ArticleAnalytical biochemistry2012
A continuous fluorescent enzyme assay for early steps of lipid A biosynthesis.
Article in Analytical biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- The role of the essential GTPase ObgE in regulating lipopolysaccharide synthesis in Escherichia coli.Nature communications · 2024Article
- (p)ppGpp and moonlighting RNases influence the first step of lipopolysaccharide biosynthesis inmicroLife · 2023Article
- Genetic mechanisms of Coxiella burnetii lipopolysaccharide phase variation.PLoS pathogens · 2018Article
- New virulence factor CSK29544_02616 as LpxA binding partner in Cronobacter sakazakii.Scientific reports · 2018Article
- Lipid A as a Drug Target and Therapeutic Molecule.Biomolecules & therapeutics · 2015Review
- PAINS in the assay: chemical mechanisms of assay interference and promiscuous enzymatic inhibition observed during a sulfhydryl-scavenging HTS.Journal of medicinal chemistry · 2015Article
- Extragenic suppressor mutations in ΔripA disrupt stability and function of LpxA.BMC microbiology · 2014Article
- Structural basis for the recognition of peptide RJPXD33 by acyltransferases in lipid A biosynthesis.The Journal of biological chemistry · 2014Article
- Dual targeting antibacterial peptide inhibitor of early lipid A biosynthesis.ACS chemical biology · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
UDP-N-acetylglucosamine acyltransferase (LpxA) and UDP-3-O-(R-3-hydroxyacyl)-glucosamine acyltransferase (LpxD) catalyze the first and third steps of lipid A biosynthesis, respectively. Both enzymes have been found to be essential for survival among gram-negative bacteria that synthesize lipopolysaccharide and are viable targets for antimicrobial development. Catalytically, both acyltransferases catalyze an acyl-acyl carrier protein (ACP)-dependent transfer of a fatty acyl moiety to a UDP-glucosamine core ring. Here, we exploited the single free thiol unveiled on holo-ACP after transfer of the fatty acyl group to the glucosamine ring using the thiol-specific labeling reagent, ThioGlo. The assay was continuously monitored as a change in fluorescence at λ(ex)=379 nm and λ(em)=513 nm using a microtiter plate reader. This assay marks the first continuous and nonradioactive assay for either acyltransferase.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.