A UDP-HexNAc:polyprenol-P GalNAc-1-P transferase (WecP) representing a new subgroup of the enzyme family

J Bacteriol. 2011 Apr;193(8):1943-52. doi: 10.1128/JB.01441-10. Epub 2011 Feb 18.


The Aeromonas hydrophila AH-3 WecP represents a new class of UDP-HexNAc:polyprenol-P HexNAc-1-P transferases. These enzymes use a membrane-associated polyprenol phosphate acceptor (undecaprenyl phosphate [Und-P]) and a cytoplasmic UDP-d-N-acetylhexosamine sugar nucleotide as the donor substrate. Until now, all the WecA enzymes tested were able to transfer UDP-GlcNAc to the Und-P. In this study, we present in vitro and in vivo proofs that A. hydrophila AH-3 WecP transfers GalNAc to Und-P and is unable to transfer GlcNAc to the same enzyme substrate. The molecular topology of WecP is more similar to that of WbaP (UDP-Gal polyprenol-P transferase) than to that of WecA (UDP-GlcNAc polyprenol-P transferase). WecP is the first UDP-HexNAc:polyprenol-P GalNAc-1-P transferase described.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aeromonas hydrophila / enzymology*
  • Carbohydrate Sequence
  • Models, Molecular
  • Molecular Sequence Data
  • N-Acetylhexosaminyltransferases / chemistry
  • N-Acetylhexosaminyltransferases / metabolism*
  • Polyisoprenyl Phosphates / metabolism*
  • Uridine Diphosphate N-Acetylgalactosamine / metabolism*


  • Polyisoprenyl Phosphates
  • undecaprenyl phosphate
  • Uridine Diphosphate N-Acetylgalactosamine
  • N-Acetylhexosaminyltransferases