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1,2-diacyl-sn-glycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacyl-sn-glycerol-3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
1,2-dioleoyl-sn-glycerol 3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-dioleoyl-sn-glycerol-3 phosphate
1,2-dioleoyl-sn-glycerol + phosphate
1,2-dipalmitoyl-sn-glycerol 3-phosphate + H2O
1,2-dipalmitoyl-sn-glycerol + phosphate
-
-
-
-
?
1-acyl-sn-glycerol 3-phosphate + H2O
1-acyl-sn-glycerol + phosphate
1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate + H2O
1-stearoyl-2-arachidonoyl-sn-glycerol + phosphate
-
-
-
-
?
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphate + H2O
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycerol + phosphate
5'-AMP + H2O
?
-
8.6% of the activity with phosphatidic acid
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
ATP + H2O
?
-
7.2% of the activity with phosphatidic acid
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
about 10% of the activity with phosphatidic acid
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
ceramide-1-phosphate + H2O
?
-
isoenzyme PAP-2a and PAP-2b
-
-
?
ceramide-1-phosphate + H2O
ceramide + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
?
diacylglycerol diphosphate + H2O
? + phosphate
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
dicaproyl phosphatidate + H2O
1,2-dicaproyl-sn-glycerol + phosphate
-
best substrate of the 104-kDa enzyme form
-
-
?
didecanoyl phosphatidic acid + H2O
1,2-didecanoyl-sn-glycerol + phosphate
dihexanoyl phosphatidic acid + H2O
1,2-dihexanoyl-sn-glycerol + phosphate
dihydro-sphingosine-1-phosphate + H2O
dihydro-sphingosine + phosphate
dimyristoyl phosphatidic acid + H2O
1,2-dimyristoyl-sn-glycerol + phosphate
dioctanoyl phosphatidic acid + H2O
1,2-dioctanoyl-sn-glycerol + phosphate
dioleoyl phosphatidate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
-
?
dioleoyl phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
dipalmitoyl phosphatidate + H2O
1,2-dipalmitoyl-sn-glycerol + phosphate
-
-
-
-
?
dipalmitoyl phosphatidic acid + H2O
?
-
-
-
-
?
distearoyl phosphatidic acid + H2O
1,2-distearoyl-sn-glycerol + phosphate
-
-
-
-
?
DL-alpha-glycerophosphate + H2O
glycerol + phosphate
-
about 10% of the activity with phosphatidic acid
-
-
?
FTY720-phosphate + H2O
FTY720 + phosphate
Glucose 6-phosphate + H2O
Glucose + phosphate
glycerophosphate + H2O
glycerol + phosphate
-
-
-
-
?
lyso-phosphatidate + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
lysophosphatidate + H2O
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
lysophosphatidic acid + H2O
?
lysophosphatidic acid + H2O
? + phosphate
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
octanoyl lysophosphatidic acid + H2O
?
-
-
-
-
?
oleoyl phosphatidic acid + H2O
?
-
-
-
-
?
p-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
about 10% of the activity with phosphatidic acid
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
phosphatidate + H2O
diacylglycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
phosphatidic acid + H2O
?
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
phosphatidic acid + H2O
phosphate + diacylglycerol
-
-
-
?
sphingosine 1-phosphate + H2O
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
sphingosine-1-phosphate + H2O
sphingosine + phosphate
additional information
?
-
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
ir
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
1,2-dioleoyl-sn-glycerol-3 phosphate
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-dioleoyl-sn-glycerol-3 phosphate
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
?
1,2-dioleoyl-sn-glycerol-3 phosphate
1,2-dioleoyl-sn-glycerol + phosphate
insulin and epinephrine control lipin 1 primarily by changing localization rather than intrinsic PAP activity, overview
-
-
?
1-acyl-sn-glycerol 3-phosphate + H2O
1-acyl-sn-glycerol + phosphate
-
at 9.1% of the activity with phosphatidic acid
-
-
?
1-acyl-sn-glycerol 3-phosphate + H2O
1-acyl-sn-glycerol + phosphate
-
less than 15% of the activity with phosphatidic acid
-
-
?
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphate + H2O
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycerol + phosphate
-
fluorescent substrate deirvative
-
-
?
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphate + H2O
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycerol + phosphate
-
fluorescent substrate deirvative
-
-
?
