ArticleThe Journal of biological chemistry2009
Purification and characterization of the lipid A 1-phosphatase LpxE of Rhizobium leguminosarum.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- TheMicroorganisms · 2021Article
- Article
- Lipid A fromInternational journal of molecular sciences · 2020Article
- Metabolic engineering of Escherichia coli to produce a monophosphoryl lipid A adjuvant.Metabolic engineering · 2020Article
- Article
- Identification ofFrontiers in microbiology · 2017Article
- A Surfactant-Induced Functional Modulation of a Global Virulence Regulator from Staphylococcus aureus.PloS one · 2016Article
- Kdo2 -lipid A: structural diversity and impact on immunopharmacology.Biological reviews of the Cambridge Philosophical Society · 2015Review
- Fast induction of biosynthetic polysaccharide genes lpxA, lpxE, and rkpI of Rhizobium sp. strain PRF 81 by common bean seed exudates is indicative of a key role in symbiosis.Functional & integrative genomics · 2013Article
- Article
- Phosphate groups of lipid A are essential for Salmonella enterica serovar Typhimurium virulence and affect innate and adaptive immunity.Infection and immunity · 2012Article
- Characterization of galacturonosyl transferase genes rgtA, rgtB, rgtC, rgtD, and rgtE responsible for lipopolysaccharide synthesis in nitrogen-fixing endosymbiont Rhizobium leguminosarum: lipopolysaccharide core and lipid galacturonosyl residues confer membrane stability.The Journal of biological chemistry · 2012Article
- Helicobacter pylori versus the host: remodeling of the bacterial outer membrane is required for survival in the gastric mucosa.PLoS pathogens · 2011Article
- Contribution of Porphyromonas gingivalis lipopolysaccharide to periodontitis.Periodontology 2000 · 2010Review
- Escherichia coli mutants that synthesize dephosphorylated lipid A molecules.Biochemistry · 2010Article
- Altered lipid A structures and polymyxin hypersensitivity of Rhizobium etli mutants lacking the LpxE and LpxF phosphatases.Biochimica et biophysica acta · 2010Article
- WaaA of the hyperthermophilic bacterium Aquifex aeolicus is a monofunctional 3-deoxy-D-manno-oct-2-ulosonic acid transferase involved in lipopolysaccharide biosynthesis.The Journal of biological chemistry · 2009Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
LpxE, a membrane-bound phosphatase found in Rhizobium leguminosarum and some other Gram-negative bacteria, selectively dephosphorylates the 1-position of lipid A on the outer surface of the inner membrane. LpxE belongs to the family of lipid phosphate phosphatases that contain a tripartite active site motif and six predicted transmembrane helices. Here we report the purification and characterization of R. leguminosarum LpxE. A modified lpxE gene, encoding a protein with an N-terminal His6 tag, was expressed in Escherichia coli. The protein was solubilized with Triton X-100 and purified to near-homogeneity. Gel electrophoresis reveals a molecular weight consistent with the predicted 31 kDa. LpxE activity is dependent upon Triton X-100, optimal near pH 6.5, and Mg2+-independent. The H197A and R133A substitutions inactivate LpxE, as does treatment with diethyl pyrocarbonate. In a mixed micelle assay system, the apparent Km for the precursor lipid IV(A) is 11 microm. Substrates containing the 3-deoxy-d-manno-oct-2-ulosonic acid disaccharide are dephosphorylated at similar rates to lipid IV(A), whereas glycerophospholipids like phosphatidic acid or phosphatidylglycerol phosphate are very poor substrates. However, an LpxE homologue present in Agrobacterium tumefaciens is selective for phosphatidylglycerol phosphate, demonstrating the importance of determining substrate specificity before assigning the functions of LpxE-related proteins. The availability of purified LpxE will facilitate the preparation of novel 1-dephosphorylated lipid A molecules that are not readily accessible by chemical methods.
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