Crystal Structure of Fatty Acid Amide Hydrolase Bound to the Carbamate Inhibitor URB597: Discovery of a Deacylating Water Molecule and Insight into Enzyme Inactivation

The endocannabinoid system regulates a wide range of physiological processes including pain, inflammation, and cognitive/emotional states. URB597 is one of the best characterized covalent inhibitors of the endocannabinoid-degrading enzyme fatty acid amide hydrolase (FAAH). Here, we report the struct...

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Veröffentlicht in:	Journal of molecular biology 2010-07, Vol.400 (4), p.743-754
Hauptverfasser:	Mileni, Mauro, Kamtekar, Satwik, Wood, David C., Benson, Timothy E., Cravatt, Benjamin F., Stevens, Raymond C.
Format:	Artikel
Sprache:	eng
Schlagworte:	AMIDASES AMIDES Amidohydrolases - antagonists & inhibitors Amidohydrolases - chemistry Benzamides - chemistry Benzamides - metabolism CARBAMATES Carbamates - chemistry Carbamates - metabolism CARBOXYLIC ACIDS Catalytic Domain catalytic mechanism CHYMOTRYPSIN CONVERGENCE CRYSTAL STRUCTURE Crystallography, X-Ray deacylating water Enzyme Inhibitors - chemistry Enzyme Inhibitors - metabolism ENZYMES fatty acid amide hydrolase (FAAH) FUNCTIONALS HYDROLASES HYPOTHESIS INACTIVATION INFLAMMATION LINERS MATERIALS SCIENCE Models, Molecular Protein Binding Protein Structure, Tertiary RESIDUES RESOLUTION SERINE SUBSTRATES TRYPSIN URB597 WATER
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