N-(long-chain-acyl)ethanolamine deacylase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: H2O + N-(long-chain-acyl)ethanolamine = ethanolamine + a fatty acid. [EC:3.5.1.60, MetaCyc:3.5.1.60-RXN]

N-(long-chain-acyl)ethanolamine deacylase activity is a crucial enzymatic process involved in the hydrolysis of N-(long-chain-acyl)ethanolamines, commonly known as fatty acid amides (FAAs). These FAAs, including anandamide (AEA), are lipid signaling molecules that play important roles in various physiological functions, such as pain perception, appetite regulation, and neurotransmission. The enzyme catalyzes the removal of a fatty acid from the N-(long-chain-acyl)ethanolamine molecule, producing ethanolamine and a free fatty acid. This hydrolytic reaction effectively terminates the signaling activity of the FAA, thus contributing to the regulation of FAA-mediated processes. The enzyme, commonly known as FAAH (fatty acid amide hydrolase), is a serine hydrolase that utilizes a catalytic triad consisting of Ser, His, and Asp residues. This triad facilitates the nucleophilic attack of the hydroxyl group of Ser on the carbonyl carbon of the amide bond, leading to the formation of a tetrahedral intermediate. This intermediate then collapses to release the free fatty acid and ethanolamine. The activity of FAAH is crucial for maintaining homeostasis of FAA signaling. Inhibition of FAAH can lead to an accumulation of FAAs, potentially resulting in altered pain perception, appetite control, and mood. Conversely, increased FAAH activity can decrease FAA levels, potentially impacting these functions. The regulation of FAAH activity is therefore a promising target for the development of therapeutic strategies for various conditions, including pain, obesity, and neurological disorders.'
"

Proteins (1)

Compounds (11)