Marked activation of the N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase by divalent cations.
N-Acylethanolamines including anandamide (an endogenous ligand for cannabinoid receptors) are released from N-acylphosphatidylethanolamine (N-acyl-PE) by the catalysis of a phosphodiesterase of the phospholipase D type. The enzyme was solubilized from the particulate fractions of rat heart with the aid of octyl glucoside, and partially purified by anion-exchange chromatography. The enzyme hydrolyzed N-palmitoyl-PE with a specific activity of 17 nmol/min/mg protein at 37 degrees C. The enzyme activity increased dramatically up to 30-fold by millimolar order of Ca(2+). Ca(2+) could be replaced with other divalent cations such as Co(2+), Mg(2+), Mn(2+), Ba(2+), Sr(2+) and Ni(2+). The hydrolysis of N-arachidonoyl-PE (a precursor of anandamide) was also markedly stimulated by Ca(2+).
Ueda
N
N
Department of Biochemistry, Tokushima University, School of Medicine, Kuramoto-cho, 770-8503, Tokushima, Japan. nueda@kms.ac.jp
Liu
Q
Q
Yamanaka
K
K
D000818:Animals; D002384:Catalysis; D002413:Cations, Divalent; D004789:Enzyme Activation; D008297:Male; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar
D002413:Cations, Divalent; C431824:N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase; D010727:Phosphoric Diester Hydrolases