BRENDA - Enzyme Database
show all sequences of 3.1.4.54

Effect of synthetic and natural phospholipids on N-acylphosphatidylethanolamine-hydrolyzing phospholipase D activity

Petersen, G.; Pedersen, A.H.; Pickering, D.S.; Begtrup, M.; Hansen, H.S.; Chem. Phys. Lipids 162, 53-61 (2009)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
1,2-dihexanoyl-glycero-3-(hexanoylamino)propylphosphonate
i.e. AHP-57, a phosphonic acid, activates 1.9fold at 1 mM
Homo sapiens
cardiolipin
from bovine liver, activates by 68% at 1 mM
Homo sapiens
methyl-1,2-dihexanoyl-glycero-3-(hexanoylamino)propylphosphonate
i.e. AHP-38, a methylphosphonate, activates 68% at 1 mM
Homo sapiens
methyl-1,2-dihexanoyl-glycero-3-(tetradecanoylamino)propylphosphonate
i.e. AHP-36, a methylphosphonate, activates 2fold at 1 mM
Homo sapiens
additional information
activator synthesis, overview
Homo sapiens
phosphatidylbutanol
activates 81% at 1 mM
Homo sapiens
phosphatidylcholine
activates 2.75fold at 1 mM
Homo sapiens
phosphatidylethanolamine
activates; activates 5.91fold at 1 mM
Homo sapiens
phosphatidylinositol
activates 99% at 1 mM
Homo sapiens
Cloned(Commentary)
Commentary
Organism
stable expression of NAPE-PLD in HEK-293 cells
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,2-dihexanoyl-glycero-N-(3-(tetradecanoylamino)propyl)phosphoramidate
i.e. AHP-71B, 96.6% inhibition at 1 mM
Homo sapiens
N-(2,4-dinitrophenyl)-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
1 mM, 35.6% inhibition
Homo sapiens
nitrocefin
-
Homo sapiens
phosphatidylhexanol
-
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
NAPE-PLD is a zinc metallohydrolase
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-acylphosphatidylethanolamine + H2O
Homo sapiens
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-acylethanolamine + phosphatidate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q6IQ20
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihexadecyl-sn-glycerol-3-phospho-(N-palmitoyl)ethanolamine + H2O
-
708110
Homo sapiens
N-palmitoylethanolamine + 1,2-dihexadecyl-sn-glycerol-3-phosphate
-
-
-
?
N-acylphosphatidylethanolamine + H2O
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
708110
Homo sapiens
N-acylethanolamine + phosphatidate
-
-
-
?
N-palmitoyl-1,2-dilauroylphosphatidylethanolamine + H2O
-
708110
Homo sapiens
N-palmitoylethanolamine + 1,2-dilauroyl-sn-glycerol 3-phosphate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.01
-
pH 8.0, 37°C
Homo sapiens
1,2-dihexanoyl-glycero-N-(3-(tetradecanoylamino)propyl)phosphoramidate
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
1,2-dihexanoyl-glycero-3-(hexanoylamino)propylphosphonate
i.e. AHP-57, a phosphonic acid, activates 1.9fold at 1 mM
Homo sapiens
cardiolipin
from bovine liver, activates by 68% at 1 mM
Homo sapiens
methyl-1,2-dihexanoyl-glycero-3-(hexanoylamino)propylphosphonate
i.e. AHP-38, a methylphosphonate, activates 68% at 1 mM
Homo sapiens
methyl-1,2-dihexanoyl-glycero-3-(tetradecanoylamino)propylphosphonate
i.e. AHP-36, a methylphosphonate, activates 2fold at 1 mM
Homo sapiens
additional information
activator synthesis, overview
Homo sapiens
phosphatidylbutanol
activates 81% at 1 mM
Homo sapiens
phosphatidylcholine
activates 2.75fold at 1 mM
Homo sapiens
phosphatidylethanolamine
activates; activates 5.91fold at 1 mM
Homo sapiens
phosphatidylinositol
activates 99% at 1 mM
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
stable expression of NAPE-PLD in HEK-293 cells
Homo sapiens
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.01
-
pH 8.0, 37°C
Homo sapiens
1,2-dihexanoyl-glycero-N-(3-(tetradecanoylamino)propyl)phosphoramidate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,2-dihexanoyl-glycero-N-(3-(tetradecanoylamino)propyl)phosphoramidate
i.e. AHP-71B, 96.6% inhibition at 1 mM
Homo sapiens
N-(2,4-dinitrophenyl)-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
1 mM, 35.6% inhibition
Homo sapiens
nitrocefin
-
Homo sapiens
phosphatidylhexanol
-
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
NAPE-PLD is a zinc metallohydrolase
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-acylphosphatidylethanolamine + H2O
Homo sapiens
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-acylethanolamine + phosphatidate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihexadecyl-sn-glycerol-3-phospho-(N-palmitoyl)ethanolamine + H2O
-
708110
Homo sapiens
N-palmitoylethanolamine + 1,2-dihexadecyl-sn-glycerol-3-phosphate
-
-
-
?
