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Information on EC 3.1.4.54 - N-acetylphosphatidylethanolamine-hydrolysing phospholipase D
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3.1.4.54 N-acetylphosphatidylethanolamine-hydrolysing phospholipase DIUBMB Comments
This enzyme is involved in the biosynthesis of anandamide. It does not hydrolyse phosphatidylcholine and phosphatidylethanolamine . No transphosphatidation . The enzyme contains Zn2+ and is activated by Mg2+ or Ca2+ .
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
napepld, n-acyl phosphatidylethanolamine phospholipase d, n-acyl-phosphatidylethanolamine-specific phospholipase d, n-acylphosphatidylethanolamine-specific phospholipase d, nape-hydrolysing phospholipase d, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAPE-hydrolysing phospholipase D
NAPE-PLD
NAPE-PLD
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-acylphosphatidylethanolamine + H2O = N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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, ,
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SYSTEMATIC NAME
IUBMB Comments
N-acetylphosphatidylethanolamine phosphatidohydrolase
This enzyme is involved in the biosynthesis of anandamide. It does not hydrolyse phosphatidylcholine and phosphatidylethanolamine [1]. No transphosphatidation [1]. The enzyme contains Zn2+ and is activated by Mg2+ or Ca2+ [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dihexadecyl-sn-glycerol-3-phospho-(N-palmitoyl)ethanolamine + H2O
N-palmitoylethanolamine + 1,2-dihexadecyl-sn-glycerol-3-phosphate
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phospho(N-palmitoyl)ethanolamine + H2O
1,2-dioleoyl-sn-glycero-3-phosphate + N-palmitoyl-phosphatidylethanolamine
1-O-octadecenyl-2-oleoyl-sn-glycero-3-phospho(N-palmitoyl)ethanolamine + H2O
1-O-octadecenyl-2-oleoyl-sn-glycerol-3-phosphate + N-palmitoyl-phosphatidylethanolamine
-
-
-
-
?
N-arachidonoyl-1,2-dioleoyl-phosphatidylehanolamine + H2O
N-arachidonoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
hydrolysis rate with 0.1 mM N-arachidonoyl-1,2-dioleoyl-phosphatidylehanolamine is about 50% of that with 0.1 mM N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
-
-
?
N-arachidonoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-arachidonoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-arachidonoyl-1,2-dioleoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-arachidonoyl-1-oleoyl-2-lysophosphatidylethanolamine + H2O
N-arachidonoylethanolamine + 1-oleoyl-2-lyso-sn-glycerol 3-phosphate
-
-
-
?
N-arachidonoyl-phosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
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
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
N-butanoyl-1-palmitoyl-2-linoleoylphosphatidylethanolamine + H2O
N-butanoylethanolamine + 1-palmitoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-decanoyl-1-palmitoyl-2-linoleoylphosphatidylethanolamine + H2O
N-decanoylethanolamine + 1-palmitoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-hexanoyl-1-palmitoyl-2-linoleoylphosphatidylethanolamine + H2O
N-hexanoylethanolamine + 1-palmitoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-lauroyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-lauroylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-myristoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-myristoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-octanoyl-1-palmitoyl-2-linoleoylphosphatidylethanolamine + H2O
N-octanoylethanolamine + 1-palmitoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-oleoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-oleoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-oleoyl-1,2-dioleoylphosphatidylethanolamine + H2O
N-oleoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoyl-1,2-dilauroylphosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1,2-dilauroyl-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
N-palmitoyl-1-palmitoyl-2-linoleoylphosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1-palmitoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoyl-1-palmitoyl-2-lysophosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1-palmitoyl-2-lyso-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoyl-1-palmitoyl-2-oleoylphosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoylphosphatidylethanolamine + H2O
N-palmitoylethanolamine + phosphatidic acid
-
-
-
?
N-stearoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-stearoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-stearoyl-1,2-dioleoylphosphatidylethanolamine + H2O
N-stearoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phospho(N-palmitoyl)ethanolamine + H2O
1,2-dioleoyl-sn-glycero-3-phosphate + N-palmitoyl-phosphatidylethanolamine
-
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phospho(N-palmitoyl)ethanolamine + H2O
1,2-dioleoyl-sn-glycero-3-phosphate + N-palmitoyl-phosphatidylethanolamine
-
-
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
N-acylethanolamines constitute a family of endogenous bioactive lipids that includes arachidonoylethanolamide, i.e. anandamide, palmitoylethanolamide, and oleoylethanolamide. These lipids are formed from their respective N-acylated ethanolamine phospholipid precursor by the action of a phospholipase D enzyme, NAPE-PLD. The bioactive lipids may influence, amongst others: neuroinflammation, food intake, and oocyte implantation
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
the enzyme is involved in formation of N-acylethanolamines, membrane-derived lipids that are utilized as signaling molecules in the nervous system (e.g., the endocannabinoid anandamide)
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
-
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidate
Km values and Vmax values for N-palmitoylphosphatidylethanolamine, N-arachidonoylphosphatidylethanolamine, N-oleoylphosphatidylethanolamine, and N-stearoylphosphatidylethanolamine are similar. The enzyme does not have selectivity for N-acyl groups of N-acylphosphatidylamines
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidate
-
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
-
-
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
-
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
-
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
-
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
-
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide, an endocannabinoid that belongs to the class of bioactive, long-chain N-acylethanolamines
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
-
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide, an endocannabinoid that belongs to the class of bioactive, long-chain N-acylethanolamines
N-arachidonoylethanolamine i.e. anandamide
-
?
N-oleoylphosphatidylethanolamine + H2O
N-oleoylethanolamine + phosphatidate
Km values and Vmax values for N-palmitoylphosphatidylethanolamine, N-arachidonoylphosphatidylethanolamine, N-oleoylphosphatidylethanolamine, and N-stearoylphosphatidylethanolamine are similar. The enzyme does not have selectivity for N-acyl groups of N-acylphosphatidylamines
-
-
?
N-oleoylphosphatidylethanolamine + H2O
N-oleoylethanolamine + phosphatidate
-
-
-
?
