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• W2002317558 startingPage "4360" @default.
• W2002317558 abstract "Acyl homoserine lactones (acyl-HSLs) are important intercellular signaling molecules used by many bacteria to monitor their population density in quorum-sensing control of gene expression. These signals are synthesized by members of the LuxI family of proteins. To understand the mechanism of acyl-HSL synthesis we have purified the Pseudomonas aeruginosa RhlI protein and analyzed the kinetics of acyl-HSL synthesis by this enzyme. Purified RhlI catalyzes the synthesis of acyl-HSLs from acyl-acyl carrier proteins and S-adenosylmethionine. An analysis of the patterns of product inhibition indicated that RhlI catalyzes signal synthesis by a sequential, ordered reaction mechanism in which S-adenosylmethionine binds to RhlI as the initial step in the enzymatic mechanism. Because pathogenic bacteria such as P. aeruginosa use acyl-HSL signals to regulate virulence genes, an understanding of the mechanism of signal synthesis and identification of inhibitors of signal synthesis has implications for development of quorum sensing-targeted antivirulence molecules." @default.
• W2002317558 created "2016-06-24" @default.
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• W2002317558 date "1999-04-13" @default.
• W2002317558 modified "2023-10-16" @default.
• W2002317558 title "Acyl homoserine-lactone quorum-sensing signal generation" @default.
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• W2002317558 doi "https://doi.org/10.1073/pnas.96.8.4360" @default.
• W2002317558 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/16337" @default.
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