Penicillin Acylase from Streptomyces lavendulae and Aculeacin A Acylase from Actinoplanes utahensis: Two Versatile Enzymes as Useful Tools for Quorum Quenching Processes

Many Gram-negative bacteria produceN-acyl-homoserine lactones (AHLs), quorum sensing(QS) molecules that can be enzymatically inactivated by quorum quenching (QQ) processes; this approachis considered an emerging antimicrobial alternative. In this study, kinetic parameters of several AHLshydrolyzed b...

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Detalles Bibliográficos
Autores: Velasco Bucheli, Rodrigo, Hormigo Cisneros, Daniel, Fernández Lucas, Jesús, Torres Ayuso, Pedro, Alfaro Ureña, Yohana, Saborido, Ana Isabel, Serrano Aguirre, Lara, García, José Luis, Ramón, Fernando, Acebal Sarabia, Carmen, Santos, Antonio, Arroyo Sánchez, Miguel, Mata Riesco, Isabel de la
Tipo de recurso: artículo
Fecha de publicación:2020
País:España
Institución:Universidad Europea (UEM)
Repositorio:ABACUS. Repositorio de Producción Científica
Idioma:inglés
OAI Identifier:oai:abacus.universidadeuropea.com:11268/10970
Acceso en línea:http://hdl.handle.net/11268/10970
Access Level:acceso abierto
Palabra clave:Penicilina amidasa
Enzimas
Salud
Bacteria
Descripción
Sumario:Many Gram-negative bacteria produceN-acyl-homoserine lactones (AHLs), quorum sensing(QS) molecules that can be enzymatically inactivated by quorum quenching (QQ) processes; this approachis considered an emerging antimicrobial alternative. In this study, kinetic parameters of several AHLshydrolyzed by penicillin acylase fromStreptomyces lavendulae(SlPA) and aculeacin A acylase fromActinoplanes utahensis(AuAAC) have been determined. Both enzymes catalyze efficiently the amide bondhydrolysis in AHLs with different acyl chain moieties (with or without 3-oxo modification) and exhibit aclear preference for AHLs with long acyl chains (C12-HSL>C14-HSL>C10-HSL>C8-HSL forSlPA,whereas C14-HSL>C12-HSL>C10-HSL>C8-HSL forAuAAC). Involvement ofSlPA andAuAAC inQQ processes was demonstrated byChromobacterium violaceumCV026-based bioassays and inhibitionof biofilm formation byPseudomonas aeruginosa, a process controlled by QS molecules, suggesting theapplication of these multifunctional enzymes as quorum quenching agents, this being the first time thatquorum quenching activity was shown by an aculeacin A acylase. In addition, a phylogenetic studysuggests thatSlPA andAuAAC could be part of a new family of actinomycete acylases, with a preferencefor substrates with long aliphatic acyl chains, and likely involved in QQ processes.

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