Skip Navigation


Glycobiology Advance Access originally published online on April 20, 2005
Glycobiology 2005 15(9):29R-42R; doi:10.1093/glycob/cwi065
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
15/9/29R    most recent
cwi065v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Price, N. P.
Right arrow Articles by Momany, F. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Price, N. P.
Right arrow Articles by Momany, F. A.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© Published by Oxford University Press 2005.

REVIEW

Modeling bacterial UDP-HexNAc: polyprenol-P HexNAc-1-P transferases

Neil P. Price1,2 and Frank A. Momany3

2 USDA-ARS-NCAUR, Bioproducts and Biocatalysis Research Unit, 1815 North University Street, Peoria, IL 61604; and 3 Plant Polymer Research Unit, 1815 North University Street, Peoria, IL 61604


1 To whom correspondence should be addressed; e-mail: pricen{at}ncaur.usda.gov

Received on March 4, 2005; accepted on April 15, 2005

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 (CR) 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.

Key words: MraY / tunicamycin / undecaprenol / WecA / WbpL


Mention of trade names or commercial products in this article is solely for the purpose of providing specific information and does not imply recommendation or endorsement by the U.S. Department of Agriculture.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
GlycobiologyHome page
C. Noffz, S. Keppler-Ross, and N. Dean
Hetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle
Glycobiology, May 1, 2009; 19(5): 472 - 478.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Larue, M. S. Kimber, R. Ford, and C. Whitfield
Biochemical and Structural Analysis of Bacterial O-antigen Chain Length Regulator Proteins Reveals a Conserved Quaternary Structure
J. Biol. Chem., March 13, 2009; 284(11): 7395 - 7403.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
B. Al-Dabbagh, D. Mengin-Lecreulx, and A. Bouhss
Purification and Characterization of the Bacterial UDP-GlcNAc:Undecaprenyl-Phosphate GlcNAc-1-Phosphate Transferase WecA
J. Bacteriol., November 1, 2008; 190(21): 7141 - 7146.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
H. Shams-Eldin, B. Chaban, S. Niehus, R. T. Schwarz, and K. F. Jarrell
Identification of the Archaeal alg7 Gene Homolog (Encoding N-Acetylglucosamine-1-Phosphate Transferase) of the N-Linked Glycosylation System by Cross-Domain Complementation in Saccharomyces cerevisiae
J. Bacteriol., March 15, 2008; 190(6): 2217 - 2220.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
M. S. Saldias, K. Patel, C. L. Marolda, M. Bittner, I. Contreras, and M. A. Valvano
Distinct functional domains of the Salmonella enterica WbaP transferase that is involved in the initiation reaction for synthesis of the O antigen subunit
Microbiology, February 1, 2008; 154(2): 440 - 453.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
J. van Heijenoort
Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan
Microbiol. Mol. Biol. Rev., December 1, 2007; 71(4): 620 - 635.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
D. M. Aanensen, A. Mavroidi, S. D. Bentley, P. R. Reeves, and B. G. Spratt
Predicted Functions and Linkage Specificities of the Products of the Streptococcus pneumoniae Capsular Biosynthetic Loci
J. Bacteriol., November 1, 2007; 189(21): 7856 - 7876.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
J. Lehrer, K. A. Vigeant, L. D. Tatar, and M. A. Valvano
Functional Characterization and Membrane Topology of Escherichia coli WecA, a Sugar-Phosphate Transferase Initiating the Biosynthesis of Enterobacterial Common Antigen and O-Antigen Lipopolysaccharide
J. Bacteriol., April 1, 2007; 189(7): 2618 - 2628.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.