Deciphering Physiological Functions of AHL Quorum Quenching Acylases

Putri D. Utari, Jan Vogel, Wim J. Quax*

*Corresponding author for this work

Research output: Contribution to journalReview articleAcademicpeer-review

28 Citations (Scopus)
346 Downloads (Pure)

Abstract

N-Acylhomoserine lactone (AHL)-acylase (also known as amidase or amidohydrolase) is a class of enzyme that belongs to the Ntn-hydrolase superfamily. As the name implies, AHL-acylases are capable of hydrolysing AHLs, the most studied signaling molecules for quorum sensing in Gram-negative bacteria. Enzymatic degradation of AHLs can be beneficial in attenuating bacterial virulence, which can be exploited as a novel approach to fight infection of human pathogens, phytopathogens or aquaculture-related contaminations. Numerous acylases from both prokaryotic and eukaryotic sources have been characterized and tested for the interference of quorum sensing-regulated functions. The existence of AHL-acylases in a multitude of organisms from various ecological niches, raises the question of what the physiological roles of AHL-acylases actually are. In this review, we attempt to bring together recent studies to extend our understanding of the biological functions of these enzymes in nature.

Original languageEnglish
Article number1123
Number of pages13
JournalFrontiers in Microbiology
Volume8
DOIs
Publication statusPublished - 19-Jun-2017

Keywords

  • N-acylhomoserine lactones
  • acylases
  • amidases
  • quorum sensing
  • quorum quenching
  • Ntn-hydrolases
  • HOMOSERINE LACTONE ACYLASE
  • N-ACYLHOMOSERINE LACTONES
  • PSEUDOMONAS-AERUGINOSA PAO1
  • SENSING SIGNAL MOLECULE
  • OF-THE-ART
  • ESCHERICHIA-COLI
  • PENICILLIN ACYLASE
  • ACTIVATED-SLUDGE
  • AEROBIC GRANULES
  • NTN-HYDROLASE

Cite this