EC 2.3.1.203 - UDP-N-acetylbacillosamine N-acetyltransferase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 2.3.1.203

Names

Accepted name:
UDP-N-acetylbacillosamine N-acetyltransferase
Other names:
UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase
pglD (gene name)
Systematic name:
acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase

Reaction

Comments:

The product, UDP-N,N'-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [1,2] and O-linked glycosylation of certain L-serine residues in Neisseria species [3].

Links to other databases

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

References

  1. Olivier, N. B., Chen, M. M., Behr, J. R., Imperiali, B.
    In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system.
    Biochemistry 45 : 13659-13669 (2006). [PMID: 17087520]
  2. Rangarajan, E. S., Ruane, K. M., Sulea, T., Watson, D. C., Proteau, A., Leclerc, S., Cygler, M., Matte, A., Young, N. M.
    Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni.
    Biochemistry 47 : 1827-1836 (2008). [PMID: 18198901]
  3. Hartley, M. D., Morrison, M. J., Aas, F. E., Borud, B., Koomey, M., Imperiali, B.
    Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine.
    Biochemistry 50 : 4936-4948 (2011). [PMID: 21542610]

[EC 2.3.1.203 created 2012, modified 2013]