Acyl‐homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum‐quenching enzymes

• Published in: Molecular microbiology Vol. 47; no. 3; pp. 849 - 860
• Main Authors: Lin, Yi‐Han, Xu, Jin‐Ling, Hu, Jiangyong, Wang, Lian‐Hui, Ong, Say Leong, Leadbetter, Jared Renton, Zhang, Lian‐Hui
• Format: Journal Article
• Language: English
• Published: Oxford,UK Blackwell Science Ltd 01.02.2003; Blackwell Publishing Ltd
• Subjects: 4-Butyrolactone - analogs & derivatives; 4-Butyrolactone - metabolism; Amidohydrolases - chemistry; Amidohydrolases - genetics; Amidohydrolases - metabolism; Amino Acid Sequence; Animals; Bacteria; Betaproteobacteria - enzymology; Betaproteobacteria - growth & development; Betaproteobacteria - physiology; Biofilms; Biotechnology; Caenorhabditis elegans - growth & development; Cloning, Molecular; E coli; Enzymes; Gene Expression Regulation, Bacterial; Inactivation; Microbiology; Molecular Sequence Data; Molecules; Pseudomonas aeruginosa - enzymology; Pseudomonas aeruginosa - genetics; Pseudomonas aeruginosa - pathogenicity; Sequence Alignment; Sequence Analysis, DNA; Signal Transduction

Summary N ‐acylhomoserine lactones (AHLs) are used as signal molecules by many quorum‐sensing Proteobacteria. Diverse plant and animal pathogens use AHLs to regulate infection and virulence functions. These signals are subject to biological inactivation by AHL‐lactonases and AHL‐acylases. Previously...