The fatty acid amide hydrolase (FAAH)

Prostaglandins Leukot Essent Fatty Acids. Feb-Mar 2002;66(2-3):201-10. doi: 10.1054/plef.2001.0358.

Abstract

The fatty acid amide hydrolase (FAAH), is the enzyme responsible for the hydrolysis of anandamide, an endocannabinoid. The FAAH knockout, the assays for FAAH, the activity of its substrates, its reversibility and its cloning from rat, mouse, human, and pig are covered in this review. The conserved regions of FAAH are described in terms of sequence and function, including the domains that contains the serine catalytic nucleophile, the hydrophobic domain important for self-association, the proline rich domain region which may be important for subcellular localization and the fatty acid chain binding domain. The FAAH mouse promoter region was characterized in terms of its transcription start site and its activity in different cell types. The distribution of FAAH in the major organs in the body is described as well as regional distribution in the brain and its correlation with cannabinoid receptors. Since FAAH is recognized as a drug target, a large number of inhibitors have been synthesized and tested since 1994 and these are reviewed in terms of reversibility, potency, and specificity for FAAH.

Publication types

  • Review

MeSH terms

  • Amidohydrolases / antagonists & inhibitors*
  • Amidohydrolases / chemistry
  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism*
  • Animals
  • Arachidonic Acids / metabolism
  • Base Sequence
  • Cannabinoid Receptor Modulators
  • Catalysis
  • Endocannabinoids
  • Gene Deletion
  • Humans
  • Molecular Sequence Data
  • Polyunsaturated Alkamides
  • Protein Structure, Tertiary
  • Substrate Specificity

Substances

  • Arachidonic Acids
  • Cannabinoid Receptor Modulators
  • Endocannabinoids
  • Polyunsaturated Alkamides
  • Amidohydrolases
  • fatty-acid amide hydrolase
  • anandamide