosylation system, transfers O-polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dolichyl diphosphooligosaccharide + [protein]-L-asparagine | PglB, the key enzyme of the Campylobacter jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an accept or protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer | Campylobacter jejuni | dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine | - |
? | |
dolichyl diphosphooligosaccharide + [protein]-L-asparagine | PglB has relaxed specificity toward its lipid-linked glycan substrate. It can transfer its endogenous substrate, the heptasaccharide Glc(GalNAc)5Bac of Campylobacter jejuni, as well as different O antigen polysaccharides that are assembled by the rhamnosyltransferase (polymerase)-dependent mechanism on the lipid carrier undecaprenyl diphosphate | Campylobacter jejuni | dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine | - |
? | |
additional information | key enzyme of Campylobacter jejuni N-glycosylation system, transfers O-polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer | Campylobacter jejuni | ? | - |
? | |
additional information | PglB can transfer diverse oligosaccharides and polysaccharides from Escherichia coli and Pseudomonas aeruginosa to proteins, in addition to the Campylobacter jejuni glycan. PglB attaches O7 polysaccharides and Campylobacter jejuni oligosaccharides to the same Asn residue in AcrA | Campylobacter jejuni | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PglB | - |
Campylobacter jejuni |
PglB oligosaccharyltransferase | - |
Campylobacter jejuni |