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine + H2O
N-palmitoylethanolamine + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
N-palmitoylphosphatidylethanolamine + H2O
N-palmitoylethanolamine + phosphatidate
Km values and Vmax values for N-palmitoyl-phosphatidylethanolamine, N-arachidonoyl-phosphatidylethanolamine, N-oleoyl-phosphatidylethanolamine, and N-stearoyl-phosphatidylethanolamine are similar. The enzyme does not have selectivity for N-acyl groups of N-acylphosphatidylamines
-
-
?
N-palmitoylphosphatidylethanolamine + H2O
N-palmitoylethanolamine + phosphatidate
-
-
-
?
N-stearoylphosphatidylethanolamine + H2O
N-stearoylethanolamine + phosphatidate
Km values and Vmax values for N-palmitoylphosphatidylethanolamine, N-arachidonoylphosphatidylethanolamine, N-oleoylphosphatidylethanolamine, and N-stearoylphosphatidylethanolamine are similar. The enzyme does not have selectivity for N-acyl groups of N-acylphosphatidylamines
-
-
?
N-stearoylphosphatidylethanolamine + H2O
N-stearoylethanolamine + phosphatidate
-
-
-
?
additional information
?
-
-
lacks the ability to catalyze a transphosphatidylation
-
-
?
additional information
?
-
the enzyme hydrolyzes N-acyl-2-lysophosphatidylamines at a much lower rate than N-acyl-phosphatidylethanolamines
-
-
?
additional information
?
-
-
recombinant NAPE-PLD catalyzes direct release of N-palmitoylethanolamine from N-palmitoylethanolamine plasmalogen, the reaction is also catalyzes in the brain in absence of NAPE-PLD, overview
-
-
?
additional information
?
-
-
substrate specificity of the brain enzyme, detailed overview
-
-
?
additional information
?
-
-
recombinant NAPE-PLD catalyzes direct release of N-palmitoylethanolamine from N-palmitoylethanolamine plasmalogen, the reaction is also catalyzes in the brain in absence of NAPE-PLD, overview
-
-
?
additional information
?
-
-
substrate specificity of the brain enzyme, detailed overview
-
-
?
additional information
?
-
lacks the ability to catalyze a transphosphatidylation
-
-
?
additional information
?
-
low activity with N-acetylphosphatidylethanolamine or N-formylphosphatidylethanolamine. The specific activities with N-palmitoyl-lyso-phosphatidylethanolamine and glycerophospho(N-palmitoyl)ethanolamine are 4% and 1%, respectively, of that with N-palmitoylphosphatidylethanolamine. Furthermore, N-palmitoylethanolamine phosphate is totally inactive. N-Palmitoyl-phosphatidylserine, phosphatidylethanol, and phosphatidylbutanol are hydrolyzed at less than 0.4% of the activity as compared with N-palmitoylphosphatidylethanolamine
-
-
?
additional information
?
-
NAPE-PLD is not capable of catalysing a transphosphatidylation reaction
-
-
?
additional information
?
-
the enzyme is inactive with phosphatidylcholine and phosphatidylethanolamine. No transphosphatidation
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-arachidonoyl-phosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
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
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
N-acylethanolamines constitute a family of endogenous bioactive lipids that includes arachidonoylethanolamide, i.e. anandamide, palmitoylethanolamide, and oleoylethanolamide. These lipids are formed from their respective N-acylated ethanolamine phospholipid precursor by the action of a phospholipase D enzyme, NAPE-PLD. The bioactive lipids may influence, amongst others: neuroinflammation, food intake, and oocyte implantation
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
biosynthetic enzyme of anandamide and its related bioactive congeners, the N-acylethanolamines
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
the enzyme is involved in formation of N-acylethanolamines, membrane-derived lipids that are utilized as signaling molecules in the nervous system (e.g., the endocannabinoid anandamide)
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
-
-
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
-
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide, an endocannabinoid that belongs to the class of bioactive, long-chain N-acylethanolamines
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide (N-arachidonoylethanolamine). NAPE-PLD is responsible for the conversion of N-acylphosphatidylethanolamines to N-acylethanolamines in vivo, but other enzyme(s) or pathway(s) are also involved in it, especially in the formation of polyunsaturated N-acylethanolamines, including anandamide. Unlike classical neurotransmitters and neuropeptides, endocannabinoids are not stored in vesicles in the cell, rather they are produced on demand from membrane phospholipids by a series of intracellular enzymes and released from cells, followed by immediate action as signaling molecules. Binding of endocannabinoids as well as cannabinoids to cannabinoid receptors results in the decrease in intracellular cyclic AMP level and the activation of mitogen-activated protein kinase through the coupled Gi/o proteins. The activation of cannabinoid receptors modulates ion channels through Gi/o proteins, leading to the activation of A-type and inwardly rectifying potassium channels and the inhibition of N-type and P/Q-type calcium channels. The endocannabinoid system is involved in a broad range of physiological functions, such as emotion, cardiovascular regulation, energy metabolism, and reproduction, and in a growing number of pathophysiological conditions
N-arachidonoylethanolamine i.e. anandamide
-
?
N-arachidonoylphosphatidylethanolamine + H2O
N-arachidonoylethanolamine + phosphatidic acid
the enzyme is involved in the biosynthesis of anandamide, an endocannabinoid that belongs to the class of bioactive, long-chain N-acylethanolamines
N-arachidonoylethanolamine i.e. anandamide
-
?
additional information
?
-
-
recombinant NAPE-PLD catalyzes direct release of N-palmitoylethanolamine from N-palmitoylethanolamine plasmalogen, the reaction is also catalyzes in the brain in absence of NAPE-PLD, overview
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-
?
additional information
?
