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

BRENDA support

Literature summary for 2.4.99.19 extracted from

  • Jervis, A.J.; Langdon. R.; Hitchen, P.; Lawson, A.J.; Wood, A.; Fothergill, J.L.; Morris, H.R.; Dell, A.; Wren, B.; Linton, D.
    Characterization of N-linked protein glycosylation in Helicobacter pullorum (2010), J. Bacteriol., 192, 5228-5236.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
genes pglB1 and pglB2, DNA and amino acid sequence determination and analysis. Gene pglB1, but not the pglB2, gene is able to partially complement the Campylobacter jejuni pglB gene Helicobacter pullorum

Protein Variants

Protein Variants Comment Organism
additional information insertional knockout mutagenesis of the gene pglB2 is unsuccessful Helicobacter pullorum

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates Campylobacter jejuni
Mn2+ activates Helicobacter pullorum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Campylobacter jejuni PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli ?
-
?
additional information Helicobacter pullorum PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli ?
-
?
additional information Helicobacter pullorum NCTC 12824 PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli ?
-
?
additional information Campylobacter jejuni NCTC 11168 PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli ?
-
?
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 Helicobacter pullorum
-
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 Helicobacter pullorum NCTC 12824
-
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 Campylobacter jejuni NCTC 11168
-
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
-
single gene pglB
-
Campylobacter jejuni NCTC 11168
-
single gene pglB
-
Helicobacter pullorum
-
the organism contains two unrelated pglB genes, pglB1 and pglB2, neither of which is located within a larger locus involved in protein glycosylation
-
Helicobacter pullorum NCTC 12824
-
the organism contains two unrelated pglB genes, pglB1 and pglB2, neither of which is located within a larger locus involved in protein glycosylation
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli Campylobacter jejuni ?
-
?
additional information PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli Helicobacter pullorum ?
-
?
additional information PglB-dependent N-glycosylation, structural analysis of in vitro-generated glycopeptides, overview Campylobacter jejuni ?
-
?
additional information PglB1-dependent N glycosylation with a linear pentasaccharide requiring an acidic residue at the -2 position of the N-glycosylation sequon, structural analysis of in vitro-generated glycopeptides, overview Helicobacter pullorum ?
-
?
additional information PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli Helicobacter pullorum NCTC 12824 ?
-
?
additional information PglB1-dependent N glycosylation with a linear pentasaccharide requiring an acidic residue at the -2 position of the N-glycosylation sequon, structural analysis of in vitro-generated glycopeptides, overview Helicobacter pullorum NCTC 12824 ?
-
?
additional information PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli Campylobacter jejuni NCTC 11168 ?
-
?
additional information PglB-dependent N-glycosylation, structural analysis of in vitro-generated glycopeptides, overview Campylobacter jejuni NCTC 11168 ?
-
?
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
-
Helicobacter pullorum 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 e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites 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 e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites Helicobacter pullorum 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
-
Helicobacter pullorum NCTC 12824 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 e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites Helicobacter pullorum NCTC 12824 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
-
Campylobacter jejuni NCTC 11168 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 e.g. Campylobacter jejuni glycoprotein (Cj0114) contaiing four potential N-glycosylation sites Campylobacter jejuni NCTC 11168 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
PglB
-
Campylobacter jejuni
PglB1
-
Helicobacter pullorum
PglB2
-
Helicobacter pullorum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Campylobacter jejuni
30
-
assay at Helicobacter pullorum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Campylobacter jejuni
7
-
assay at Helicobacter pullorum

General Information

General Information Comment Organism
malfunction insertional knockout mutagenesis of the gene pglB2 is unsuccessful, suggesting that it is essential Helicobacter pullorum
physiological function the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB Campylobacter jejuni
physiological function the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB Helicobacter pullorum