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Updated: Jul 29, 2026

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
The fatty acid amide hydrolase (FAAH).
D G Deutsch1, N Ueda, S Yamamoto
1Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-5215, USA. ddeutsch@notes.sunysb.edu
Fatty acid amide hydrolase (FAAH) is key to endocannabinoid breakdown. This review covers FAAH structure, function, genetics, distribution, and its role as a drug target, highlighting numerous inhibitors.
Area of Science:
- Biochemistry
- Enzymology
- Pharmacology
Background:
- Fatty acid amide hydrolase (FAAH) hydrolyzes anandamide, a crucial endocannabinoid.
- Understanding FAAH is vital for modulating the endocannabinoid system.
Purpose of the Study:
- To provide a comprehensive review of fatty acid amide hydrolase (FAAH).
- To detail FAAH's structure, function, genetic basis, and distribution.
- To explore FAAH as a drug target and review existing inhibitors.
Main Methods:
- Review of existing literature on FAAH.
- Analysis of FAAH sequence and functional domains.
- Characterization of the FAAH mouse promoter region.
- Examination of FAAH distribution in organs and brain regions.
- Compilation and analysis of FAAH inhibitors synthesized since 1994.
Main Results:
- Detailed description of conserved FAAH regions, including catalytic and binding domains.
- Characterization of the FAAH mouse promoter and its cell-type specific activity.
- Mapping of FAAH distribution in major organs and brain regions, correlating with cannabinoid receptors.
- Overview of numerous FAAH inhibitors, categorized by reversibility, potency, and specificity.
Conclusions:
- FAAH is a well-characterized enzyme with conserved functional domains across species.
- FAAH distribution suggests significant roles in both peripheral organs and the central nervous system.
- The extensive development of FAAH inhibitors underscores its importance as a therapeutic drug target.
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