Velasco Bucheli, RodrigoHormigo, DanielFernández-Lucas, JesúsTorres Ayuso, PedroAlfaro Ureña, YohanaSaborido Modia, AnaSerrano Aguirre, LaraGarcía, José LuisRamón, FernandoAcebal Sarabia, CarmenSantos de la Sen, AntonioArroyo Sánchez, MiguelDe La Mata Riesco, Mª Isabel2023-06-172023-06-172020-07-01Electronic: 2073-434410.3390/catal10070730https://hdl.handle.net/20.500.14352/7938Many 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.engAtribución 3.0 Españajournal articlehttps://doi.org/10.3390/catal10070730https://www.mdpi.com/2073-4344/10/7/730open access577.15579.87615.33Penicillin acylaseAculeacin acylaseN-acyl-homoserine lactone acylasesQuorum quenchingBiofouling Penicillin acylaseBiofoulingBioquímica (Biología)Microbiología (Biología)2302 Bioquímica2414 Microbiología