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-acetylglucosamine 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.
lipid, enzymatic synthesis, Acetylglucosamine, biocatalysis, WecA transferase, bacterial cell envelope
NCBI PubMed ID: 19442646Journal NLM ID: 0370535Publisher: Academic Press
Correspondence: ahmed.bouhss@u-psud.fr
Institutions: Univ Paris-Sud, UMR 8619, Institut de Biochimie et de Biophysique Moleculaire et Cellulaire, Orsay 91405, France
Methods: TLC, MALDI-TOF MS, biochemical methods
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