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Título:
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Penicillin Acylase from Streptomyces lavendulae andAculeacin A Acylase from Actinoplanes utahensis:Two Versatile Enzymes as Useful Tools for QuorumQuenching Processes
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Autores:
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Velasco Bucheli, Rodrigo ;
Hormigo, Daniel ;
Fernández-Lucas, Jesús ;
Torres Ayuso, Pedro ;
Alfaro Ureña, Yohana ;
Saborido Modia, Ana ;
Serrano Aguirre, Lara ;
García, José Luis ;
Ramón, Fernando ;
Acebal Sarabia, Carmen ;
Santos de la Sen, Antonio ;
Arroyo Sánchez, Miguel ;
Mata Riesco, Isabel de la
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Tipo de documento:
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texto impreso
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Editorial:
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MDPI, 2020-07-01
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Dimensiones:
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application/pdf
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Nota general:
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cc_by
info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias Biomédicas: Biología: Bioquímica
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Materia = Ciencias Biomédicas: Biología: Microbiología
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Tipo = Artículo
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Resumen:
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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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En línea:
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https://eprints.ucm.es/id/eprint/64551/1/Velasco-%20Buchelli%2C%20R.%20et%20al.%20Penicillin%20Acylase%20from%20Streptomyces%20lavendulae......pdf
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