Anthranilate-CoA ligase (PqsA) (PqsA)

PqsA (Anthranilate-CoA ligase) is a key enzyme in the quorum-sensing network of the opportunistic pathogen Pseudomonas aeruginosa [Journal of Bacteriology, ACS Chemical Biology]. It initiates the biosynthesis of 2-alkyl-4-quinolones, including the Pseudomonas Quinolone Signal (PQS) and its precursor 2-heptyl-4-hydroxyquinoline (HHQ), by converting anthranilate into anthranilyl-CoA [Journal of Bacteriology]. These signaling molecules are critical for the density-dependent regulation of virulence factors such as pyocyanin, elastase, and lectins, as well as for the development of robust biofilms that contribute to antibiotic tolerance [Frontiers in Molecular Biosciences]. As an enzyme with no human homolog, PqsA is a prominent target for the development of antivirulence agents designed to attenuate bacterial pathogenicity without directly affecting cell viability [ACS Chemical Biology]. Inhibition of PqsA has been shown to reduce the production of quorum-sensing molecules and impair biofilm formation, making it a promising strategy for treating chronic P. aeruginosa infections, particularly in patients with cystic fibrosis or compromised immune systems [Frontiers in Microbiology]. Small-molecule inhibitors, such as anthranilyl-AMP mimics, have demonstrated the potential to block quinolone biosynthesis and reduce virulence in various infection models [Antimicrobial Agents and Chemotherapy].

Other names

Anthranilyl-CoA synthetaseAnthranilate-coenzyme A ligasepqsA gene product

Inhibition of anthranilate-CoA ligase activity to block the biosynthesis of Pseudomonas Quinolone Signal (PQS) and related virulence factors.