ArticleScientific reports2019
A sensitive fluorescence-based assay to monitor enzymatic activity of the essential integral membrane protein Apolipoprotein N-acyltransferase (Lnt).
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Lipid Metabolism and Immune Function: Chemical Tools for Insights into T-Cell Biology.Chembiochem : a European journal of chemical biology · 2025Review
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
- Monitoring Enzyme Activity Using Near-Infrared Fluorescent Single-Walled Carbon Nanotubes.ACS sensors · 2024Review
- Components Subcellular Localization: Identification of Lipoproteins Using Alkyne Fatty Acids and Click Chemistry.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A GMR enzymatic assay for quantifying nuclease and peptidase activity.Frontiers in bioengineering and biotechnology · 2024Article
- Dawn of a New Era for Membrane Protein Design.Biodesign research · 2022Review
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- Mode of action of lipoprotein modification enzymes-Novel antibacterial targets.Molecular microbiology · 2021Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoprotein modification is an essential process in Gram-negative bacteria. The action of three integral membrane proteins that catalyze the transfer of fatty acids derived from membrane phospholipids or cleave the signal peptide of the lipoprotein substrate result in the formation of mature triacylated proteins. Inactivation of the enzymes leads to mis-localization of immature lipoproteins and consequently cell death. Biochemical studies and the development of in vitro assays are challenging due to the fact that the enzymes and substrates are all membrane-embedded proteins difficult to overproduce and purify. Here we describe a sensitive fluorescence-based assay to monitor bacterial apolipoprotein N-acyltransferase activity.
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