N-acylphosphatidylethanolamine + H2O
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
708110
Homo sapiens
N-acylethanolamine + phosphatidate
-
-
-
?
N-palmitoyl-1,2-dilauroylphosphatidylethanolamine + H2O
-
708110
Homo sapiens
N-palmitoylethanolamine + 1,2-dilauroyl-sn-glycerol 3-phosphate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
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
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
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
Homo sapiens
Other publictions for EC 3.1.4.54
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
751374
Lin
Dietary fatty acids augment t ...
Mus musculus
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134-142
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750295
Castellani
Synthesis and characterizatio ...
Homo sapiens
Chem. Commun. (Camb.)
53
12814-12817
2017
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750992
Inoue
Peripheral tissue levels and ...
Mus musculus
J. Biochem.
162
449-458
2017
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751274
Chen
Leptogenic effects of NAPE re ...
Mus musculus
J. Lipid Res.
58
1624-1635
2017
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749965
Leishman
Lipidomics profile of a NAPE- ...
Mus musculus
Biochim. Biophys. Acta
1861
491-500
2016
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1
1
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750480
Correa
Ethanol downregulates N-acyl ...
Mus musculus
Eur. J. Pharmacol.
786
224-233
2016
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1
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749455
Scott
Discovery of desketoraloxifen ...
Homo sapiens
ACS Chem. Biol.
10
421-432
2015
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752275
Magotti
Structure of human N-acylphos ...
Homo sapiens
Structure
23
598-604
2015
1
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1
1
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729782
Rivera
Localization of peroxisome pro ...
Rattus norvegicus
Front. Neuroanat.
8
12
2014
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729811
Reguero
Subcellular localization of NA ...
Mus musculus
Histochem. Cell Biol.
141
543-550
2014
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729805
Hegyi
Differential distribution of d ...
Rattus norvegicus
Glia
60
1316-1329
2012
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730478
Pickel
Cannabinoid-1 receptors in the ...
Mus musculus
Neuroscience
227
10-21
2012
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710010
Zhu
Proinflammatory stimuli contro ...
Mus musculus
Mol. Pharmacol.
79
786-792
2011
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1
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1
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714338
Wellner
Studies on the anorectic effec ...
Mus musculus, Mus musculus C57BL/6
Biochim. Biophys. Acta
1811
508-512
2011
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1
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142
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1
1
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714339
Tsuboi
Enzymatic formation of N-acyle ...
Mus musculus, Mus musculus C57BL/6
Biochim. Biophys. Acta
1811
565-577
2011
-
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1
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5
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1
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140
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1
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7
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5
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4
4
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708110
Petersen
Effect of synthetic and natura ...
Homo sapiens
Chem. Phys. Lipids
162
53-61
2009
9
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1
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4
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1
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1
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3
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1
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1
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1
9
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1
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4
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1
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1
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3
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1
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1
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1
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710115
Nagy
Capsaicin-sensitive primary se ...
Mus musculus
Neuroscience
161
572-577
2009
-
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2
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2
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6
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