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| http://dx.doi.org/10.1128/JB.00441-12 | DOI Listing |
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Lipoprotein -Acylation in Is Catalyzed by a Two-Component Acyl Transferase System.
mBio
July 2020
The Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, Pennsylvania, USA
Bacterial lipoproteins (Lpps) are a class of membrane-associated proteins universally distributed among all bacteria. A characteristic N-terminal cysteine residue that is variably acylated anchors C-terminal globular domains to the extracellular surface, where they serve numerous roles, including in the capture and transport of essential nutrients. Lpps are also ligands for the Toll-like receptor 2 (TLR2) family, a key component of the innate immune system tasked with bacterial recognition.
View Article and Find Full Text PDFBacterial lyso-form lipoproteins are synthesized via an intramolecular acyl chain migration.
J Biol Chem
July 2020
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania, USA
All bacterial lipoproteins share a variably acylated N-terminal cysteine residue. Gram-negative bacterial lipoproteins are triacylated with a thioether-linked diacylglycerol moiety and an -acyl chain. The latter is transferred from a membrane phospholipid donor to the α-amino terminus by the enzyme lipoprotein -acyltransferase (Lnt), using an active-site cysteine thioester covalent intermediate.
View Article and Find Full Text PDFConformational changes in Apolipoprotein N-acyltransferase (Lnt).
Sci Rep
January 2020
Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C, 10691, Stockholm, Sweden.
Lipoproteins are important components of the cell envelope and are responsible for many essential cellular functions. They are produced by the post-translational covalent attachment of lipids that occurs via a sequential 3-step process controlled by three integral membrane enzymes. The last step of this process, unique to Gram-negative bacteria, is the N-acylation of the terminal cysteine by Apolipoprotein N-acyltransferase (Lnt) to form the final mature lipoprotein.
View Article and Find Full Text PDFCopper-Induced Expression of a Transmissible Lipoprotein Intramolecular Transacylase Alters Lipoprotein Acylation and the Toll-Like Receptor 2 Response to Listeria monocytogenes.
J Bacteriol
July 2019
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania, USA
Bacterial lipoproteins are globular proteins anchored to the extracytoplasmic surfaces of cell membranes through lipidation at a conserved N-terminal cysteine. Lipoproteins contribute to an array of important cellular functions for bacteria, as well as being a focal point for innate immune system recognition through binding to Toll-like receptor 2 (TLR2) heterodimer complexes. Although lipoproteins are conserved among nearly all classes of bacteria, the presence and type of α-amino-linked acyl chain are highly variable and even strain specific within a given bacterial species.
View Article and Find Full Text PDFDesferrioxamine biosynthesis: diverse hydroxamate assembly by substrate-tolerant acyl transferase DesC.
Philos Trans R Soc Lond B Biol Sci
June 2018
Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK
Article Synopsis
- Hydroxamate groups are crucial in the biological activity of various natural products, including trichostatin A, which inhibits enzymes by binding zinc(II) ions, and desferrioxamines, which chelate iron using hydroxamate groups.
- The biosynthesis of desferrioxamines involves a condensation reaction catalyzed by the enzyme DesD, which combines derivatives of hydroxycadaverine.
- The study identifies the gene responsible for producing the acyl transferase DesC, which modifies hydroxycadaverine with different acyl groups, leading to the variety of desferrioxamines, while also revealing insights about the structure and function of the ferrioxamine B receptor.
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