Reactome | CES1 trimer.CES2 hydrolyse COCN to BEG

CES1 trimer.CES2 hydrolyse COCN to BEG

Stable Identifier

R-HSA-5693691

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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.

Literature References

PubMed ID	Title	Journal	Year
9169443	Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin Bosron, WF, Dean, RA, Kedishvili, NY, Pindel, EV, Zhang, J, Brzezinski, MR, Abraham, TL	J. Biol. Chem.	1997
12725862	Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition Redinbo, MR, Morton, CL, Danks, MK, Hyatt, JL, Bencharit, S, Potter, PM, Kuhn, P	Chem. Biol.	2003
7980644	Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine Bosron, WF, Dean, RA, Stone, CL, Brzezinski, MR, Abraham, TL	Biochem. Pharmacol.	1994