Abstract
WaaL is a membrane enzyme that catalyzes the glycosidic bonding of a sugar at the proximal end of the undecaprenyl-diphosphate (Und-PP)-O-antigen with a terminal sugar of the lipid A-core oligosaccharide (OS). This is a critical step in lipopolysaccharide synthesis. We describe here an assay to perform the ligation reaction in vitro utilizing native substrates.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Blotting, Western / methods
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Carbon-Oxygen Ligases / isolation & purification
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Carbon-Oxygen Ligases / metabolism*
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Electrophoresis, Polyacrylamide Gel / methods
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Enzyme Assays / methods*
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Escherichia coli / enzymology*
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Escherichia coli / metabolism
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Escherichia coli Proteins / isolation & purification
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Escherichia coli Proteins / metabolism*
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Lipopolysaccharides / analysis
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Lipopolysaccharides / metabolism*
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O Antigens / metabolism*
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Silver Staining / methods
Substances
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Escherichia coli Proteins
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Lipopolysaccharides
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O Antigens
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Carbon-Oxygen Ligases
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WaaL protein, E coli