GalNAc5-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase

GalNAc5-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase (EC 2.4.1.293, PglI) is an enzyme with systematic name UDP-alpha-D-glucose:(GalNAc-alpha-(1->4))4-GalNAc-alpha-(1->3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol 3-beta-D-glucosyltransferase.[1][2] This enzyme catalyses the following chemical reaction

UDP-alpha-D-glucose + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol UDP + [GalNAc-alpha-(1->4)]2-[Glc-beta-(1->3)]-[GalNAc-alpha-(1->4)]2-GalNAc-alpha-(1->3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol
GalNAc5-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase
Identifiers
EC number2.4.1.293
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This enzyme is isolated from the bacterium Campylobacter jejuni.

References

  1. Glover KJ, Weerapana E, Imperiali B (October 2005). "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14255–9. doi:10.1073/pnas.0507311102. PMC 1242339. PMID 16186480.
  2. Kelly J, Jarrell H, Millar L, Tessier L, Fiori LM, Lau PC, Allan B, Szymanski CM (April 2006). "Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer". Journal of Bacteriology. 188 (7): 2427–34. doi:10.1128/JB.188.7.2427-2434.2006. PMC 1428418. PMID 16547029.
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