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphate + H2O
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycerol + phosphate
-
fluorescent substrate derivative
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
dephosphorylation of these lipids terminates their signaling actions and generates products with additional biological activities or metabolic fates, overview
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Lipin-1 influences lipid homeostasis and plays a critical role in adipocyte development with lipin-1A and lipin-1B having distinct purposes in the process, overview. Phosphorylation plays an important role in modulation of enzyme activity, overview
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in the regulation of lipid synthesis, PAP generates a pool of diacylglycerol used for protein kinase C activation, and attenuates the signaling functions of phosphatidic acid
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
lipin-1 is negatively regulated by phosphorylation during mitosis
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
phosphatidate phosphatases are key enzymes in lipid biosynthesis and signaling. Type I PAP enzymes participate in de-novo phospholipid biosynthesis, whereas type II PAP enzymes have an established role in lipid signaling. The eukaryotic, endoplasmic reticulum-resident PA-PSP is a bifunctional enzyme with specific type II PAP activity, and regulates, in addition to type I PAPs, the de-novo biosynthesis of phospholipids and triacylglycerols
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
the presqualene diphosphate phosphatase is a potent Mg2+-independent, NEM-insensitive type II PAP
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Lipin-1 influences lipid homeostasis and plays a critical role in adipocyte development with lipin-1A and lipin-1B having distinct purposes in the process, overview. Phosphorylation plays an important role in modulation of enzyme activity, overview
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in the regulation of lipid synthesis, it PAP generates a pool of diacylglycerol used for protein kinase C activation, and attenuates the signaling functions of phosphatidic acid
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
lipin 1 is a bifunctional intracellular protein that regulates fatty acid metabolism in the nucleus via interactions with DNA-bound transcription factors and at the endoplasmic reticulum as a phosphatidic acid phosphohydrolase enzyme to catalyze the penultimate step in triglyceride synthesis. Lipin 2 plays an important role as a hepatic PAP-1 enzyme
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
lipin-1 plays a critical role in the perturbation of hepatic insulin signaling
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
lipin-2 is negatively regulated by phosphorylation during mitosis
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Lipin-1 influences lipid homeostasis and plays a critical role in adipocyte development with lipin-1A and lipin-1B having distinct purposes in the process, overview. Phosphorylation plays an important role in modulation of enzyme activity, overview
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Pah1p regulates nuclear membrane growth during cell cycle. Phosphorylation plays an important role in modulation of enzyme activity, overview
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in the regulation of lipid synthesis, it PAP generates a pool of diacylglycerol used for protein kinase C activation, and attenuates the signaling functions of phosphatidic acid
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
the enzyme is involved in lipid synthesis and cell signalling
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
LPP1 but not LPR1
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
?
preferred substrate of isozyme DPPL1
-
-
?
diacylglycerol diphosphate + H2O
?
preferred substrate of isozyme DPPL2
-
-
?
diacylglycerol diphosphate + H2O
?
-
-
-
?
diacylglycerol diphosphate + H2O
? + phosphate
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
? + phosphate
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional LPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it removes the phosphate from phosphatidate to form diacylglycerol
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol
-
-
?
didecanoyl phosphatidic acid + H2O
1,2-didecanoyl-sn-glycerol + phosphate
-
-
-
-
?
didecanoyl phosphatidic acid + H2O
1,2-didecanoyl-sn-glycerol + phosphate
-
-
-
-
?
dihexanoyl phosphatidic acid + H2O
1,2-dihexanoyl-sn-glycerol + phosphate
-
-
-
-
?
dihexanoyl phosphatidic acid + H2O
1,2-dihexanoyl-sn-glycerol + phosphate
-
-
-
-
?
dihydro-sphingosine-1-phosphate + H2O
dihydro-sphingosine + phosphate
-
all LPPs
-
-
?
dihydro-sphingosine-1-phosphate + H2O
dihydro-sphingosine + phosphate
-
all LPPs
-
-
?
dimyristoyl phosphatidic acid + H2O
1,2-dimyristoyl-sn-glycerol + phosphate
-
-
-
-
?
dimyristoyl phosphatidic acid + H2O
1,2-dimyristoyl-sn-glycerol + phosphate
-
-
-
-
?
dioctanoyl phosphatidic acid + H2O
1,2-dioctanoyl-sn-glycerol + phosphate
-
-
-
-
?
dioctanoyl phosphatidic acid + H2O
1,2-dioctanoyl-sn-glycerol + phosphate
-
PAP1 activity is linear with respect to the substrate at concentrations between 0.05-0.8 mM
-
-
?
dioleoyl phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
-
?
dioleoyl phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
-
?
