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                  <mods:namePart>Velasco Bucheli, Rodrigo</mods:namePart>
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                  <mods:namePart>Torres Ayuso, Pedro</mods:namePart>
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                  <mods:namePart>Alfaro Ureña, Yohana</mods:namePart>
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                  <mods:namePart>Arroyo Sánchez, Miguel</mods:namePart>
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                  <mods:namePart>De La Mata Riesco, Mª Isabel</mods:namePart>
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                  <mods:dateAccessioned encoding="iso8601">2023-06-17T09:01:06Z</mods:dateAccessioned>
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               <mods:identifier type="issn">Electronic: 2073-4344</mods:identifier>
               <mods:identifier type="doi">10.3390/catal10070730</mods:identifier>
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               <mods: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.</mods:abstract>
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Aculeacin A Acylase from Actinoplanes utahensis:
Two Versatile Enzymes as Useful Tools for Quorum
Quenching Processes</mods:title>
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