Trifluoromethyl ketone inhibitors of fatty acid amide hydrolase: a probe of structural and conformational features contributing to inhibition
| Autor: | Matthew P. Patricelli, Dale L. Boger, Benjamin F. Cravatt, Aaron E. Lerner, Jean E. Patterson, Bryce J. Austin, Haruhiko Sato |
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| Rok vydání: | 1999 |
| Předmět: |
Stereochemistry
Clinical Biochemistry Pharmaceutical Science Oleic Acids Biochemistry Chemical synthesis Amidohydrolases chemistry.chemical_compound Inhibitory Concentration 50 Fatty acid amide hydrolase Drug Discovery Hydrolase Molecular Biology chemistry.chemical_classification Fatty acid amide biology Organic Chemistry Temperature Substrate (chemistry) Ketones Haloketone chemistry Enzyme inhibitor Electrophile biology.protein Molecular Medicine lipids (amino acids peptides and proteins) |
| Zdroj: | Bioorganicmedicinal chemistry letters. 9(2) |
| ISSN: | 0960-894X |
| Popis: | The examination of a series of trifluoromethyl ketone inhibitors of Fatty Acid Amide Hydrolase (FAAH, oleamide hydrolase, anandamide amidohydrolase) is detailed in efforts that define structural and conformational properties that contribute to enzyme inhibition and substrate binding. The results imply an extended bound conformation, highlight a role for the presence, position, and stereochemistry of a Δ9.10 cis double bond, and suggest little apparent role for C11-C18/C22 of the fatty acid amide substrates. The examination of a series of trifluoromethyl ketone inhibitors of Fatty Acid Amide Hydrolase (FAAH, oleamide hydrolase, anandamide amidohydrolase) is detailed in efforts that define structural and conformational properties that contribute to enzyme inhibition and substrate binding. |
| Databáze: | OpenAIRE |
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