FTY720-phosphate + H2O
FTY720 + phosphate
-
LPP3
-
-
?
FTY720-phosphate + H2O
FTY720 + phosphate
-
LPP3
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
at 5.2% of the activity with phosphatidic acid
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
about 10% of the activity with phosphatidic acid
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
-
all LPPs
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
LPP1 but not LPR1
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
-
all LPPs
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidate + H2O
?
-
-
-
-
?
lysophosphatidate + H2O
?
-
isoenzyme PAP-2a and PAP-2b
-
-
?
lysophosphatidate + H2O
?
-
-
-
-
?
lysophosphatidate + H2O
?
-
poor substrate
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidic acid + H2O
?
-
-
-
?
lysophosphatidic acid + H2O
?
-
-
-
?
lysophosphatidic acid + H2O
?
-
-
-
-
?
lysophosphatidic acid + H2O
? + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
? + phosphate
-
-
-
?
lysophosphatidic acid + H2O
? + phosphate
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
biochemical regulation of PA phosphatases involving phospholipids, nucleotides ATP and CTP and the cAMP-dependent protein kinase A, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction, overview, PA phosphatase activity is regulated by biochemical and genetic mechanisms in a reciprocal manner with the regulation of the phospholipid biosynthetic enzyme phosphatidylserin synthase, overview
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
preferred substrate, the bifunctional LPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it removes the phosphate from phosphatidate to form diacylglycerol
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
preferred substrate
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
both PAH1 and PAH2 have two domains, the amino-terminal lipin and carboxy-terminal lipin domains. PAH1 and PAH2 may supply diacylglycerol as a substrate of galactolipid synthesis, and phosphatidic acid hydrolyzed by PAH1 and PAH2 may be derived from phosphatidylcholine and phosphatidylethanolamine
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
diacylglycerol is the necessary precursor for the synthesis of triacylglycerols, phosphatidylcholine and phosphatidylethanolamine
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
lipin-1, lipin-2, and lipin-3
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
diacylglycerol is the necessary precursor for the synthesis of triacylglycerols, phosphatidylcholine and phosphatidylethanolamine
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
134859, 134860, 134861, 134863, 134865, 134867, 134868, 134871, 134873, 134874, 134876, 134877 -
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
membrane-bound phosphatidic acid and aqueously dispersed phosphatidic acid
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
phosphatidate bound to microsomal membrane, phosphatidate in sonicated dispersion of organic solvent-disrupted microsomes or phosphatidate dispersed in sonicated microsomal lipid
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
phosphatidic acid pure or in mixed micelles with phosphatidylcholine
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
diacylglycerol is the necessary precursor for the synthesis of triacylglycerols, phosphatidylcholine and phosphatidylethanolamine
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
ir
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
highly specific for
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
Pah1p also uses phosphatidic acid to produce phosphatidylethanolamine and phosphatidylcholine through a second parallel route, the cytidine diphosphate diacylglycerol pathway
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
r
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
r
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
lipid phosphate phosphatase-1 regulates lysophosphatidate-induced fibroblast migration by controlling phospholipase D2-dependent phosphatidate generation, LPP1 expression decreases PLD activity and PA accumulation after stimulating fibroblasts with either LPA or PDGF, but PLD-dependent PA formation Is only required for LPA-induced fibroblast migration, overview
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
lipid phosphate phosphatase enzymes may play a role in signal transduction by terminating signaling events of lipid phosphates
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate, isozyme PAP1 plays a role in the transcriptional regulation of phospholipid synthesis, overview
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
the conserved arginine residue in domain 1 and the conserved histidine residues in domains 2 and 3 are essential for catalytic activity
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
the plastidic phosphatidic acid phosphatase dephosphorylates phosphatidic acid to yield diacylglycerol, which is a precursor for galactolipids, a primary and indispensable component of photosynthetic membranes
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
preferred substrate
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
preferred substrate
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
LPP1 but not LPR1
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
?
