Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylglucosamine / analogs & derivatives*
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Acetylglucosamine / biosynthesis
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Acetylglucosamine / isolation & purification
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Biocatalysis
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Cell Wall / metabolism
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Escherichia coli Proteins / metabolism*
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Polyisoprenyl Phosphates / biosynthesis*
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Polyisoprenyl Phosphates / isolation & purification
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Polymers / chemistry
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Polymers / metabolism*
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Transferases (Other Substituted Phosphate Groups) / metabolism*
Substances
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Escherichia coli Proteins
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Polyisoprenyl Phosphates
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Polymers
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polyprenyl-pyrophosphoryl-N-acetylglucosamine
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Transferases (Other Substituted Phosphate Groups)
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wecA protein, E coli
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Acetylglucosamine