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Titolo:
The fatty acid amide hydrolase (FAAH)
Autore:
Ueda, N; Puffenbarger, RA; Yamamoto, S; Deutsch, DG;
Indirizzi:
SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA SUNYStony Brook Stony Brook NY USA 11794 Biol, Stony Brook, NY 11794 USA Univ Tokushima, Sch Med, Dept Biochem, Tokushima 7708503, Japan Univ Tokushima Tokushima Japan 7708503 Biochem, Tokushima 7708503, Japan
Titolo Testata:
CHEMISTRY AND PHYSICS OF LIPIDS
fascicolo: 1-2, volume: 108, anno: 2000,
pagine: 107 - 121
SICI:
0009-3084(200011)108:1-2<107:TFAAH(>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
CANNABINOID-RECEPTOR-LIGAND; RAT-BRAIN MICROSOMES; CENTRAL-NERVOUS-SYSTEM; ANANDAMIDE AMIDOHYDROLASE; ENZYMATIC-SYNTHESIS; ENDOGENOUS LIGAND; CB1 RECEPTOR; N-ARACHIDONOYLETHANOLAMINE; MOLECULAR CHARACTERIZATION; PERIIMPLANTATION PERIOD;
Keywords:
fatty acid amide hydrolase; anandamide; 2-arachidonoylglycerol; oleamide; amidase; amidohydrolase;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
75
Recensione:
Indirizzi per estratti:
Indirizzo: Deutsch, DG SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Brook, NY 11794 USA
Citazione:
N. Ueda et al., "The fatty acid amide hydrolase (FAAH)", CHEM PHYS L, 108(1-2), 2000, pp. 107-121

Abstract

The topic of this review is fatty acid amide hydrolase (FAAH), one of the best-characterized enzymes involved in the hydrolysis of bioactive lipids such as anandamide, 2-arachidonoylglycerol (2-AG), and oleamide. Herein, we discuss the nomenclature, the various assays that have been developed, the relative activity of the various substrates and the reversibility of the enzyme reactions catalyzed by FAAH. We also describe the cloning of the enzyme from rat and subsequent cDNA isolation from mouse, human, and pig. The proteins and the mRNAs from different species are compared. Cloning the enzyme permitted the purification and characterization of recombinant FAAH. The conserved regions of FAAH are described in terms of sequence and function, including the amidase domain which contains the serine catalytic nucleophile, the hydrophobic domain important for self association, and the proline rich domain region, which may be important for subcellular localization. Thedistribution of FAAH in the major organs of the body is described as well as regional distribution in the brain and its correlation with cannabinoid receptors. Since FAAH is recognized as a drug target, a large number of inhibitors have been synthesized and tested since 1994 and these are reviewed in terms of reversibility, potency, and specificity for FAAH and cannabinoid receptors. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 21:04:42