Catalysts (Jul 2020)

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

  • Rodrigo Velasco-Bucheli,
  • Daniel Hormigo,
  • Jesús Fernández-Lucas,
  • Pedro Torres-Ayuso,
  • Yohana Alfaro-Ureña,
  • Ana I. Saborido,
  • Lara Serrano-Aguirre,
  • José L. García,
  • Fernando Ramón,
  • Carmen Acebal,
  • Antonio Santos,
  • Miguel Arroyo,
  • Isabel de la Mata

DOI
https://doi.org/10.3390/catal10070730
Journal volume & issue
Vol. 10, no. 7
p. 730

Abstract

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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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