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The fatty acid amide hydrolase (FAAH).

N Ueda1, R A Puffenbarger, S Yamamoto

  • 1Department of Biochemistry, School of Medicine, University of Tokushima, Kuramoto-cho, 770-8503, Tokushima, Japan.

Chemistry and Physics of Lipids
|December 7, 2000
PubMed
Summary

Fatty acid amide hydrolase (FAAH) is a key enzyme in lipid hydrolysis. This review details FAAH

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Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Neuroscience

Background:

  • Fatty acid amide hydrolase (FAAH) is a critical enzyme responsible for hydrolyzing bioactive lipids like anandamide.
  • Understanding FAAH's function is vital due to its role in lipid signaling pathways and its potential as a drug target.

Purpose of the Study:

  • To provide a comprehensive review of fatty acid amide hydrolase (FAAH).
  • To discuss FAAH nomenclature, assays, substrate activity, reversibility, and cloning across species.
  • To explore FAAH's structure, distribution, and its significance as a drug target for inhibitor development.

Main Methods:

  • Review of existing literature on FAAH nomenclature, assays, and substrate characterization.
  • Analysis of cloned FAAH sequences and protein structures from various species (rat, mouse, human, pig).
  • Compilation and comparison of data on FAAH distribution in organs and brain regions.
  • Review of synthesized FAAH inhibitors, assessing their reversibility, potency, and specificity.

Main Results:

  • Detailed comparison of FAAH proteins and mRNAs across different species, highlighting conserved regions.
  • Characterization of recombinant FAAH, including its amidase, hydrophobic, and proline-rich domains.
  • Mapping of FAAH distribution in major organs and brain regions, correlating with cannabinoid receptors.
  • Extensive review of FAAH inhibitors developed since 1994, detailing their pharmacological profiles.

Conclusions:

  • FAAH is a well-characterized enzyme with conserved structural and functional domains across species.
  • FAAH's distribution and its role in lipid hydrolysis underscore its importance in physiological processes.
  • The extensive development of FAAH inhibitors confirms its status as a significant drug target.

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