-
hydrolysis by isoenzyme PAP-2b, no hydrolysis by isoenzyme PAP-2a
-
-
?
sphingosine 1-phosphate + H2O
?
-
poor substrate
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
all LPPs
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
LPP1 but not LPR1
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
all LPPs
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
-
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
-
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
-
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
-
-
?
additional information
?
-
-
the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
-
-
?
additional information
?
-
-
the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
-
-
?
additional information
?
-
-
competition between phosphatidic acid, lysophosphatidic acid by the active site of LPPs is modulated by rod outer segment illumination state and by rod outer segment protein association/dissociation, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, Wunen and Wunen2 are essential for germ cell development, overview
-
-
?
additional information
?
-
-
the enzyme dephosphorylates bioactive lipid messengers, modifying or attenuating their activities, it plays a pivotal role in primordial germ cell migration and survival during embryogenesis
-
-
?
additional information
?
-
-
the enzyme is involved in phototransduction, the enzyme acts synergistically with the diacylglycerol kinase, encoded by gene rdgA, both regulating response termination during phototransduction, regulation of phototransduction and phosphatidyl inositol 4,5-bisphosphate lipid signaling cascade, overview
-
-
?
additional information
?
-
-
Wunen and Wunen2 are involved in regulation of bioactive lipids and in survival and migration of germ cells, physiological roles of LPP isozymes
-
-
?
additional information
?
-
-
Wunen does not interact with its counterpart Wunen-2
-
-
?
additional information
?
-
-
Wunen does not interact with Wunen2
-
-
?
additional information
?
-
-
mutations in laza causes a reduction in the light response and faster termination kinetics, loss of laza suppressed the severity of the phenotype caused by mutation of the diacylglycerol kinase, RDGA, retinal degeneration resulting from overexpression of the phospholipase D is suppressed by elimination of Laza, the flies have a requirement for a PLD/PAP-dependent pathway for achieving the maximal light response, since the Drosophila phototransduction cascade serves as a paradigm for characterizing the regulation of sensory signaling and TRP channels in vivo
-
-
?
additional information
?
-
-
both long and short chain lysophosphatidic acids are hydrolyzed at rates comparable with that observed for short chain phosphatidic acids
-
-
?
additional information
?
-
-
negligible activity towards long-chain phosphatidic acid
-
?
additional information
?
-
-
activation of cytosolic phospholipase A 2 and attendant arachidonic acid release by phorbol esters in WISH cells requires prior generation of diacylglycerol by phosphatidate phosphohydrolase
-
-
?
additional information
?
-
-
the enzyme from plasma membrane increases in liver fibrosis but not regeneration. Stimulation of phosphatidate phosphohydrolase with its effect on the diacylglycerol/phosphatidate ratio may play a role in transduction of the fibrosis signal
-
-
?
additional information
?
-
-
critical roles of the enzyme in cell growth and differentiation
-
-
?
additional information
?
-
-
the enzyme may play an important role in regulating inflammatory cell responses to extracellular phosphatidic acid in biological system
-
-
?
additional information
?
-
-
role of PAP-1 as a key enzyme for cell integrity and survival
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids, physiological roles of LPP isozymes
-
-
?
additional information
?
-
-
regulation of cell survival by lipid phosphate phosphatases involves the modulation of intracellular phosphatidic acid and sphingosine 1-phosphate pools, the enzyme reduces the stimulation of the p42/p44 MAPK signalling pathway by sphingosine 1-phosphate and lysophosphatidic acid
-
-
?
additional information
?
-
-
substrate specificities of isozymes
-
-
?
additional information
?
-
-
the enzyme is homologous to murine lipid phosphate phosphatase isozyme LPP-1
-
-
?
additional information
?
-
-
expression of phosphatidic acid phosphatase 2a, which hydrolyzes lipids to generate diacylglycerol, is regulated by p73, a member of the p53 family, overview
-
-
?
additional information
?
-
-
increasing LPP2 activity causes premature cyclin A expression and decreased LPP2 expression delays cyclin A expression, overview
-
-
?
additional information
?
-
-
phosphatidic acid phosphohydrolase, PAP, catalyzes the dephosphorylation of phosphatidic acid to diacylglycerol, the second messenger responsible for activation of protein kinase C
-
-
?
additional information
?
