FAAH




Fatty acid amide hydrolase (FAAH) dimer shown with covalent inhibitor (MAFP, yellow) bound in the active site.
Fatty acid amide hydrolase
Identifiers
Symbol FAAH
Entrez 2166
HUGO 3553
OMIM 602935
PDB 1MT5
RefSeq NM_001441
UniProt O00519
Other data
EC number 3.5.1.-
Locus Chr. 1 p35-p34

oleamide as well as the less well-characterized N-acyl taurines.

Due to its ability to regulate cannabinoid receptors.

FAAH was cloned in 1996 by Ben Cravatt at The Scripps Research Institute where it continues to be intensively studied and characterized.[3][4]

Inhibitors and assays

Both non-selective and selective inhibitors of the URB597 is widely regarded as the current 'gold standard' FAAH inhibitor.[citation needed] The enzyme is typically assayed making use of a radiolabelled anandamide substrate, which generates free labelled spectrophotometric methods have also been described.

References

  1. ^ McKinney M.K., Cravatt B.F., "Structure and Function of Fatty Acid Amide Hydrolase." Ann. Rev. Biochem. 74:411(2005). PMID 15952893
  2. ^ Sipe J.C., Chiang K., Gerber A.L., Beutler E., Cravatt B.F., "A missense mutation in human fatty acid amide hydrolase associated with problem drug use." Proc. Natl. Acad. Sci. U.S.A. 99:8394-8399(2002). PMID 12060782
  3. ^ Cravatt B.F., Giang D.K., Mayfield S.P., Boger D.L., Lerner, R.A.; "Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides"; Nature 384:83 (1996). PMID 8900284
  4. ^ Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (2002). "Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling". Science 298 (5599): 1793-6. doi:10.1126/science.1076535. PMID 12459591.
 
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