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

GalNAc5-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase
Identifiers
EC no.2.4.1.293
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins
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

This enzyme is isolated from the bacterium Campylobacter jejuni.

References

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  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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