EC - UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolysing)

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IntEnz Enzyme Nomenclature


Accepted name:
UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolysing)
Other names:
UDP-Bac2Ac4Ac 2-epimerase
Systematic name:
UDP-N,N'-diacetylbacillosamine hydrolase (2-epimerising)




Requires Mg2+. Involved in biosynthesis of legionaminic acid, a nonulosonate derivative that is incorporated by some bacteria into assorted virulence-associated cell surface glycoconjugates. The initial product formed by the enzyme from Legionella pneumophila, which incorporates legionaminic acid into the O-antigen moiety of its lipopolysaccharide, is 2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose, which rapidly mutarotates to a mixture of anomers [1]. The enzyme from Campylobacter jejuni, which incorporates legionaminic acid into flagellin, prefers GDP-N,N'-diacetylbacillosamine [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102388


  1. Glaze, P. A., Watson, D. C., Young, N. M., Tanner, M. E.
    Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila.
    Biochemistry 47: 3272-3282 (2008). [PMID: 18275154]
  2. Schoenhofen, I. C., Vinogradov, E., Whitfield, D. M., Brisson, J. R., Logan, S. M.
    The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.
    Glycobiology 19: 715-725 (2009). [PMID: 19282391]

[EC created 2012]