1-Oxazolo[4,5-b]pyridin-2-yl-1-dodecanone

Fatty acid amide hydrolase (FAAH) is the enzyme responsible for hydrolysis and inactivation of fatty acid amides including anandamide and oleamide. CAY10435 is a selective, potent inhibitor of rat FAAH exhibiting a K_i value of 0.57 nM. Using a proteonomics approach, CAY10435 was screened against the serine hydrolase family of enzymes, of which FAAH is a member. In this assay, CAY10435 exhibited IC₅₀ values of 0.81 nM, 83 nM, and 50 μM for FAAH, triacylglycerol hydrolase (TGH), and an uncharacterized hydrolase (KIAA1363), respectively. Knowledge of the specificity of CAY10435 obtained from this experiment should allow for more accurate interpretation of results using the inhibitor in complex environments such as whole cells or animals.

CAY10435 is a β-ketooxazapyridine, selective FAAH inhibitor with antimicrobial activity. CAY10435 binds non-competitively to the FAAH of Dictyostelium discoideum with a Kd value of 0.57 nM[1][2].

ChEBI: CAY10435 is an oxazolopyridine.

[1] Hayes AC, et al. Identification of N-acylethanolamines in Dictyostelium discoideum and confirmation of their hydrolysis by fatty acid amide hydrolase. J Lipid Res. 2013 Feb;54(2):457-66. DOI:10.1194/jlr.M032219
[2] Glaser ST, et al. Ex vivo imaging of fatty acid amide hydrolase activity and its inhibition in the mouse brain. J Pharmacol Exp Ther. 2006 Mar;316(3):1088-97. DOI:10.1124/jpet.105.094748