-
-
recombinant NAPE-PLD catalyzes direct release of N-palmitoylethanolamine from N-palmitoylethanolamine plasmalogen, the reaction is also catalyzes in the brain in absence of NAPE-PLD, overview
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Mg2+
Mn2+
Ni2+
Sr2+
Zinc
member of the zinc metallohydrolase family of the beta-lactamase fold
Zn2+
Ba2+
stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
Ca2+
activation is observed only in the enzyme preparations after solubilization, EC50: 3 mM. Synergistic activation of the enzyme by spermine and CaCl2 or by spermine and Triton X-100 is not observed
Ca2+
in the presence of 100 mM phospholipid (phosphatidylethanolamine, phosphatidylcholine, or phosphatidylserine), Ca2+ dose-dependently activates NAPE-PLD in varied degrees. Ca2+ at 10 mM stimulates the activity 2.1 fold in the presence of phosphatidylethanolamine. In the presence of phosphatidylcholine or phosphatidylserine, the stimulatory effects of 10 mM Ca2+ (5.2 and 10 fold, respectively) are similar to the effect by 10 mM Ca2+ in the absence of phospholipids (7fold)
Ca2+
stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
Co2+
stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
Mg2+
-
activates, methyl arachidonyl fluorophosphonate inhibits activation by Mg2+ slightly
Mg2+
stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
Mn2+
stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
Ni2+
stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
Sr2+
stimulated up to 30fold by millimolar order of Ca2+. This effect is fully substituted by other divalent cations such as Co2+, Mg2+, Mn2+, Ba2+, Sr2+ and Ni2+
Zn2+
dependent on, NAPE-PLD belongs to the zinc metallohydrolase family of the beta-lactamase fold
Zn2+
presence of of catalytically crucial Zn2+, NAPE-PLD is a member of the metallo-beta-lactamase family
Zn2+
the enzyme belongs to the metallo-beta-lactamase family, presence of catalytically important zinc
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dihexanoyl-glycero-N-(3-(tetradecanoylamino)propyl)phosphoramidate
i.e. AHP-71B, 96.6% inhibition at 1 mM
2,4-dioxo-N-[4-(4-pyridyl)phenyl]-1H-quinazoline-6-sulfonamide
reversible uncompetitive inhibitor, compound binds via a reversible mechanism to the enzyme's zinc center. Compound is not inhibitory to carbonic anhydrase II, neutral endopeptidase and angiotensin-converting enzyme
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
-
compound additionally inhibits human phospholipases Pld1 and Pld2 and Pseudomonas aeruginosa PldA
cetyltrimethylammonium chloride
strongly inhibits the enzyme of all brain regions
N-(2,4-dinitrophenyl)-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
1 mM, 35.6% inhibition
p-chloromercuribenzoic acid
strongly inhibits the enzyme of all brain regions
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dihexanoyl-glycero-3-(hexanoylamino)propylphosphonate
i.e. AHP-57, a phosphonic acid, activates 1.9fold at 1 mM
1,2-dioleoylphosphatidylethanolamine
0.1 mM, increases activity with N-palmitoylphosphatidylamine (0.025 mM) 3.3fold, increases activity with N-arachidonoylphosphatidylamine (0.025 mM), N-oleoylphosphatidylamine (0.025 mM) and N-stearoylphosphatidylamine (0.025 mM), 2.6-2.7fold
15-hydroxy-N-arachidonoylethanolamine
0.005 mM, activation to 145% of the control
deoxycholate
presence of deoxycholate stabilizes the enzyme dimer and increases the catalytic activity with EC50 value of 0.186 mM. Binding is rapid and reversible
methyl-1,2-dihexanoyl-glycero-3-(hexanoylamino)propylphosphonate
i.e. AHP-38, a methylphosphonate, activates 68% at 1 mM
methyl-1,2-dihexanoyl-glycero-3-(tetradecanoylamino)propylphosphonate
i.e. AHP-36, a methylphosphonate, activates 2fold at 1 mM
Triton X-100
maximally active at 0.05%, higher concentrations reduce activity. Synergistic activation of the enzyme by spermine and CaCl2 or by spermine and Triton X-100 is not observed
spermine
activation is observed only in the enzyme preparations after solubilization. EC50: about 0.1 mM. Synergistic activation of the enzyme by spermine and CaCl2 or by spermine and Triton X-100 is not observed
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Atherosclerosis
Palmitoylethanolamide Promotes a Proresolving Macrophage Phenotype and Attenuates Atherosclerotic Plaque Formation.
Colitis
A Palmitoylethanolamide Producing Lactobacillus paracasei Improves Clostridium difficile Toxin A-Induced Colitis.
Endometrial Neoplasms
Expression and Function of the Endocannabinoid Modulating Enzymes Fatty Acid Amide Hydrolase and N-Acylphosphatidylethanolamine-Specific Phospholipase D in Endometrial Carcinoma.
Endometritis
Endocannabinoids as endometrial inflammatory markers in lactating Holstein cows.
Hyperalgesia
Antihyperalgesic Activities of Endocannabinoids in a Mouse Model of Antiretroviral-Induced Neuropathic Pain.
Multiple Sclerosis
Cannabinoid Receptor and N-acyl Phosphatidylethanolamine Phospholipase D - Evidence for Altered Expression in Multiple Sclerosis.
Neoplasms
Altered mRNA Expression of Genes Involved in Endocannabinoid Signalling in Squamous Cell Carcinoma of the Oral Tongue.
Neoplasms
Effects of orthotopic implantation of rat prostate tumour cells upon components of the N-acylethanolamine and monoacylglycerol signalling systems: an mRNA study.
Neoplasms
Perturbations of the endocannabinoid system in mantle cell lymphoma: correlations to clinical and pathological features.
Obesity
A Common Haplotype in NAPEPLD Is Associated With Severe Obesity in a Norwegian Population-Based Cohort (the HUNT Study).
