Aldridge_1993_Chem.Biol.Interact_87_5

Many proteins capable of hydrolysing esters are present in biological material of all kinds (microorganisms, plants, invertebrates and vertebrates). Some serve, as indicated by their substrate specificity and distribution within organisms, a defined biological function. However for most esterases a rather general substrate specificity is found indicating that they may have a broad biological function. Their properties will be briefly reviewed with particular emphasis on inhibitors. The mechanism of hydrolysis of esters by many carboxylesterases (B-esterases) is well established largely due to the reaction of OP compounds with their catalytic centre. For others, such as enzymes hydrolysing (i) OP compounds and/or (ii) carboxyl esters which are not inhibited by a time and temperature dependent reaction by OP compounds, reaction mechanisms are still conjecture. The purpose of this presentation is to explore similarities and differences between the esterases and to discuss possible routes for progress in the A-esterase group.