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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

Crystal structures of FAAH show that the enzyme is a homodimer in solution, with each subunit having a mass of 63 kD. The protein's of 11 strands is surrounded by 24 alpha helices.

with

alpha helices 18 and 19 form a membrane binding cap

Catalytic Triad

Mutagenesis and inhibitor studies have shown that FAAH has a , consisting of S241, S217, and K142. Ser-Ser-Lys catalytic triads are not often seen in hydrolases, making FAAH an enzyme of interest for additional research. S241 acts as the catalytic nucleophile for the cleavage of amide bonds.