FAAH2 Human

Fatty Acid Amide Hydrolase 2 (FAAH2) is an enzyme that belongs to the amidase signature family of enzymes. This enzyme is responsible for the hydrolysis of a broad range of bioactive lipids, including those from the three main classes of fatty acid amides: N-acylethanolamines, fatty acid primary amides, and N-acyl amino acids . FAAH2 is a protein-coding gene and is associated with various metabolic pathways, including fatty acid metabolism .

The FAAH2 gene encodes a protein that shares a conserved protein motif with the amidase signature family of enzymes . The enzyme has a preference for monounsaturated acyl chains as substrates . The recombinant human FAAH2 protein is often produced with an N-terminal His-tag and corresponds to the amino acids 32-532 of the human FAAH2 . The theoretical molecular weight of the recombinant protein is approximately 57.4 kDa .

FAAH2 catalyzes the hydrolysis of endogenous amidated lipids such as the sleep-inducing lipid oleamide and the endocannabinoid anandamide . By hydrolyzing these bioactive lipids to their corresponding fatty acids, FAAH2 plays a crucial role in regulating the signaling functions of these molecules . The enzyme preferentially hydrolyzes monounsaturated substrates like anandamide compared to polyunsaturated substrates .

FAAH2 is involved in various physiological processes due to its role in lipid metabolism. The enzyme’s activity affects the levels of bioactive lipids, which are involved in signaling pathways related to sleep, pain, and inflammation . Genetic or pharmacologic knockdown of FAAH2 can increase levels of certain bioactive lipids, potentially influencing pain sensitivities and inflammatory responses .

Mutations or dysregulation of the FAAH2 gene have been associated with certain diseases, including non-syndromic X-linked intellectual disability and Alacrima, Achalasia, and Impaired Intellectual Development Syndrome . Understanding the function and regulation of FAAH2 can provide insights into the development of therapeutic strategies for these conditions.

Recombinant human FAAH2 is typically produced in E. coli and purified for research purposes . The recombinant protein is used in various biochemical assays to study the enzyme’s activity and its role in lipid metabolism .