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Glycobiology Advance Access published online on April 20, 2005
Glycobiology, doi:10.1093/glycob/cwi065
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Published by Oxford University Press 2005.
Received March 4, 2005
Revised April 15, 2005
Accepted April 15, 2005

Review

Modeling Bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P Transferases

Neil P. Price 1* and Frank A. Momany 2

1 USDA-ARS-NCAUR, Bioproducts and Biocatalysis Research Unit, 1815 North University Street, Peoria, Illinois 61604
2 Plant Polymer Research Unit, 1815 North University Street, Peoria, Illinois 61604

* To whom correspondence should be addressed.
Neil P. Price, E-mail: pricen{at}ncaur.usda.gov


  Abstract

Protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria are both initiated by the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate. These reactions are catalyzed by a family of transmembrane proteins known as the UDP-D-N-acetylhexosamine: polyprenol phosphate D-N-acetylhexosamine 1-phosphate transferases. The sole eukaryotic member of this family, the D-N-acetylglucosamine 1-phosphate transferase (GPT), is specific for UDP-GlcNAc as the donor substrate and uses dolichol phosphate as the membrane-bound acceptor. The bacterial translocases, MraY, WecA, and WbpL, utilize undecaprenol phosphate as the acceptor substrate, but differ in their specificity for the UDP-sugar donor substrate. The structural basis of this sugar nucleotide specificity is uncertain. However, potential carbohydrate recognition domains have been identified within the C-terminal cytoplasmic loops of MraY, WecA, and WbpL that are highly conserved in family members with the same UDP-N-acetylhexosamine specificity. This review focuses on the catalytic mechanism and substrate specificity of these bacterial UDP-D-N-acetylhexosamine: polyprenol phosphate D-N-acetylhexosamine 1-P transferases and may provide insights for the development of selective inhibitors of cell wall biosynthesis.

Keywords: MraY / tunicamycin / undecaprenol / WecA / WbpL.
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