Article ID Journal Published Year Pages File Type
10763602 Biochemical and Biophysical Research Communications 2011 6 Pages PDF
Abstract
► We identified LpxD as a binding partner of NPr of the Escherichia coli nitrogen PTS. ► LpxD shows a preferential interaction with dephosphorylated NPr. ► LpxD catalyzes biosynthesis of the bacterial endotoxin lipid A and lipopolysaccharide. ► A npr mutant shows increased lipopolysaccharide synthesis and rifampin resistance.
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Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Preview
Dephosphorylated NPr of the nitrogen PTS regulates lipid A biosynthesis by direct interaction with LpxD
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