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Titolo:
Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression and site-directed mutagenesis
Autore:
Goparaju, SK; Kurahashi, Y; Suzuki, H; Ueda, N; Yamamoto, S;
Indirizzi:
Univ Tokushima, Sch Med, Dept Biochem, Kuramoto, Tokushima 7708503, Japan Univ Tokushima Kuramoto Tokushima Japan 7708503 Tokushima 7708503, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
fascicolo: 1, volume: 1441, anno: 1999,
pagine: 77 - 84
SICI:
1388-1981(19991018)1441:1<77:AAOPBC>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID AMIDE HYDROLASE; CANNABINOID RECEPTOR-LIGAND; MOLECULAR CHARACTERIZATION; RAT-BRAIN; IDENTIFICATION; HYDROLYSIS; ENZYME; 2-ARACHIDONOYLGLYCEROL; PROTEIN; AGONIST;
Keywords:
anandamide; cannabinoid; amidohydrolase; fatty acid amide hydrolase; brain; (pig);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, S Univ Tokushima, Sch Med, Dept Biochem, Kuramoto, Tokushima 7708503, Japan Univ Tokushima Kuramoto Tokushima Japan 7708503 708503, Japan
Citazione:
S.K. Goparaju et al., "Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression and site-directed mutagenesis", BBA-MOL C B, 1441(1), 1999, pp. 77-84

Abstract

Anandamide (arachidonoylethanolamide) is an endogenous ligand for cannabinoid receptors, and its cannabimimetic activities are lost when the compoundis hydrolyzed to arachidonic acid and ethanolamine by an enzyme referred to as anandamide amidohydrolase. We cloned a cDNA for the enzyme of porcine brain, and the cDNA encoded a protein of 579 amino acids with a molecular mass of 62.9 kDa. The amino acid sequence was 81, 80 and 85% identical with the enzymes previously cloned from the liver of rat, mouse, and human, respectively. When the enzyme protein was overexpressed in COS-7 cells, the particulate fraction of the cells showed an anandamide hydrolyzing activity and also catalyzed the reverse reaction synthesizing anandamide from arachidonic acid and ethanolamine both with a specific activity of 0.2-0.3 mu mol/min/mg protein at 37 degrees C. The brain enzyme exhibited a wide substrate specificity hydrolyzing oleamide, 2-arachidonoylglycerol, and methyl arachidonate. The point mutation of Ser-217, Asp-237, Ser-241, or Cys-249 completely abolished the hydrolyses of all the above-mentioned substrates as well as the synthesis of anandamide in the reverse reaction. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/20 alle ore 20:59:27