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FAAH

FAAH
Identifiers
Aliases FAAH, fatty acid amide hydrolase, FAAH-1, PSAB
External IDs MGI: 109609 HomoloGene: 68184 GeneCards: FAAH
Targeted by Drug
pf-04457845, urb-597
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001441

NM_010173

RefSeq (protein)

NP_001432

NP_034303.3
NP_034303

Location (UCSC) Chr 1: 46.39 – 46.41 Mb Chr 4: 115.97 – 116.02 Mb
PubMed search

NM_001441

NM_010173

NP_001432

NP_034303.3
NP_034303

Fatty acid amide hydrolase or FAAH (EC 3.5.1.99, oleamide hydrolase, anandamide amidohydrolase) is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide in 1993. In humans, it is encoded by the gene FAAH.

FAAH is an integral membrane hydrolase with a single N-terminal transmembrane domain. In vitro, FAAH has esterase and amidase activity.In vivo, FAAH is the principal catabolic enzyme for a class of bioactive lipids called the fatty acid amides (FAAs). Members of the FAAs include:

FAAH knockout mice display highly elevated (>15-fold) levels of N-acylethanolamines and N-acyltaurines in various tissues. Because of their significantly elevated anandamide levels, FAAH KOs have an analgesic phenotype, showing reduced pain sensation in the hot plate test, the formalin test, and the tail flick test. Finally, because of their impaired ability to degrade anandamide, FAAH KOs also display supersensitivity to exogenous anandamide, a cannabinoid receptor (CB) agonist.


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