Enzymological and molecular biological studies on anandamide amidohydrolase.
Previously we suggested that anandamide amidohydrolase partially purified from porcine brain catalyzed the anandamide synthesis. The reversibility of the anandamide hydrolytic reaction was confirmed with a recombinant enzyme of rat liver. We also showed that the recombinant enzyme had a wide substrate specificity hydrolyzing primary amides and esters of fatty acids in addition to anandamide. When the organ distribution of anandamide amidohydrolase was examined with rats, a large amount of the enzyme was contained in small intestine as well as liver and brain. The intestinal hydrolase was masked by endogenous lipid inhibitors. The enzyme was also found in various eye tissues.
Ueda
N
N
Department of Biochemistry, Tokushima University School of Medicine, Japan.
Katayama
K
K
Kurahashi
Y
Y
Suzuki
M
M
Suzuki
H
H
Yamamoto
S
S
Katoh
I
I
Di Marzo
V
V
De Petrocellis
L
L
D000581:Amidohydrolases / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D019556:COS Cells; D002460:Cell Line; D006801:Humans; D007700:Kinetics; D008297:Male; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D051381:Rats; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D014018:Tissue Distribution; D000099252:Fatty Acid Amide Hydrolases
D000581:Amidohydrolases; D012333:RNA, Messenger; D011994:Recombinant Proteins; D000099252:Fatty Acid Amide Hydrolases