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Literature summary extracted from

  • Morrison, J.P.; Troutman, J.M.; Imperiali, B.
    Development of a multicomponent kinetic assay of the early enzymes in the Campylobacter jejuni N-linked glycosylation pathway (2010), Bioorg. Med. Chem., 18, 8167-8171.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.135 Triton X-100 at 0.04% 30fold higher activity than at 1% Campylobacter jejuni

Application

EC Number Application Comment Organism
4.2.1.135 biotechnology assay targets enzymes involved in the biosynthesis of the unusual bacterial sugar diNAcBac and the transfer of diNAcBac-phosphate to UndP. This multienzyme assay, together with the established assays for the individual enzymes, can be used to screen for inhibitors, and may be used to evaluate substrate flux along the inhibited pathway. This assay is optimized for maximum sensitivity to inhibition of PglF, PglE, PglD, and PglC by balancing the enzyme concentrations such that each is partially rate determining Campylobacter jejuni

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.135 recombinantly expressed Campylobacter jejuni

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.290 additional information screening for inhibitors of the first four steps in the N-linked glycosylation system pathway, overview Campylobacter jejuni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.290 UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol Campylobacter jejuni
-
UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
-
?
2.6.1.34 UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate Campylobacter jejuni the enzyme is involved in the biosynthesis of an undecaprenyl diphosphate-linked disaccharide UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.290 Campylobacter jejuni
-
gene pglA
-
2.6.1.34 Campylobacter jejuni
-
-
-
4.2.1.135 Campylobacter jejuni
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.135 using affinity chromatography Campylobacter jejuni

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.290 additional information development and optimization of an assay method to monitor the transfer of GalNAc from the hydrophilic UDP-linked carrier to the lipophilic UndPP-diNAcBac, i.e. 2,4-diacetamido-2,4,6-trideoxyglucose Campylobacter jejuni ?
-
?
2.4.1.290 UDP-N-acetyl-alpha-D-galactosamine + N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
-
Campylobacter jejuni UDP + N-acetyl-D-galactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
-
?
2.6.1.34 UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose + L-glutamate the enzyme is involved in the biosynthesis of an undecaprenyl diphosphate-linked disaccharide Campylobacter jejuni UDP-4-amino-4,6-dideoxy-alpha-D-N-acetyl-D-glucosamine + 2-oxoglutarate
-
?
4.2.1.135 UDP-N-acetylglucosamine
-
Campylobacter jejuni ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.290 PglA
-
Campylobacter jejuni
4.2.1.135 PglF
-
Campylobacter jejuni

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.135 25
-
assay at Campylobacter jejuni

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.135 7.8
-
assay at Campylobacter jejuni

General Information

EC Number General Information Comment Organism
2.4.1.290 metabolism PglF, PglE, PglD, PglC and PglA are the enzymes involved in the biosynthesis of an undecaprenyl diphosphate-linked disaccharide Campylobacter jejuni
2.4.1.290 physiological function the enzyme is involved in a general N-linked glycosylation system that plays a role in pathogenicity Campylobacter jejuni
2.6.1.91 malfunction the N-linked glycosylation pathway is greatly reduced in pglE mutants Campylobacter jejuni