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Literature summary for 2.4.99.19 extracted from

  • Glover, K.J.; Weerapana, E.; Numao, S.; Imperiali, B.
    Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni (2005), Chem. Biol., 12, 1311-1315.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene pglB, expression of the wild-type and mutant WAAYGY-PglB variant in Escherichia coli in membranes Campylobacter jejuni

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 the native substrate for PglB is a heptasaccharide 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 ability of PglB to transfer a wide variety of saccharides and peptides, substrate specificity, mass spectrometric glycopeptide product analysis, overview. PglB readily accepts a disaccharide in vitro. PglB does require determinants in the peptide sequence beyond the canonical N-X-S/Ttripeptide Campylobacter jejuni ?
-
?
N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol + KDFNVSKA oligosaccharyl transferase activity of PglB in vitro with synthetic disaccharide glycan donor and peptide acceptor substrate Campylobacter jejuni tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-beta-D-bacillosaminyl]-Asn-Val-Ser-Lys-Ala
-
?
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 the native substrate for PglB is a heptasaccharide 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
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
malfunction if the WWDYGY signature sequence is mutated to WAAYGY, PglB is no longer active in vivo Campylobacter jejuni
metabolism PglB is involved in the general N-linked glycosylation pathway encoded by the pgl gene cluster Campylobacter jejuni
physiological function PglB catalyzes the transfer of an undecaprenyl-linked heptasaccharide to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif Campylobacter jejuni