EC Number   |
General Information |
Reference |
|---|
  2.4.1.290 | metabolism |
a general N-linked glycosylation pathway, encoded by the pgl gene cluster, culminates in the transfer of a heptasaccharide: GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcalpha1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac, where Bac is bacillosamine, i.e. 2,4-diacetamido-2,4,6-trideoxyglucose, from a membrane-anchored undecaprenylpyrophosphate (Und-PP)-linked donor to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif. For biosynthesis of Und-PP-linked heptasaccharide, PglA and PglJ add the first two GalNAc residues on to the isoprenoid-linked Bac carrier, respectively. Elongation of the trisaccharide with PglH results in a hexasaccharide revealing the polymerase activity of PglH. The final branching glucose is then added by PglI, which prefers native lipids for optimal activity. Pathway overview |
-, 720888 |
| 2.4.1.290 | metabolism |
PglF, PglE, PglD, PglC and PglA are the enzymes involved in the biosynthesis of an undecaprenyl diphosphate-linked disaccharide |
714453 |
| 2.4.1.290 | metabolism |
the enzyme is involved in the biosynthesis of the sugar 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose, termed N,N'-diacetylbacillosamine or Bac2,4diNAc, the first carbohydrate in the glycoprotein N-linked heptasaccharide, in vitro biosynthesis of the complete heptasaccharide lipid-linked donor by coupling the action of eight enzymes, PglF, PglE, PglD, PglC, PglA, PglJ, PglH, and PglI, in the Pgl pathway |
-, 714160 |
| 2.4.1.290 | metabolism |
the enzyme is part of the enzyme system catalyzing the synthesis of the Und-PP-linked heptasaccharide GalNAc-alpha1,4- GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-Gal-NAc-alpha1,4-GalNAc-R1,3-Bac-R1,PP-Und, where Bac is the unusual sugar bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucose) that is only found in specific bacterial systems |
719641 |
| 2.4.1.290 | physiological function |
the enzyme is involved in a general N-linked glycosylation system that plays a role in pathogenicity |
714453 |