Obesity, Morbid
A Common Haplotype in NAPEPLD Is Associated With Severe Obesity in a Norwegian Population-Based Cohort (the HUNT Study).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0028
N-arachidonoyl-1,2-dioleoylphosphatidylethanolamine
pH 7.5, 37°C
0.004
N-arachidonoyl-1-oleoyl-2-lysophosphatidylethanolamine
pH 7.5, 37°C
0.0033
N-palmitoyl-1-palmitoyl-2-linoleoylphosphatidylethanolamine
pH 7.5, 37°C
0.004
N-palmitoyl-1-palmitoyl-2-lysophosphatidylethanolamine
pH 7.5, 37°C
0.002
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
pH 7.5, 37°C, in presence of 1 mM spermine
0.0029
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme D389N
0.0029
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme DELTAN55
0.0036
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme 387stop
0.0037
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme S152A
0.0042
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme C237S
0.0043
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme C122S
0.0045
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme C288S
0.0046
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, wild-type enzyme
0.0047
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, wild-type enzyme
0.0047
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme C170S
0.0061
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme C255S
0.0142
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme H380R
0.0143
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme C224S
0.0647
N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
37°C, pH 7.4, mutant enzyme L207F
0.0017
N-palmitoylphosphatidylethanolamine
pH 7.4, 37°C, 10 mM CaCl2, 0.1 mM 1,2-dioleoyl-phosphatidylethanolamine
0.0038
N-palmitoylphosphatidylethanolamine
pH 7.4, 37°C, 5 mM EDTA, 0.1 mM 1,2-dipalmitoyl-phosphatidylcholine
0.0069
N-palmitoylphosphatidylethanolamine
pH 7.4, 37°C, 10 mM CaCl2, 0.1 mM 1,2-dioleoyl-phosphatidylserine
0.008
N-palmitoylphosphatidylethanolamine
37°C, pH not specified in the publication, Ca2+ stimulated enzyme
0.0116
N-palmitoylphosphatidylethanolamine
pH 7.4, 37°C, 5 mM EDTA, 0.1 mM 1,2-dioleoyl-phosphatidylethanolamine
0.0122
N-palmitoylphosphatidylethanolamine
pH 7.4, 37°C, 10 mM CaCl2, 0.1 mM 1,2-dipalmitoyl-phosphatidylcholine
0.0122
N-palmitoylphosphatidylethanolamine
pH 7.4, 37°C, 5 mM EDTA, 0.1 mM 1,2-dioleoyl-phosphatidylserine
0.045
N-palmitoylphosphatidylethanolamine
37°C, pH not specified in the publication, Triton X-100 stimulated enzyme
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
1,2-dihexanoyl-glycero-N-(3-(tetradecanoylamino)propyl)phosphoramidate
Homo sapiens
pH 8.0, 37°C
0.067
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
Homo sapiens
-
pH 7.5, 37°C
0.0367
2,4-dioxo-N-[4-(4-pyridyl)phenyl]-1H-quinazoline-6-sulfonamide
Homo sapiens
mutant Q320S, pH not specified in the publication, temperature not specified in the publication
0.0462
2,4-dioxo-N-[4-(4-pyridyl)phenyl]-1H-quinazoline-6-sulfonamide
Homo sapiens
wild-type, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00002
the endogenous NAPE-PLD activity with the homogenates of COS-7 cells transfected with the insert-free vector, pH and temperature not specified in the publication
0.019
hydrolysis of N-palmitoylphosphatidylethanolamine, homogenates of transfected cells, pH and temperature not specified in the publication
0.0979
substrate: N-palmitoyl-1-palmitoyl-2-linoleoyl-phosphatidylethanolamine, pH 7.5, 37°C
2.6
37°C, pH 7.4, substrate: N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine, wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
a substantial proportion of astrocytic and microglial profiles are immunolabeled for both diacylglycerol lipase alpha and NAPE-PLD. NAPE-PLD immunoreactivity on glial profiles at the vicinity of synapses is only occasionally observed. Results suggest that both neurons and glial cells can synthesize and release anandamide in the superficial spinal dorsal horn. Anandamide can predominantly be released from nonsynaptic dendritic and glial compartments
brenda
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ventromedial nucleus. N-arachidonoylphosphatidylethanolamine phospholipase D is localized presynaptically and postsynaptically but shows a preferential distribution in dendrites. The dorsomedial region of the ventromedial nucleus of the hypothalamus displays the necessary machinery for the endocannabinoid-mediated modulation of synaptic transmission of brain circuitries that regulate important hypothalamic functions such as feeding behaviors
brenda
NAPE-PLD is expressed in mouse oviduct on days one to four of pregnancy
brenda
NAPE-PLD is a major player in regulating the dynamic levels of anandamide in the uterus during early pregnancy
brenda
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ventral palladium, approximately 60% of cannabinoid-1 receptor-labeled axonal profiles oppose or converge with axon terminals containing N-acylphosphatidylethanolamine-hydrolyzing phospholipase D immunoreactivity
brenda
additional information
a large degree of colocalization between transient receptor potential vanilloid type 1 and NAPE-PLD or fatty acid amide hydrolase, cycloxygenase-2, 12-lipoxygenase and catechol-O-methyltransferase is found in the hippocampal pyramidal neurons of the CA3 area of the Ammons horn and (with the exception of 12-lipoxyghenase) in some Purkinje cells
brenda
activity detected in almost all of the mouse organs, with higher specific activities in brain, kidney, and testis
brenda
NAPE-PLD is expressed by specific populations of neurons in the brain and targeted to axonal processes. In the dentate gyrus a strong mRNA signal is detected in granule cells. Immunocytochemical analysis reveales intense NAPE-PLD immunoreactivity in the axons of granule cells (mossy fibers) and in axons of the vomeronasal nerve that project to the accessory olfactory bulb. NAPE-PLD expression is detected in hippocampus, cortex, thalamus, hypothalamus, but the intensity of immunostaining is weaker than in mossy fibers
brenda
the enzyme concentrated presynaptically in several types of hippocampal excitatory axon terminals. Localized predominantly on the intracellular membrane cisternae of axonal calcium stores. The highest density of NAPE-PLD is found in mossy terminals of granule cells, which do not express CB1 receptors
brenda
widely distributed with higher specific activities in brain, kidney and testis
brenda
