Carboxylesterase 2

Carboxylesterase 2

Carboxylesterase 2 (CES2) is an enzyme that belongs to the carboxylesterase family, which is involved in the hydrolysis of ester and amide bonds. This enzyme plays a crucial role in the metabolism of various xenobiotics and endogenous substrates, including drugs, environmental toxins, and dietary substances.

Structure

Carboxylesterase 2 is a member of the serine hydrolase superfamily and is characterized by the presence of a catalytic triad composed of serine, histidine, and aspartate residues. The enzyme is typically found in the endoplasmic reticulum of cells and is highly expressed in the liver, intestine, and other tissues.

Function

CES2 is involved in the hydrolysis of a wide range of substrates, including prodrugs, which are inactive compounds that are metabolized into active drugs in the body. This enzyme is particularly important in the activation of certain anticancer agents, such as irinotecan, which is converted into its active form, SN-38, by CES2.

Clinical Significance

The activity of carboxylesterase 2 can significantly affect the pharmacokinetics and pharmacodynamics of drugs. Variations in CES2 expression and activity can lead to differences in drug efficacy and toxicity among individuals. Genetic polymorphisms in the CES2 gene have been associated with altered drug metabolism and response.

Research and Applications

Research on CES2 is ongoing to better understand its role in drug metabolism and to develop strategies to modulate its activity for therapeutic benefit. Inhibitors of CES2 are being investigated as potential tools to enhance the efficacy of certain drugs by preventing their premature hydrolysis.

Also see

• Carboxylesterase
• Drug metabolism
• Enzyme
• Pharmacokinetics
• Prodrug

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