EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.4.99.19 | (bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY |
- |
Campylobacter jejuni |
? |
- |
? |
| 2.4.99.19 | (GalNAc2-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY |
- |
Campylobacter jejuni |
? |
- |
? |
| 2.4.99.19 | (Glc1GalNAc5-bacillosamine1) undecaprenyl diphosphate + Ac-D-F-N-V-TNH(CH2CH2O)2CH2CH2NH-BODIPY |
- |
Campylobacter jejuni |
? |
- |
? |
| 2.4.99.19 | Lys-Asp-Phe-Asn-Val-Ser-Lys-Ala + N-acetyl-alpha-D-galactosaminyl-diphospho-tritrans,heptacis-undecaprenol |
a chemically synthesized sugar donor with synthesized peptide acceptor |
Campylobacter jejuni |
tritrans,heptacis-undecaprenyl diphosphate + Lys-Asp-Phe-N4-[N-acetyl-beta-D-galactosaminyl]-Asn-Val-Ser-Lys-Ala |
- |
? |
| 2.4.99.19 | more |
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli |
Campylobacter jejuni |
? |
- |
? |
| 2.4.99.19 | more |
PglB1 protein, but not PglB2, is able to transfer Campylobacter jejuni N-linked glycan onto an acceptor protein in Escherichia coli |
Helicobacter pullorum |
? |
- |
? |
| 2.4.99.19 | more |
PglBCj can glycosylate residues in both unstructured and structured regions of eukaryotic acceptor proteins in vivo |
Campylobacter jejuni |
? |
- |
? |
| 2.4.99.19 | more |
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 |
? |
- |
? |
| 2.4.99.19 | more |
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 | more |
PglB is solely responsible for the oligosaccharyltransferase activity, PglB exhibits relaxed sugar substrate specificity |
Campylobacter jejuni |
? |
- |
? |
