Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.99.19 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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
additional information functional transfer of the Campyobacter jejuni glycosylation system into Salmonella enterica 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 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 ?
-
?
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 ?
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 ?
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 ?
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 ?
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 ?
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 ?
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

Synonyms Comment Organism
bacterial oligosaccharyltransferase
-
Campylobacter jejuni
oligosacharyltransferase
-
Campylobacter jejuni
OTase
-
Campylobacter jejuni
PglB
-
Campylobacter jejuni

General Information

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