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Literature summary extracted from

  • Chen, M.M.; Glover, K.J.; Imperiali, B.
    From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni (2007), Biochemistry, 46, 5579-5585.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.99.18 0.0008
-
 acetyl-DQNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni
2.4.99.18 0.00087
-
 acetyl-DFNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni
2.4.99.18 0.00106
-
 acetyl-DVNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni
2.4.99.18 0.00122
-
 acetyl-DFNVT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni
2.4.99.18 0.00144
-
 acetyl-DVNVT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni
2.4.99.18 0.003
-
 acetyl-DVNAS-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni
2.4.99.18 0.0225
-
 acetyl-EVNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.99.19 Mn2+ activates Campylobacter jejuni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 DQNAT is the optimal acceptor substrate. PglB is not capable of utilizing glycosyl donors such as dolichyl-pyrophosphatechitobiose Campylobacter jejuni dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine
-
 ?
2.4.99.18 GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DFNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni ?
-
 ?
2.4.99.18 GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DFNVT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni ?
-
 ?
2.4.99.18 GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DQNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni ?
-
 ?
2.4.99.18 GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DVNAS-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni ?
-
 ?
2.4.99.18 GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DVNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni ?
-
 ?
2.4.99.18 GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-DVNVT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni ?
-
 ?
2.4.99.18 GalNAc-N,N'-diacetyl-bacillosamine-PP-undecaprenyl + acetyl-EVNAT-(4-nitrophenylalanine)-NH2
-
 Campylobacter jejuni ?
-
 ?
2.4.99.18 additional information no activity with acetyl-NVAAT-(para-nitrophenylalanine)-NH2 and acetyl-DVAAT-(para-nitrophenylalanine)-NH2 Campylobacter jejuni ?
-
 ?
2.4.99.19 additional information peptide substrate library construction, based on the known glycosylation site 88DFNVS92 from the Campylobacter jejuni glycoprotein PEB3, and assessment of the amino acids at each position of the consensus glycosylation sequence for their impact on glycosylation efficiency using a quantitative radioactivity-based in vitro assay, and glycosylation sequences specificity, overview. Circular dichroism spectra of acceptor proteins. PglB is inactive with glycosyl donors such as dolichyl-pyrophosphatechitobiose Campylobacter jejuni ?
-
 ?
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 ?
2.4.99.19 tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline, sequence DQNAT is the optimal acceptor substrate 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 PglB
-
 Campylobacter jejuni
2.4.99.19 oligosaccharyl transferase
-
 Campylobacter jejuni
2.4.99.19 OT
-
 Campylobacter jejuni
2.4.99.19 PglB
-
 Campylobacter jejuni

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.99.19 7.5
-
 assay at Campylobacter jejuni

General Information

EC Number General Information Comment Organism
2.4.99.19 metabolism PglB is involved in the Campylobacter jejuni general N-linked protein glycosylation pathway, overview Campylobacter jejuni
2.4.99.19 physiological function PglB catalyzes the transfer of an oligosaccharide from a polyisoprenyl pyrophosphate carrier to the asparagine side chain of proteins within the conserved glycosylation sites D/E-X1-N-X2-S/T, where X1 and X2 can be any amino acids except proline Campylobacter jejuni