Preparative enzymatic synthesis of polyprenyl-pyrophosphoryl-N-acetylglucosamine, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope polymers

被引：10
作者：
Al-Dabbagh, Bayan [1 ]
Blanot, Didier [1 ]
Mengin-Lecreulx, Dominique [1 ]
Bouhss, Ahmed [1 ]
机构：
[1] Univ Paris 11, Inst Biochim & Biophys Mol & Cellulaire, CNRS UMR 8619, Lab Enveloppes Bacteriennes & Antibiot, F-91405 Orsay, France
来源：
ANALYTICAL BIOCHEMISTRY | 2009年 / 391卷 / 02期
关键词：
ENTEROBACTERIAL COMMON ANTIGEN; ESCHERICHIA-COLI; LIPOPOLYSACCHARIDE; WECA; WALL; GENE;
D O I：
10.1016/j.ab.2009.05.011
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The WecA transferase is an integral membrane protein and a member of the polyprenyl phosphate N-acetylhexosamine-1-phosphate transferase superfamily. It initiates the biosynthesis of various bacterial cell envelope components such as the lipopolysaccharide O-antigen. We report on the first large-scale enzymatic synthesis, Purification, and characterization of the undecaprenyl-pyrophosphoryl-N-acetylglucosa mine product of the WecA transferase. This is an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. Its availability in a pure form will allow the biochemical and structural characterization of the various enzymes requiring it as a substrate for the synthesis of cell wall polymers. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码：163 / 165
页数：3
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