Hydrolyzes acyl homoserine lactones with varying lengths of acyl chains, with a slight preference for substrates without 3-oxo substitution at the C3 position. Has only residual activity towards non-acyl lactones, and no activity towards non-cyclic esters. an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+) Binds 2 Zn(2+) ions per subunit. Completely inhibited by Cu(2+) and Ag(+). Partially inhibited by Cr(2+), Pb(2+) and Fe(2+). Mg(2+), Ca(2+), Mn(2+), Co(2+), Ni(2+), Zn(2+) and Cd(2+) have no effect on activity. The chelating agents EDTA, 2,2'bipyridine and o-phenanthroline have no effect on enzyme activity. Optimum pH is 8.0 with 3-oxo-C8-HSL as substrate. Activity increases with increase in pH from 6.0 to 8.0, and declines slightly at pH 9.0. Little or no activity at pH 5.0 or below. Stable below 37 degrees Celsius, activity decreases sharply after incubation for 2 hours at 45 degrees Celsius. Monomer. Belongs to the metallo-beta-lactamase superfamily.