Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. Catalyzes the hydrolysis of the intermediate 2-aminobenzoylacetyl-CoA (2-ABA-CoA) to form 2-aminobenzoylacetate (2-ABA), the precursor of HHQ. In vitro, can also hydrolyze other substrates such as S-ethyl-acetothioacetate and acetoacetyl-CoA, but is inactive against anthraniloyl-CoA, malonyl-CoA and octanoyl-CoA (PubMed:25960261, PubMed:27082157). Beyond its thioesterase function, is involved in the regulation of diverse genes coding for key virulence determinants and biofilm development (PubMed:27851827). (2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA + H(+) Thioesterase activity, but not pyocyanine production, is inhibited by 2-(pyridin-3-yl)benzoic acid, 2-(1H-pyrrol-1-yl)benzoic acid and 3-methylthiophene-2-carboxylic acid. Compounds bind to the active center. kcat is 0.85 sec(-1) with S-ethyl-acetothioacetate as substrate. kcat is 0.36 sec(-1) with acetoacetyl-CoA as substrate. kcat is 0.022 sec(-1) with cysteamine-S-phosphate as substrate (PubMed:25960261). kcat is 7.2 min(-1) with S-(4-nitrobenzoyl)mercaptoethane as substrate (PubMed:19788310). Mutant is defective in pyocyanine and rhamnolipid production and fails to kill worms efficiently, but can still produce PQS (PubMed:12426334, PubMed:18776012). Deletion mutant produces increased levels of DHQ, resulting from intramolecular cyclization of 2-ABA-CoA (PubMed:25960261). As mutant can produce wild-type levels of PQS, it was originally thought that PqsE is not involved in HHQ/PQS biosynthesis (PubMed:12426334, PubMed:18776012). It was shown later that the role of PqsE can be taken over to some extent by the broad-specificity thioesterase TesB, explaining why the pqsE deletion mutant still synthesizes HHQ and PQS (PubMed:25960261). Belongs to the metallo-beta-lactamase superfamily.