ArticleThe Journal of biological chemistry2009
WaaA of the hyperthermophilic bacterium Aquifex aeolicus is a monofunctional 3-deoxy-D-manno-oct-2-ulosonic acid transferase involved in lipopolysaccharide biosynthesis.
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 20 papers.
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20 citing papers in PubMed, 34 citations in OpenAlex.
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- Evaluation of Azido 3-Deoxy-d-ACS omega · 2022Article
- Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter.Nature communications · 2022Article
- A study of Rose Bengal against a 2-keto-3-deoxy-d-Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Structure and Ligand-Binding Properties of the O Antigen ABC Transporter Carbohydrate-Binding Domain.Structure (London, England : 1993) · 2020Article
- Prdx4 limits caspase-1 activation and restricts inflammasome-mediated signaling by extracellular vesicles.The EMBO journal · 2019Article
- Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide.International journal of microbiology · 2018Review
- A lectin S-domain receptor kinase mediates lipopolysaccharide sensing in Arabidopsis thaliana.Nature immunology · 2015Article
- Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4'-kinase LpxK.The Journal of biological chemistry · 2014Article
- Assembly of lipopolysaccharide in Escherichia coli requires the essential LapB heat shock protein.The Journal of biological chemistry · 2014Article
- Mechanistic characterization of the tetraacyldisaccharide-1-phosphate 4'-kinase LpxK involved in lipid A biosynthesis.Biochemistry · 2013Article
- Being Aquifex aeolicus: Untangling a hyperthermophile's checkered past.Genome biology and evolution · 2013Article
- Crystal structure of LpxK, the 4'-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Evidence for a two-metal-ion mechanism in the cytidyltransferase KdsB, an enzyme involved in lipopolysaccharide biosynthesis.PloS one · 2011Article
- Interchangeable domains in the Kdo transferases of Escherichia coli and Haemophilus influenzae.Biochemistry · 2010Article
- Complete genome sequence of Thermocrinis albus type strain (HI 11/12).Standards in genomic sciences · 2010Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hyperthermophile Aquifex aeolicus belongs to the deepest branch in the bacterial genealogy. Although it has long been recognized that this unique Gram-negative bacterium carries genes for different steps of lipopolysaccharide (LPS) formation, data on the LPS itself or detailed knowledge of the LPS pathway beyond the first committed steps of lipid A and 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) synthesis are still lacking. We now report the functional characterization of the thermostable Kdo transferase WaaA from A. aeolicus and provide evidence that the enzyme is monofunctional. Compositional analysis and mass spectrometry of purified A. aeolicus LPS, showing the incorporation of a single Kdo residue as an integral component of the LPS, implicated a monofunctional Kdo transferase in LPS biosynthesis of A. aeolicus. Further, heterologous expression of the A. aeolicus waaA gene in a newly constructed Escherichia coli DeltawaaA suppressor strain resulted in synthesis of lipid IVA precursors substituted with one Kdo sugar. When highly purified WaaA of A. aeolicus was subjected to in vitro assays using mass spectrometry for detection of the reaction products, the enzyme was found to catalyze the transfer of only a single Kdo residue from CMP-Kdo to differently modified lipid A acceptors. The Kdo transferase was capable of utilizing a broad spectrum of acceptor substrates, whereas surface plasmon resonance studies indicated a high selectivity for the donor substrate.
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