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

Impacto

Downloads

Downloads per month over past year

Velasco Bucheli, Rodrigo and Hormigo, Daniel and Fernández-Lucas, Jesús and Torres Ayuso, Pedro and Alfaro Ureña, Yohana and Saborido Modia, Ana and Serrano Aguirre, Lara and García, José Luis and Ramón, Fernando and Acebal Sarabia, Carmen and Santos de la Sen, Antonio and Arroyo Sánchez, Miguel and Mata Riesco, Isabel de la (2020) Penicillin Acylase from Streptomyces lavendulae and Aculeacin A Acylase from Actinoplanes utahensis: Two Versatile Enzymes as Useful Tools for Quorum Quenching Processes. Catalysts, 10 (7). pp. 1-19. ISSN Electronic: 2073-4344

[thumbnail of Velasco- Buchelli, R. et al. Penicillin Acylase from Streptomyces lavendulae......pdf] PDF
Creative Commons Attribution.

2MB

Official URL: https://doi.org/10.3390/catal10070730




Abstract

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.


Item Type:Article
Uncontrolled Keywords:Penicillin acylase; Aculeacin acylase; N-acyl-homoserine lactone acylases; Quorum quenching; Biofouling Penicillin acylase; Aculeacin acylase; N-acyl-homoserine lactone acylases; Quorum quenching; Biofouling
Subjects:Medical sciences > Biology > Biochemistry
Medical sciences > Biology > Microbiology
ID Code:64551
Deposited On:22 Mar 2021 14:37
Last Modified:22 Mar 2021 17:44

Origin of downloads

Repository Staff Only: item control page