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 |
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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.135 | recombinantly expressed | Campylobacter jejuni |
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 |
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 | - |
? |
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 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.2.1.135 | using affinity chromatography | Campylobacter jejuni |
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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.290 | PglA | - |
Campylobacter jejuni |
4.2.1.135 | PglF | - |
Campylobacter jejuni |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.2.1.135 | 25 | - |
assay at | Campylobacter jejuni |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.2.1.135 | 7.8 | - |
assay at | Campylobacter jejuni |
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 |