ArticleBiochemistry2010
The essential Escherichia coli apolipoprotein N-acyltransferase (Lnt) exists as an extracytoplasmic thioester acyl-enzyme intermediate.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Article
- Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification and Characterization of the LipoproteinbioRxiv : the preprint server for biology · 2024Article
- Biofilm Formation ofMicroorganisms · 2023Review
- Lysophosphatidylglycerol (LPG) phospholipase D maintains membrane homeostasis in Staphylococcus aureus by converting LPG to lysophosphatidic acid.The Journal of biological chemistry · 2023Article
- Structure snapshots reveal the mechanism of a bacterial membrane lipoproteinScience advances · 2023Article
- The Phospholipase A1 Activity of Glycerol Ester Hydrolase (Geh) Is Responsible for Extracellular 2-12(mSphere · 2023Article
- Breaking down the cell wall: Still an attractive antibacterial strategy.Frontiers in microbiology · 2022Review
- Mode of action of lipoprotein modification enzymes-Novel antibacterial targets.Molecular microbiology · 2021Review
- Bacterial lyso-form lipoproteins are synthesized via an intramolecular acyl chain migration.The Journal of biological chemistry · 2020Article
- A sensitive fluorescence-based assay to monitor enzymatic activity of the essential integral membrane protein Apolipoprotein N-acyltransferase (Lnt).Scientific reports · 2019Article
- Lipid moieties on lipoproteins of commensal and non-commensal staphylococci induce differential immune responses.Nature communications · 2017Article
- Structural insights into lipoprotein N-acylation byProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Crystal structure of E. coli apolipoprotein N-acyl transferase.Nature communications · 2017Article
- Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis.Nature communications · 2017Article
- The Proteome and Lipidome of Thermococcus kodakarensis across the Stationary Phase.Archaea (Vancouver, B.C.) · 2016Article
- Article
- Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are N-acylated by apolipoprotein N-acyltransferase BCG_2070c.BMC microbiology · 2013Article
- RNA-seq based identification and mutant validation of gene targets related to ethanol resistance in cyanobacterial Synechocystis sp. PCC 6803.Biotechnology for biofuels · 2012Article
- Environment-mediated accumulation of diacyl lipoproteins over their triacyl counterparts in Staphylococcus aureus.Journal of bacteriology · 2012Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Escherichia coli apolipoprotein N-acyltransferase (Lnt) transfers an acyl group from sn-1-glycerophospholipid to the free alpha-amino group of the N-terminal cysteine of apolipoproteins, resulting in mature triacylated lipoprotein. Here we report that the Lnt reaction proceeds through an acyl-enzyme intermediate in which a palmitoyl group forms a thioester bond with the thiol of the active site residue C387 that was cleaved by neutral hydroxylamine. Lnt(C387S) also formed a fatty acyl intermediate that was resistant to neutral hydroxylamine treatment, consistent with formation of an oxygen-ester linkage. Lnt(C387A) did not form an acyl-enzyme intermediate and, like Lnt(C387S), did not have any detectable Lnt activity, indicating that acylation cannot occur at other positions in the catalytic domain. The existence of this thioacyl-enzyme intermediate allowed us to determine whether essential residues in the catalytic domain of Lnt affect the first step of the reaction, the formation of the acyl-enzyme intermediate, or the second step in which the acyl chain is transferred to the apolipoprotein substrate. In the catalytic triad, E267 is required for the formation of the acyl-enzyme intermediate, indicating its role in enhancing the nucleophilicity of C387. E343 is also involved in the first step but is not in close proximity to the active site. W237, Y388, and E389 play a role in the second step of the reaction since acyl-Lnt is formed but N-acylation does not occur. The data presented allow discrimination between the functions of essential Lnt residues in catalytic activity and substrate recognition.
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Registered trials
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