EC - GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase
Other name:
Systematic name:
UDP-N-acetyl-α-D-galactosamine:GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-α-N-acetyl-D-galactosaminyltransferase



Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Glover, K. J., Weerapana, E., Imperiali, B.
    In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation.
    Proc. Natl. Acad. Sci. U.S.A. 102: 14255-14259 (2005). [PMID: 16186480]
  2. Troutman, J. M., Imperiali, B.
    Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions.
    Biochemistry 48: 2807-2816 (2009). [PMID: 19159314]
  3. Borud, B., Viburiene, R., Hartley, M. D., Paulsen, B. S., Egge-Jacobsen, W., Imperiali, B., Koomey, M.
    Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system.
    Proc. Natl. Acad. Sci. U.S.A. 108: 9643-9648 (2011). [PMID: 21606362]

[EC created 2012]