Carboxylesterases that are responsible for the hydrolysis of ester and amide bonds. They have broad substrate specificity ranging from small molecule esters such as phenylester to long chain fatty acid esters and thioesters. They play a major role as determinants of pharmacokinetic behavior for most therapeutic agents containing an ester. By deesterification, they can activate or inactivate the agents. They also participate in detoxification of drugs such as cocaine and heroin in serum and liver. The resulting deesterified metabolites are secreted out in urine. They can also detoxify organophosphate and carbamate analogues used in agrochemicals or chemical nerve agents, such as malathion, sarin, tabun, and VX. In addition to the hydrolytic activity, they can perform transesterification, a reaction important for cholesterol homeostasis. Carboxylesterase deficiency may be associated with nonHodgkin lymphoma or Bcell lymphocytic leukemia. CES1 shares the serine hydrolase fold observed in other esterases.