Summary The carboxylesterases (EC 3.1.1.x) are widely distributed and form an important yet diverse group of hydrolases catalysing the ester bond cleavage in a variety of substrates. Besides acting on plant cell wall components like cutin, tannin and feruloyl esters, they are often the first line of defence to metabolize drugs, xenobiotics, pesticides, insecticides and plastic. But for the promiscuity of some carboxylesterases and cutinases, very few enzymes act exclusively on aromatic carboxylic acid esters. Infrequent occurrence of aromatic carboxylesterases suggests that aromatic carboxylesters are inherently more difficult to hydrolyse than the regular carboxylesters because of both steric and polar effects. Naturally occurring aromatic carboxylesters were rare before the anthropogenic activity augmented their environmental presence and diversity. An appraisal of the literature shows that the hydrolysis of aromatic carboxylic esters is a uniquely difficult endeavour and hence deserves special attention. Enzymes to hydrolyse such esters are evolving rapidly in nature. Very few such enzymes are known and they often display much lower catalytic efficiencies. Obviously, the esters of aromatic carboxylic acids, including polyethylene terephthalate waste, pose an environmental challenge. In this review, we highlight the uniqueness of aromatic carboxylesters and then underscore the importance of relevant carboxylesterases.