Carboxylesterase 2 (CES2) (CES2)

Human Carboxylesterase 2 (hCE2), encoded by the CES2 gene, is a major serine hydrolase enzyme primarily localized in the endoplasmic reticulum of cells in the gastrointestinal tract, liver, and kidney [2, 9, 21]. It plays a critical role in the first-pass metabolism and activation of various ester-containing prodrugs, most notably the chemotherapeutic agents irinotecan and capecitabine [2, 17, 21]. Unlike its counterpart hCE1, hCE2 exhibits a substrate preference for molecules with large alcohol moieties and small acyl groups [2, 3, 17]. Beyond its pharmacological importance in prodrug activation, hCE2 is involved in the detoxification of substances such as cocaine and heroin and participates in endogenous lipid and prostaglandin metabolism [2, 9, 17]. The expression levels of hCE2 in tumor tissues can serve as a predictive biomarker for treatment efficacy, while genetic polymorphisms in the CES2 gene are associated with significant inter-individual variability in drug response and safety, including the risk of severe gastrointestinal toxicity [9, 17, 21].

Other names

CE-2CES2A1PCE-2iCEhiCECES-2Intestinal carboxylesterase

Hydrolysis of ester, carbamate, and amide bonds in prodrugs to release active metabolites; detoxification of xenobiotics through hydrolysis.