-
-
phosphatidic acid phosphohydrolase-1 is required for lipopolysaccharide-induced cyclooxygenase-2 expression in human U937 macrophages or P388D1 cells, inhibition of PAP-1 results in a decrease in LPS-induced COX-2 mRNA transcript production, COX-2 protein expression, and prostaglandin E2 release, regulation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the activation of 5-lipoxygenase in polymorphonuclear leukocytes together with phospholipase D via diacylglyceride generation, PLD/PA-P pathway, overview
-
-
?
additional information
?
-
LPR1 does not hydrolyze phospholipid substrates under conditions that readily support LPP1 activity
-
-
?
additional information
?
-
-
lipin-1 operates as a transcriptional coactivator in the nucleus together with nuclear receptors and coactivators to modulate gene expression in lipid metabolism. Lipin-1 levels are reduced in adipocytes from obesive persons. Lipin-2 mutations are involved in human diseases such as cutaneous inflammation, osteomyelitis and dyserythropoietic anemia, muations of lipin-1 cause recurrent acute myoglobinuria
-
-
?
additional information
?
-
-
the catalytic site is arranged into three distinct domains: one substrate recognition site and two catalytic sites
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, LPP-1 regulates lysophosphatidic acid- and platelet-derived-growth-factor-induced cell migration via the p42/p44 MAPK pathway, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids, physiological roles of LPP isozymes
-
-
?
additional information
?
-
-
the enzyme regulates the level of phosphorylated lipids acting as growth factors or second messengers, the enzyme is involved in lipid signaling pathways
-
-
?
additional information
?
-
-
substrate specificities of isozymes
-
-
?
additional information
?
-
-
lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
-
-
?
additional information
?
-
-
the enzyme is regulated by estrogens in the liver and the uterus, E2 downregulates the enzyme in the uterus via the estrogen receptor in a primary response, overview
-
-
?
additional information
?
-
-
hyperactivation of TORC2 exacerbates insulin resistance by enhancing expression of LIPIN1, a mammalian phosphatidic acid phosphatase for diacylglycerol synthesis, overview
-
-
?
additional information
?
-
-
lipin 2 is dynamically regulated in liver but is not a target gene of PGC-1alpha
-
-
?
additional information
?
-
-
lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators, e.g. PPARgamma coactivator 1alpha, i.e. PGC-1alpha, to modulate gene expression in lipid metabolism
-
-
?
additional information
?
-
-
phosphatidic acid phosphohydrolase 1 and protein kinase C are required for Toll-like receptor-4-mediated group IVA phospholipase A2 activation, regulation, overview
-
-
?
additional information
?
-
-
endogenous LPP2 and LPP3 form a complex
-
-
?
additional information
?
-
recombinant PAP2L2 shows a broad substrate specificity
-
-
?
additional information
?
-
-
recombinant PAP2L2 shows a broad substrate specificity
-
-
?
additional information
?
-
recombinant PAP2L2 shows a broad substrate specificity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in de novo synthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine
-
-
?
additional information
?
-
-
the Mg2+-dependent enzyme of rat lung is involved in pulmonary glycerolipid biosynthesis
-
-
?
additional information
?
-
-
the activity associated with the cytosol has a role in phosphocholine biosynthesis in rat lung
-
-
?
additional information
?
-
-
the enzyme catalyzes the final steps in the reesterification of fatty acids to triacylglycerols
-
-
?
additional information
?
-
-
key enzyme involved in glycerolipid synthesis where it converts phosphatidic acid to diacylglycerol. PAP-1 is involved in phospholipid biosynthesis
-
?
additional information
?
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rate-limiting enzyme for triglyceride synthesis, short-term administration of conjugated linoleic acid reduces activity 20%
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?
additional information
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LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
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?
additional information
?
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LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
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?
additional information
?