distribution of NAPE-PLD in various brain regions and its age-dependent expression
brenda
widely distributed in various brain regions of rat, with the highest activity in the brain stem. The enzyme activity in rat brain changes during development, and infant rats show a several-fold higher activity than adult rats
brenda
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proliferator-activated receptor PPARalpha is expressed in the calbindin-containing cells of the granular cell-layer of the dentate gyrus and the stratum pyramidale of CA1. These principal PPARalpha+/calbindin+ cells are closely surrounded by N-acyl phosphatidylethanolamine phospholipase D+ fiber varicosities. No pyramidal PPARalpha+/calbindin+ cells are detected in CA3. Most cells containing parvalbumin express both N-acyl phosphatidylethanolamine phospholipase D and PPARalpha in the principal layers of the dentate gyrus and CA1/3. A small number of cells containing PPARalpha and calretinin is found along the hippocampus. Scattered N-acyl phosphatidylethanolamine phospholipase D+/calretinin+ cells are specifically detected in CA3. N-acyl phosphatidylethanolamine phospholipase D+ puncta surround the calretinin+ cells localized in the principal cells of the dentate gyrus and CA1
brenda
activity detected in almost all of the mouse organs, with higher specific activities in brain, kidney, and testis
brenda
widely distributed with higher specific activities in brain, kidney and testis
brenda
-
approximately 60% of cannabinoid-1 receptor-labeled axonal profiles oppose or converge with axon terminals containing N-acylphosphatidylethanolamine-hydrolyzing phospholipase D immunoreactivity
brenda
-
dendritic labeling of N-acylphosphatidylethanolamine-specific phospholipase NAPE-PLD is never observed in association with synaptic contacts. In addition to dendrites, a substantial proportion of astrocytic and microglial profiles are also immunolabeled for both diacylglycerol lipase alpha and NAPE-PLD. NAPE-PLD immunoreactivity on glial profiles at the vicinity of synapses is only occasionally observed. Results suggest that both neurons and glial cells can synthesize and release anandamide in the superficial spinal dorsal horn. Anandamide can predominantly be released from nonsynaptic dendritic and glial compartments
brenda
activity detected in almost all of the mouse organs, with higher specific activities in brain, kidney, and testis
brenda
widely distributed with higher specific activities in brain, kidney and testis
brenda
additional information
neuronal tissue distribution of NAPE-PLD expression analysis, quantitative realtime PCR
brenda
additional information
-
neuronal tissue distribution of NAPE-PLD expression analysis, quantitative realtime PCR
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
associated to membrane. At the membrane interface, the NAPE-PLD dimer forms a hydrophobic nook that contains two molecules of phosphatidylethanolamine, one bound to each monomer
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
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
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
malfunction
-
anorectic effect of NAPE in NAPE-hydrolysing phospholipase D knockout animals, food intake studies in NAPE-PLD-/- mice, overview
malfunction
-
remarkable accumulation of 1-alkenyl-2-hydroxy-glycero-3-phospho(N-acyl)ethanolamines in the brain of NAPE-PLD-deficient mice
malfunction
-
anorectic effect of NAPE in NAPE-hydrolysing phospholipase D knockout animals, food intake studies in NAPE-PLD-/- mice, overview
-
malfunction
-
remarkable accumulation of 1-alkenyl-2-hydroxy-glycero-3-phospho(N-acyl)ethanolamines in the brain of NAPE-PLD-deficient mice
-
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
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.
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.
-
physiological function
NAPE-PLD produces various long and medium chain bioactive N-acylethanolamines, including anandamide in a Ca2+-dependent fashion. Primary sensory neurons, including the capsaicin-sensitive cells are capable of producing anandamide
physiological function
the down-regulation of NAPE-PLD expression may be functionally important because mutant NAPE-PLD-null mice, in which this regulatory process is defective, are unable to mount a normal inflammatory reaction in response to carrageenan
physiological function
the enzyme is involved in formation of N-acylethanolamines, membrane-derived lipids that are utilized as signaling molecules in the nervous system (e.g., the endocannabinoid anandamide). N-acylethanolamines generated by NAPE-PLD in axons may act as anterograde synaptic signaling molecules that regulate the activity of postsynaptic neurons
physiological function
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
physiological function
-
NAPE-PLD is involved in formation of N-acylethanolamines, e.g. include anandamide, N-palmitoylethanolamine,, and N-oleoylethanolamine, from N-acylphosphatidylethanolamines in the brain
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
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
physiological function
feeding of post-weaning male wild-type, NAPE-PLD-/+ and NAPE-PLD -/- mice isocaloric fat diets leads to increased levels in brain docosahexaenoic acid in NAPE-PLD-/+ and NAPE-PLD-/- mice compared to wild-type consuming fish oil. In NAPE-PLD-/- mice, brain docosahexaenoylethanolamide levels are higher after fish oil feeding. Liver and jejunum arachidonoylethanolamide, 1,2-arachidonoylglycerol and docosahexaenoylethanolamide levels reflect their corresponding fatty acid precursors. NAPE-PLD -/- mice have lower oleoylethanolamide levels in the jejunum and a leaner phenotype compared to wild-type mice
physiological function
in brain of NAPE-PLD knockout mice, levels of all 6 N-acyl ethanolamines measured are significantly reduced. 2-Arachidonyl glycerol levels are significantly increased in the brainstem of knockout mice, and levels of arachidonic acid are significantly decreased exclusively in brainstem. N-arachidonoyl glycine levels are significantly increased in 4 brain regions and levels of prostaglandin PGE2 are increased in 6 of 8 brain regions in knockout mice
physiological function
-
NAPE-PLD is involved in formation of N-acylethanolamines, e.g. include anandamide, N-palmitoylethanolamine,, and N-oleoylethanolamine, from N-acylphosphatidylethanolamines in the brain
-
additional information
-
