Search results for CES2

Showing 6 results out of 6

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Species

Types

Compartments

Reaction types

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Protein (2 results from a total of 2)

Identifier: R-HSA-5693713
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: CES2: O00748
Identifier: R-HSA-2429659
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: CES1: P23141

Set (1 results from a total of 1)

Identifier: R-HSA-5693688
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen

Interactor (1 results from a total of 1)

Identifier: P23141-3
Species: Homo sapiens
Primary external reference: UniProt: P23141-3

Reaction (2 results from a total of 2)

Identifier: R-HSA-5693691
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Cocaine (COCN) is an addictive, psychoactive alkaloid that is primarily inactivated by hydrolysis to benzoylecgonine (BEG), the major urinary metabolite of the drug. Human liver carboxylesterases 1 and 2 (CES1 and 2), located in the ER lumen, are involved in the detoxification of xenobiotics and can hydrolyse COCN to BEG (Brzezinski et al. 1994, Pindel et al. 1997). CES1 is functional as a homotrimer or homohexamer (Bencharit et al. 2003) whereas CES2 is monomeric.
Identifier: R-HSA-9619024
Species: Homo sapiens
Compartment: extracellular region
Mammalian carboxylesterases (CES) are a well conserved family that catalyse the hydrolysis of a vast array of endogenous and exogenous substrates including environmental toxins and drugs. CES-mediated hydrolysis plays an important role in the disposition of a number of widely prescribed therapeutic agents from a diverse range of drug classes including angiotensin-converting enzyme inhibitors (ACEIs). In humans, two carboxylesterases, CES1 and CES2, are important enzymes in drug metabolism (Brzezinski et al. 1994, Pindel et al. 1997). Both are expressed in liver but levels of CE1 are much higher than CE2. Most ACEI prodrugs (except captopril and lisinopril) are administered as esterified prodrugs which are probably susceptible to hydrolysis by CES1 trimer (Thomsen et al. 2014). The resultant active drugs (suffix 'prilat') can inhibit the conversion of angiotensin I to angiotensin II, thereby contributing to the antihypertensive effect of these drugs. Some CES1 genetic variants (eg. G143E) may impair ACEI activation, and consequently affect therapeutic outcomes of ACEI prodrugs (Wang et al. 2016).
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