Hydrolase des amides d'acides gras

Fatty-acid amide hydrolase 1 or FAAH-1(, oleamide hydrolase, anandamide amidohydrolase) is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide (AEA), an N-acylethanolamine (NAE) in 1993. In humans, it is encoded by the gene FAAH. FAAH also regulate the contents of NAE's in Dictyostelium discoideum, as they modulate their NAE levels in vivo through the use of a semispecific FAAH inhibitor. The FAAH protein, involved in the metabolism of endocannabinoids, is encoded by the FAAH gene, which also contains the SNP rs324420 (C385A allele), associated with a higher sensitivity of FAAH to proteolytic degradation and a shorter half-life, as compared to the C variant, as the A variant displays normal catalytic properties, but an enhanced sensitivity to the proteolytic degradation, and shorter half-life, leading to increased N-acylethanolamine (NAE) and anandamide (AEA) signaling at the CB1 receptor etc., and which accounts for the protein’s lower amounts seen in high-level performance athletes (i.e., elite athletes), that present an extraordinary interindividual variability of physical, but also mental traits, which greatly influence their sports accomplishments and their career longevity. However, the role of the C385A variant in athletic performance is not consensual, as other evidence suggesting, that the A polymorphism allele genotype is underrepresented in the Polish elite athletes, regardless of metabolic characteristics of their sport disciplines, where it seems to affect the elite athletic performance negatively. 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: Anandamide (N-arachidonoylethanolamine), an endocannabinoid 2-arachidonoylglycerol (2-AG), an endocannabinoid.