A FAAH-regulated class of N-acyl taurines that activates TRP ion channels.

@article{Saghatelian2006AFC,
  title={A FAAH-regulated class of N-acyl taurines that activates TRP ion channels.},
  author={Alan Saghatelian and Michele K McKinney and Michael Bandell and Ardem Patapoutian and Benjamin F Cravatt},
  journal={Biochemistry},
  year={2006},
  volume={45 30},
  pages={9007-15}
}
Fatty acid amide hydrolase (FAAH) is an integral membrane enzyme that catabolizes several bioactive lipids in vivo. Most of the physiological substrates of FAAH characterized to date belong to the N-acyl ethanolamine (NAE) class of fatty acid amides, including the endocannabinoid anandamide, the anti-inflammatory lipid N-palmitoyl ethanolamine, and the satiating factor N-oleoyl ethanolamine. We recently identified a second structural class of fatty acid amides regulated by FAAH in vivo: the N… CONTINUE READING