Molecular characterization of human and mouse fatty acid amide hydrolases
AUTOR(ES)
Giang, Dan K.
FONTE
The National Academy of Sciences of the USA
RESUMO
Recently, we reported the isolation, cloning, and expression of a rat enzyme, fatty acid amide hydrolase (FAAH), that degrades bioactive fatty acid amides like oleamide and anandamide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Here, we report the molecular characterization of both a mouse and a human FAAH and compare these enzymes to the rat FAAH. The enzymes are well conserved in primary structure, with the mouse and rat FAAHs sharing 91% amino acid identity and the human FAAH sharing 82% and 84% identity with the rat FAAH and mouse FAAH, respectively. In addition, the expressed human and rat FAAHs behave biochemically as membrane proteins of comparable molecular size and show similar, but distinguishable, enzymological properties. The identification of highly homologous FAAH proteins in rat, mouse, and human supports a general role for the fatty acid amides in mammalian biology.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=20071Documentos Relacionados
- Human fatty acid synthase: properties and molecular cloning.
- Functional disassociation of the central and peripheral fatty acid amide signaling systems
- A missense mutation in human fatty acid amide hydrolase associated with problem drug use
- Relationship Between the Structures of Fatty Acid Amide Derivatives and Their Antimicrobial Activities
- Carbocyclic fatty acids in plants: Biochemical and molecular genetic characterization of cyclopropane fatty acid synthesis of Sterculia foetida