EC Number   |
General Information |
Reference |
|---|
   3.1.4.54 | malfunction |
anorectic effect of NAPE in NAPE-hydrolysing phospholipase D knockout animals, food intake studies in NAPE-PLD-/- mice, overview |
-, 714338 |
| 3.1.4.54 | malfunction |
generation and characterization of mice with a targeted disruption in the NAPE-PLD gene [NAPE-PLD(-/-) mice]. Brain tissue from NAPE-PLD-(-/-) mice shows more than a 5fold reduction in the calcium-dependent conversion of N-acyl-phosphatidylethanolamines to N-acylethanolamines bearing both saturated and polyunsaturated N-acyl chains. Only the former group of N-acylethanolamines is decreased in level in NAPE-PLD(-/-) brains, and these reductions are most dramatic for N-acylethanolamines bearing very long acyl chains (above C20). Further studies identified a calcium independent phospholipase D activity in brains from NAPE-PLD(-/-) mice that accepts multiple N-acylethanolamine substrates, including the anandamide precursor C20:4 N-acylphosphatidylethanolamine |
707471 |
| 3.1.4.54 | malfunction |
NAPE-PLD -/- mice have greatly reduced brain levels of long-chain saturated N-acylethanolamines but wild-type levels of polyunsaturated N-acylethanolamines (e.g., anandamide), suggesting an important role for NAPE-PLD in the biosynthesis of at least a subset of endogenous NAEs in the mammalian nervous system |
681093 |
| 3.1.4.54 | malfunction |
remarkable accumulation of 1-alkenyl-2-hydroxy-glycero-3-phospho(N-acyl)ethanolamines in the brain of NAPE-PLD-deficient mice |
-, 714339 |
| 3.1.4.54 | malfunction |
the enzyme is involved in the biosynthesis of anandamide, an endocannabinoid that belongs to the class of bioactive, long-chain N-acylethanolamines. Analysis of NAPE-PLD-deficient mice reveals the presence of NAPE-PLD independent pathways for the anandamide formation |
708079 |
| 3.1.4.54 | metabolism |
NAPE-PLD-dependent and -independent, via lysophospholipase D, N-acylphosphatidylethanolamines metabolism in the brain, overview. Brain tissue N-acylethanolamines, including anandamide, can be formed from N-acylated plasmalogen through an NAPE-PLD-independent pathway as well as by their direct release via NAPE-PLD. |
-, 714339 |
| 3.1.4.54 | metabolism |
the enzyme catalyzes a step in the biosynthesis of N-acylethanolamines, the biosynthetic route of N-acylethanolamines seems to involve at least three alternative pathways, overview |
708110 |
| 3.1.4.54 | more |
brain homogenate also form N-palmitoylethanolamine, N-oleoylethanolamine, and anandamide from their corresponding lyso pNAPEs by a Mg2+-dependent lysophospholipase D |
-, 714339 |
| 3.1.4.54 | physiological function |
approximately 60% of cannabinoid-1 receptor-labeled axonal profiles oppose or converge with axon terminals containing N-acylphosphatidylethanolamine-hydrolyzing phospholipase D immunoreactivity. Cannabinoid-1 receptors in the mouse ventral pallidum have subcellular distributions consistent with on demand activation by endocannabinoids that can regulate the release of functionally opposed opioid peptides and also modulate inhibitory and excitatory transmission |
730478 |
| 3.1.4.54 | physiological function |
deletion of NAPE-PLD does not alter the N-acylethanolamine levels of heart, kidney, liver, and jejunum. N-acyl-phosphatidylethanolamine levels except in jejunum are significantly higher in NAPE-PLD-/- mice than in wild-type mice. Glycero-3-phospho-N-acylethanolamine species having an acyl moiety with 22 carbons and 6 double bonds are enriched in these peripheral tissues. 18:2-acyl-containing N-acyl-phosphatidylethanolamine species are predominant over 18:1-containing species in heart, liver, and jejunum |
750992 |