brain homogenate also form N-palmitoylethanolamine, N-oleoylethanolamine, and anandamide from their corresponding lyso pNAPEs by a Mg2+-dependent lysophospholipase D
additional information
-
brain homogenate also form N-palmitoylethanolamine, N-oleoylethanolamine, and anandamide from their corresponding lyso pNAPEs by a Mg2+-dependent lysophospholipase D
-
Show AA Sequence and Transmembrane Helices (726 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is not a subject to posttranslational modification
additional information
the enzyme is not a subject to posttranslational modification
additional information
the enzyme is not a subject to posttranslational modification
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.65 A resolution. NAPE-PLD forms homodimers partly separated by an internal about 9 A wide channel and adapted to associate with phospholipids. A hydrophobic cavity provides an entryway for N-acylphosphatidylethanolamine into the active site, where a binuclear Zn2+ center is involved in hydrolysis. Bile acids bind with high affinity to selective pockets in this cavity, enhancing dimer assembly and enabling catalysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D389N
Vmax is about 87% of wild-type activity, single nucleotide polymorphism mutant
L207F
complete loss of activity, single nucleotide polymorphism mutant of
Q158S/Y159S
mutant is unable to form stable dimers and shows a decreased melting temperature
S152A
Vmax is about 84% of wild-type activity, single nucleotide polymorphism mutant
387stop
Vmax is 20% of wild-type activity, slight decrease in Km-value for N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
C224S
DELTAN55
Vmax is 28% of wild-type activity, slight decrease in Km-value for N-palmitoyl-1,2-dioleoyl-phosphatidylethanolamine
H380R
L207F
additional information
H380R
Vmax is about 4% of wild-type activity, single nucleotide polymorphism mutant
L207F
Vmax is about 1% of wild-type activity, single nucleotide polymorphism mutant
additional information
-
construction of and food intake studies in NAPE-PLD-/- mice, phenotype, overview
additional information
-
construction of and food intake studies in NAPE-PLD-/- mice, phenotype, overview
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1% (w/v) octyl glucoside improves the stability of the purified enzyme
one cycle of freezing and thawing causes loss of the enzyme activity up to 50%
phenylmethylsulfonylfluoride stabilizes at high concentrations (10 mM)
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
HEK-293 and CHO-K1 cell are stably transfected with mouse NAPE-PLD cDNA. Overexpressed NAPE-PLD is capable of forming N-acylethanolamines, including anandamide, in living cells. Overexpression of NAPE-PLD causes a decrease in the total amount of N-acylphosphatidylethanolamines and an increase in the total amount of N-acylethanolamines without showing obvious selectivity for N-acyl species of the endogenous N-acylphosphatidylethanolamines and N-acylethanolamines
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
capsaicin treatment overnight downregulates NAPE-PLD expression in capsaicin-sensitive cells by 70% at 0.01 mM
ethanol downregulates microglial NAPE-PLD expression by activating cAMP/PKA and ERK1/2
Nape-pld is regulated by ovarian steroid hormones via their nuclear receptors
the pro-inflammatory bacterial endotoxin, lipopolysaccharide, decreases palmitoylethanolamide biosynthesis in RAW264.7 macrophages by suppressing the transcription of NAPE-PLD, which catalyzes the production of palmitoylethanolamide and other lipid amides. Liopolysaccharide treatment reduces acetylation of histone proteins bound to the NAPE-PLD promoter, an effect that is blocked by the histone deacetylase inhibitor richostatin A. The transcription factor Sp1 is involved in regulating baseline NAPE-PLD expression, but not in the transcriptional suppression induced by lipopolysaccharide. The down-regulation of NAPE-PLD expression may be functionally important because mutant NAPE-PLD-null mice, in which this regulatory process is defective, are unable to mount a normal inflammatory reaction in response to carrageenan
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
nutrition
medicine
-
the dorsomedial region of the ventromedial nucleus of the hypothalamusdisplays the necessary machinery for the endocannabinoid-mediated modulation of synaptic transmission of brain circuitries that regulate important hypothalamic functions such as feeding behaviors
medicine
effects of acute ethanol exposure to murine BV2 microglial cells. Ethanol downregulates microglial NAPE-PLD expression by activating cAMP/PKA and ERK1/2. Ethanol induces an increase in histone acetyltransferase activity which leads to higher levels of acetylation of histone H3
nutrition
delivering of N-acylphosphatidylethanolamines and N-acylethanolamides intestinally using gut bacteria synthesizing them. Unlike in wild-type mice, increasing intestinal levels of N-acylphosphatidylethanolamines using N-acylphosphatidylethanolamine-synthesizing bacteria in Nape-Pld-/- mice fails to reduce food intake and weight gain or alter gene expression. Increasing intestinal N-acylethanolamide levels in Nape-Pld-/- mice using N-acylethanolamide-synthesizing bacteria induces all of these effects. The N-acylethanolamide-synthesizing bacteria also markedly increase N-acylethanolamide levels and decrease inflammatory gene expression in omental adipose tissue
nutrition
feeding of post-weaning male wild-type, NAPE-PLD-/+ and NAPE-PLD -/- mice isocaloric fat diets leads to increased levels in brain docosahexaenoic acid in NAPE-PLD-/+ and NAPE-PLD-/- mice compared to wild-type consuming fish oil. In NAPE-PLD-/- mice, brain docosahexaenoylethanolamide levels are higher after fish oil feeding. Liver and jejunum arachidonoylethanolamide, 1,2-arachidonoylglycerol and docosahexaenoylethanolamide levels reflect their corresponding fatty acid precursors. NAPE-PLD -/- mice have lower oleoylethanolamide levels in the jejunum and a leaner phenotype compared to wild-type mice
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ueda, N.; Okamoto, Y.; Morishita, J.
N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: a novel enzyme of the beta-lactamase fold family releasing anandamide and other N-acylethanolamines
Life Sci.
77
1750-1758
2005
Rattus norvegicus (Q769K2), Mus musculus (Q8BH82)
brenda
Wang, J.; Okamoto, Y.; Morishita, J.; Tsuboi, K.; Miyatake, A.; Ueda, N.
Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family
J. Biol. Chem.
281
12325-12335
2006
Homo sapiens (Q6IQ20), Rattus norvegicus (Q769K2)
brenda
Egertova, M.; Simon, G.M.; Cravatt, B.F.; Elphick, M.R.
Localization of N-acyl phosphatidylethanolamine phospholipase D (NAPE-PLD) expression in mouse brain: A new perspective on N-acylethanolamines as neural signaling molecules
J. Comp. Neurol.
506
604-615
2008
Mus musculus (Q8BH82), Mus musculus
brenda
Fezza, F.; Gasperi, V.; Mazzei, C.; Maccarrone, M.
Radiochromatographic assay of N-acyl-phosphatidylethanolamine-specific phospholipase D activity
Anal. Biochem.
339
113-120
2005
Mus musculus (Q8BH82), Mus musculus
brenda
Okamoto, Y.; Morishita, J.; Wang, J.; Schmid, P.C.; Krebsbach, R.J.; Schmid, H.H., Ueda, N.
Mammalian cells stably overexpressing N-acylphosphatidylethanolamine-hydrolysing phospholipase D exhibit significantly decreased levels of N-acylphosphatidylethanolamines
Biochem. J.
389
241-247
2005
Mus musculus (Q8BH82)
brenda
Leung, D.; Saghatelian, A.; Simon, G.M.; Cravatt, B.F.
Inactivation of N-acyl phosphatidylethanolamine phospholipase D reveals multiple mechanisms for the biosynthesis of endocannabinoids
Biochemistry
45
4720-4726
2006
Mus musculus (Q8BH82)
brenda
Okamoto, Y.; Wang, J.; Morishita, J.; Ueda, N.
Biosynthetic pathways of the endocannabinoid anandamide
Chem. Biodivers.
4
1842-1857
2007
Homo sapiens (Q6IQ20), Rattus norvegicus (Q769K2), Mus musculus (Q8BH82)
brenda
Liu, Q.; Tonai, T.; Ueda, N.
Activation of N-acylethanolamine-releasing phospholipase D by polyamines
Chem. Phys. Lipids
115
77-84
2002
Rattus norvegicus (Q769K2)
brenda
Petersen, G.; Pedersen, A.H.; Pickering, D.S.; Begtrup, M.; Hansen, H.S.
Effect of synthetic and natural phospholipids on N-acylphosphatidylethanolamine-hydrolyzing phospholipase D activity
Chem. Phys. Lipids
162
53-61
2009
Homo sapiens (Q6IQ20)
brenda
Petersen, G.; Hansen, H.S.
N-Acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate
FEBS Lett.
455
41-44
1999
Rattus norvegicus (Q769K2)
brenda
Wang, J.; Zhao, L.Y.; Uyama, T.; Tsuboi, K.; Wu, X.X., Kakehi, Y.; Ueda, N.
Expression and secretion of N-acylethanolamine-hydrolysing acid amidase in human prostate cancer cells
J. Biochem.
144
685-690
2008
Homo sapiens
brenda
Okamoto, Y.; Morishita, J.; Tsuboi, K.; Tonai, T.; Ueda, N.
Molecular characterization of a phospholipase D generating anandamide and its congeners
J. Biol. Chem.
279
5298-5305
2003
Rattus norvegicus (Q769K2)
brenda
Guo, Y.; Wang, H.; Okamoto, Y.; Ueda, N.; Kingsley, P.J.; Marnett, L.J.; Schmid, H.H.; Das, S.K.; Dey, S.K.
N-Acylphosphatidylethanolamine-hydrolyzing phospholipase D is an important determinant of uterine anandamide levels during implantation
J. Biol. Chem.
280
23429-23432
2005
Mus musculus (Q8BH82)
brenda
Morishita, J.; Okamoto, Y.; Tsuboi, K.; Ueno, M.; Sakamoto, H.; Maekawa, N.; Ueda N.
Regional distribution and age-dependent expression of N-acylphosphatidylethanolamine-hydrolyzing phospholipase D in rat brain
J. Neurochem.
94
753-762
2005
Rattus norvegicus (Q769K2)
brenda
Nyilas, R.; Dudok, B.; Urbn, G.M.; Mackie, K.; Watanabe, M.; Cravatt, B.F.; Freund, T.F.; Katona, I.
Enzymatic machinery for endocannabinoid biosynthesis associated with calcium stores in glutamatergic axon terminals
J. Neurosci.
28
1058-1063
2008
Mus musculus (Q8BH82)
brenda
Zhu, C.; Solorzano, C.; Sahar, S.; Realini, N.; Fung, E.; Sassone-Corsi, P.; Piomelli, D.
Proinflammatory stimuli control NAPE-PLD expression in macrophages
Mol. Pharmacol.
79
786-792
2011
Mus musculus (Q8BH82)
brenda
Wang, J.; Okamoto, Y.; Tsuboi, K.; Ueda, N.
The stimulatory effect of phosphatidylethanolamine on N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD)
Neuropharmacology
54
8-15
2007
Rattus norvegicus (Q769K2)
brenda
Cristino, L.; Starowicz, K.; de Petrocellis, L.; Morishita, J.; Ueda, N.; Guglielmotti, V.; di Marzo, V.
Immunohistochemical localization of anabolic and catabolic enzymes for anandamide and other putative endovanilloids in the hippocampus and cerebellar cortex of the mouse brain
Neuroscience
151
955-968
2008
Mus musculus (Q8BH82), Mus musculus
brenda
Nagy, B.; Fedonidis, C.; Photiou, A.; Wahba, J.; Paule, C.C.; Ma, D.; Buluwela, L.; Nagy, I.
Capsaicin-sensitive primary sensory neurons in the mouse express N-acyl phosphatidylethanolamine phospholipase D
Neuroscience
161
572-577
2009
Mus musculus (Q8BH82), Mus musculus
brenda
Wang, J.; Ueda, N.
Biology of endocannabinoid synthesis system
Prostaglandins Other Lipid Mediat.
