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Introduction

Fatty acid amide hydrolase (FAAH) degrades fatty acid amides to terminate their signaling activity. A serine hydrolase from the Amidase signature superfamily of enzymes (other amidases), FAAH degrades endocannabinoid signaling lipids, molecules associated with pain relief. Because endocannabinoids are lipid molecules, they cannot be compartmentalized in vesicles (the degradation method for other neurotransmitters) and must instead be degraded in the bilayer of the cell membrane. FAAH is an integral membrane protein that degrades FAAs as they enter the membrane bilayer. Current research about FAAH aims to find inhibitors for the enzyme, which would prolong the pain alleviation provided by endocannabinoid molecules.

FAAH Subunit

Hydrolase Information

with

of 11 strands surrounded by 24 alpha helices

alpha helices 18 and 19 form a membrane binding cap

Catalytic Triad

Applications

The human nervous system has several types of chemical messengers, including amino acids, lipids, peptide hormones, and monoamines. FAAH primarily degrades anandamide (AEA), a naturally-occurring signaling lipid that functions in the brain. AEA brings pain relief to the body. Inhibiting FAAH would likely sustain AEA signaling, leading to prolonged pain relief and decreased inflammation.

Anandamide

References