%0 Journal Article
%A Velasco Bucheli, Rodrigo
%A Hormigo, Daniel
%A Fernández-Lucas, Jesús
%A Torres Ayuso, Pedro
%A Alfaro Ureña, Yohana
%A Saborido Modia, Ana Isolina
%A Serrano Aguirre, Lara
%A García, José Luis
%A Ramón, Fernando
%A Acebal Sarabia, Carmen
%A Santos de la Sen, Antonio
%A Arroyo Sánchez, Miguel
%A De La Mata Riesco, Mª Isabel
%T Penicillin Acylase from Streptomyces lavendulae andAculeacin A Acylase from Actinoplanes utahensis:Two Versatile Enzymes as Useful Tools for QuorumQuenching Processes
%D 2020
%@ Electronic: 2073-4344
%U https://hdl.handle.net/20.500.14352/7938
%X Many Gram-negative bacteria produce N-acyl-homoserine lactones (AHLs), quorum sensing (QS) molecules that can be enzymatically inactivated by quorum quenching (QQ) processes; this approach is considered an emerging antimicrobial alternative. In this study, kinetic parameters of several AHLs hydrolyzed by penicillin acylase from Streptomyces lavendulae (SlPA) and aculeacin A acylase from Actinoplanes utahensis (AuAAC) have been determined. Both enzymes catalyze efficiently the amide bond hydrolysis in AHLs with different acyl chain moieties (with or without 3-oxo modification) and exhibit a clear preference for AHLs with long acyl chains (C12-HSL > C14-HSL > C10-HSL > C8-HSL for SlPA, whereas C14-HSL > C12-HSL > C10-HSL > C8-HSL for AuAAC). Involvement of SlPA and AuAAC in QQ processes was demonstrated by Chromobacterium violaceum CV026-based bioassays and inhibition of biofilm formation by Pseudomonas aeruginosa, a process controlled by QS molecules, suggesting the application of these multifunctional enzymes as quorum quenching agents, this being the first time that quorum quenching activity was shown by an aculeacin A acylase. In addition, a phylogenetic study suggests that SlPA and AuAAC could be part of a new family of actinomycete acylases, with a preference for substrates with long aliphatic acyl chains, and likely involved in QQ processes.
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