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Literature summary extracted from

  • Wacker, M.; Feldman, M.F.; Callewaert, N.; Kowarik, M.; Clarke, B.R.; Pohl, N.L.; Hernandez, M.; Vines, E.D.; Valvano, M.A.; Whitfield, C.; Aebi, M.
    Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems (2006), Proc. Natl. Acad. Sci. USA, 103, 7088-7093.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.99.18 functionally expressed in Escherichia coli Campylobacter jejuni
2.4.99.19 gene pglB, functional expression in Escherichia coli strains E69, CWG28, or CWG44 using an arabinose-inducible promoter, coexpression of the Acra protein substrate Campylobacter jejuni

Protein Variants

EC Number Protein Variants Comment Organism
2.4.99.19 additional information functional transfer of the Campyobacter jejuni glycosylation system into Salmonella enterica Campylobacter jejuni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine Campylobacter jejuni
-
dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
?
2.4.99.19 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

EC Number Organism UniProt Comment Textmining
2.4.99.18 Campylobacter jejuni
-
-
-
2.4.99.19 Campylobacter jejuni
-
gene pglB
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine
-
Campylobacter jejuni dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
?
2.4.99.18 dolichyl diphosphooligosaccharide + [protein]-L-asparagine to investigate the substrate specificity of PglB, the transfer of a set of lipid-linked polysaccharides in Escherichia coli and Salmonella enterica serovar typhimurium is tested. A hexose linked to the C-6 of the monosaccharide at the reducing end does not inhibit the transfer of the O antigen to the acceptor protein. PglB requires an acetamido group at the C-2. A model for the mechanism of PglB involving this functional group is proposed. Eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism. Substitution at the C-6 position in the reducing end of the oligosaccharide does not prevent its PglB-mediated transfer to the protein acceptor AcrA. PglB transferrs a polysaccharide that is assembled by a Wzy-protein-independent pathway. An N-acetyl group in position 2 of the sugar directly linked to the undecaprenyl diphosphate carrier is necessary for recognition and/or catalysis Campylobacter jejuni dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
-
?
2.4.99.19 additional information the PglB relaxed oligosaccharide substrate specificity allows the transfer of different glycans from the lipid carrier undecaprenyl pyrophosphate to an acceptor protein, substrate specificity of PglB with a set of lipid-linked polysaccharides in Escherichia coli and Salmonella enterica serovar Typhimurium. PglB required an acetamido group at the C-2, while a hexose linked to the C-6 of the monosaccharide at the reducing end does not inhibit the transfer of the O antigen to the acceptor protein, mechanism of PglB, modeling, overview. The Salmonella enterica O antigen containing Gal at the reducing end , and K30 capsular antigen, and LT2 antigen are not substrates for PglB, as Campylobacter jejuni ?
-
?
2.4.99.19 tritrans,heptacis-undecaprenyl diphospho-O1 antigen + [protein]-L-asparagine from Shigella dysenteriae Campylobacter jejuni tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O1 antigen a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine ?
2.4.99.19 tritrans,heptacis-undecaprenyl diphospho-O11 antigen + [protein]-L-asparagine from Pseudomonas aeruginosa Campylobacter jejuni tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O11 antigen a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine ?
2.4.99.19 tritrans,heptacis-undecaprenyl diphospho-O157 antigen + [protein]-L-asparagine from Escherichia coli Campylobacter jejuni tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O157 antigen a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine ?
2.4.99.19 tritrans,heptacis-undecaprenyl diphospho-O16 antigen + [protein]-L-asparagine from Escherichia coli Campylobacter jejuni tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O16 antigen a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine ?
2.4.99.19 tritrans,heptacis-undecaprenyl diphospho-O7 antigen + [protein]-L-asparagine from Escherichia coli Campylobacter jejuni tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-O7 antigen a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine ?
2.4.99.19 tritrans,heptacis-undecaprenyl diphospho-O9 antigen + [Acra]-L-asparagine PglB transfers the O9a antigen, an ABC transporter-dependent O antigen, to AcrA in Escherichia coli strain CWG28, the K30 antigen is not transferred to AcrA Campylobacter jejuni tritrans,heptacis-undecaprenyl diphosphate + [Acra]-L-asparagine-O9 antigen a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine ?
2.4.99.19 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 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.99.18 OTase
-
Campylobacter jejuni
2.4.99.18 PglB
-
Campylobacter jejuni
2.4.99.18 PglB oligosaccharyltransferase
-
Campylobacter jejuni
2.4.99.19 bacterial oligosaccharyltransferase
-
Campylobacter jejuni
2.4.99.19 oligosacharyltransferase
-
Campylobacter jejuni
2.4.99.19 OTase
-
Campylobacter jejuni
2.4.99.19 PglB
-
Campylobacter jejuni

General Information

EC Number General Information Comment Organism
2.4.99.19 evolution eukaryotic and prokaryotic OTases catalyze the transfer of oligosaccharides by a conserved mechanism Campylobacter jejuni