89
112-119
2009
Canis lupus familiaris, Homo sapiens (Q6IQ20), Rattus norvegicus (Q769K2), Mus musculus (Q8BH82)
brenda
Wellner, N.; Tsuboi, K.; Madsen, A.N.; Holst, B.; Diep, T.A.; Nakao, M.; Tokumura, A.; Burns, M.P.; Deutsch, D.G.; Ueda, N.; Hansen, H.S.
Studies on the anorectic effect of N-acylphosphatidylethanolamine and phosphatidylethanolamine in mice
Biochim. Biophys. Acta
1811
508-512
2011
Mus musculus, Mus musculus C57BL/6
brenda
Tsuboi, K.; Okamoto, Y.; Ikematsu, N.; Inoue, M.; Shimizu, Y.; Uyama, T.; Wang, J.; Deutsch, D.G.; Burns, M.P.; Ulloa, N.M.; Tokumura, A.; Ueda, N.
Enzymatic formation of N-acylethanolamines from N-acylethanolamine plasmalogen through N-acylphosphatidylethanolamine-hydrolyzing phospholipase D-dependent and -independent pathways
Biochim. Biophys. Acta
1811
565-577
2011
Mus musculus, Mus musculus C57BL/6
brenda
Rivera, P.; Arrabal, S.; Vargas, A.; Blanco, E.; Serrano, A.; Pavon, F.J.; Rodriguez de Fonseca, F.; Suarez, J.
Localization of peroxisome proliferator-activated receptor alpha (PPARalpha) and N-acyl phosphatidylethanolamine phospholipase D (NAPE-PLD) in cells expressing the Ca(2+)-binding proteins calbindin, calretinin, and parvalbumin in the adult rat hippocampus
Front. Neuroanat.
8
12
2014
Rattus norvegicus
brenda
Hegyi, Z.; Hollo, K.; Kis, G.; Mackie, K.; Antal, M.
Differential distribution of diacylglycerol lipase-alpha and N-acylphosphatidylethanolamine-specific phospholipase d immunoreactivity in the superficial spinal dorsal horn of rats
Glia
60
1316-1329
2012
Rattus norvegicus
brenda
Reguero, L.; Puente, N.; Elezgarai, I.; Ramos-Uriarte, A.; Gerrikagoitia, I.; Bueno-Lopez, J.L.; Donate, F.; Grandes, P.
Subcellular localization of NAPE-PLD and DAGL-alpha in the ventromedial nucleus of the hypothalamus by a preembedding immunogold method
Histochem. Cell Biol.
141
543-550
2014
Mus musculus
brenda
Pickel, V.M.; Shobin, E.T.; Lane, D.A.; Mackie, K.
Cannabinoid-1 receptors in the mouse ventral pallidum are targeted to axonal profiles expressing functionally opposed opioid peptides and contacting N-acylphosphatidylethanolamine-hydrolyzing phospholipase D terminals
Neuroscience
227
10-21
2012
Mus musculus
brenda
Scott, S.; Spencer, C.; OReilly, M.; Brown, K.; Lavieri, R.; Cho, C.; Jung, D.; Larock, R.; Brown, H.; Lindsley, C.
Discovery of desketoraloxifene analogues as inhibitors of mammalian, Pseudomonas aeruginosa, and NAPE phospholipase D enzymes
ACS Chem. Biol.
10
421-432
2015
Homo sapiens
brenda
Leishman, E.; Mackie, K.; Luquet, S.; Bradshaw, H.B.
Lipidomics profile of a NAPE-PLD KO mouse provides evidence of a broader role of this enzyme in lipid metabolism in the brain
Biochim. Biophys. Acta
1861
491-500
2016
Mus musculus (Q8BH82)
brenda
Castellani, B.; Diamanti, E.; Pizzirani, D.; Tardia, P.; Maccesi, M.; Realini, N.; Magotti, P.; Garau, G.; Bakkum, T.; Rivara, S.; Mor, M.; Piomelli, D.
Synthesis and characterization of the first inhibitor of N-acylphosphatidylethanolamine phospholipase D (NAPE-PLD)
Chem. Commun. (Camb.)
53
12814-12817
2017
Homo sapiens (Q6IQ20)
brenda
Correa, F.; De Laurentiis, A.; Franchi, A.M.
Ethanol downregulates N-acyl phosphatidylethanolamine-phospholipase D expression in BV2 microglial cells via epigenetic mechanisms
Eur. J. Pharmacol.
786
224-233
2016
Mus musculus (Q8BH82)
brenda
Inoue, M.; Tsuboi, K.; Okamoto, Y.; Hidaka, M.; Uyama, T.; Tsutsumi, T.; Tanaka, T.; Ueda, N.; Tokumura, A.
Peripheral tissue levels and molecular species compositions of N-acyl-phosphatidylethanolamine and its metabolites in mice lacking N-acyl-phosphatidylethanolamine-specific phospholipase D
J. Biochem.
162
449-458
2017
Mus musculus (Q8BH82)
brenda
Chen, Z.; Zhang, Y.; Guo, L.; Dosoky, N.; de Ferra, L.; Peters, S.; Niswender, K.D.; Davies, S.S.
Leptogenic effects of NAPE require activity of NAPE-hydrolyzing phospholipase D
J. Lipid Res.
58
1624-1635
2017
Mus musculus (Q8BH82)
brenda
Lin, L.; Metherel, A.H.; Kitson, A.P.; Alashmali, S.M.; Hopperton, K.E.; Trepanier, M.O.; Jones, P.J.; Bazinet, R.P.
Dietary fatty acids augment tissue levels of n-acylethanolamines in n-acylphosphatidylethanolamine phospholipase D (NAPE-PLD) knockout mice
J. Nutr. Biochem.
62
134-142
2018
Mus musculus (Q8BH82)
brenda
Magotti, P.; Bauer, I.; Igarashi, M.; Babagoli, M.; Marotta, R.; Piomelli, D.; Garau, G.
Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D regulation of fatty acid ethanolamide biosynthesis by bile acids
Structure
23
598-604
2015
Homo sapiens (Q6IQ20)
brenda
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