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LPP is involved in regulation of bioactive lipids, physiological roles of LPP isozymes
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?
additional information
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the enzyme activity is involved in generation of phosphatidic acid and diaclyglycerol implicated in signal transduction, and in aging, overview
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additional information
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substrate specificities of isozymes
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additional information
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phosphatidic acid phosphohydrolase, PAP, catalyzes the dephosphorylation of phosphatidic acid to diacylglycerol, the second messenger responsible for activation of protein kinase C
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additional information
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expression of lipin-1 cells stimulates glycerolipid synthesis and secretion in McA-RH7777, overview
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additional information
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lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators, e.g. PPARgamma coactivator 1alpha, i.e. PGC-1alpha, to modulate gene expression in lipid metabolism
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additional information
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the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
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additional information
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the 45000 Da enzyme form and 104000 Da enzyme form are induced when cells enter the stationary phase of growth
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additional information
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the enzyme plays an important role in regulating lipid synthesis in Saccharomyces cerevisiae, the enzyme is also involved in cell signaling mechanisms as part of the phospholipase D-phosphatidate phosphatase pathway
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?
additional information
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the enzyme is homologous to mammalian lipin
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additional information
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lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
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?
additional information
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the enzyme plays a major role in the synthesis of triacylglycerols and phospholipids in Saccharomyces cerevisiae, the PAH1 gene product is essential for its roles in lipid metabolism and cell physiology, role of PAH1-encoded PAP1 in lipid synthesis, pathway, overview
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additional information
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lipin contains the DXDX(T/V) active site motif
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?
additional information
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PAH1-encoded Mg2+-dependent PAP1 catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol and phosphate, PAP1 contains the catalytic motif DIDGT at residues 398402 and a conserved Gly80 residue
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?
additional information
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the enzyme also shows diacylglycerol lipase activity, EC 3.1.1.34, overview
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additional information
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the LPP1-encoded enzyme has broad substrate specificity
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additional information
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lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators to modulate gene expression in lipid metabolism
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additional information
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PAP1 activity is conferred by the DxDxT motif of the C-Lip domain contained in all lipin family members
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additional information
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the diacylglycerol formed by the enzyme is used as a substrate for galactolipid synthesis on the inner envelope membrane
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additional information
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the functional role of the enzyme in lamellar bodies is proposed in relation to glycerophospholipd metabolism
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
1,2-dioleoyl-sn-glycerol-3 phosphate
1,2-dioleoyl-sn-glycerol + phosphate
insulin and epinephrine control lipin 1 primarily by changing localization rather than intrinsic PAP activity, overview
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
phosphatidic acid + H2O
diacylglycerol + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
sphingosine-1-phosphate + H2O
sphingosine + phosphate
additional information
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-
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
ir
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
dephosphorylation of these lipids terminates their signaling actions and generates products with additional biological activities or metabolic fates, overview
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-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Lipin-1 influences lipid homeostasis and plays a critical role in adipocyte development with lipin-1A and lipin-1B having distinct purposes in the process, overview. Phosphorylation plays an important role in modulation of enzyme activity, overview
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-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in the regulation of lipid synthesis, PAP generates a pool of diacylglycerol used for protein kinase C activation, and attenuates the signaling functions of phosphatidic acid
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-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
lipin-1 is negatively regulated by phosphorylation during mitosis
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
phosphatidate phosphatases are key enzymes in lipid biosynthesis and signaling. Type I PAP enzymes participate in de-novo phospholipid biosynthesis, whereas type II PAP enzymes have an established role in lipid signaling. The eukaryotic, endoplasmic reticulum-resident PA-PSP is a bifunctional enzyme with specific type II PAP activity, and regulates, in addition to type I PAPs, the de-novo biosynthesis of phospholipids and triacylglycerols
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Lipin-1 influences lipid homeostasis and plays a critical role in adipocyte development with lipin-1A and lipin-1B having distinct purposes in the process, overview. Phosphorylation plays an important role in modulation of enzyme activity, overview
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in the regulation of lipid synthesis, it PAP generates a pool of diacylglycerol used for protein kinase C activation, and attenuates the signaling functions of phosphatidic acid
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
lipin 1 is a bifunctional intracellular protein that regulates fatty acid metabolism in the nucleus via interactions with DNA-bound transcription factors and at the endoplasmic reticulum as a phosphatidic acid phosphohydrolase enzyme to catalyze the penultimate step in triglyceride synthesis. Lipin 2 plays an important role as a hepatic PAP-1 enzyme
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
lipin-1 plays a critical role in the perturbation of hepatic insulin signaling
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
lipin-2 is negatively regulated by phosphorylation during mitosis
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Lipin-1 influences lipid homeostasis and plays a critical role in adipocyte development with lipin-1A and lipin-1B having distinct purposes in the process, overview. Phosphorylation plays an important role in modulation of enzyme activity, overview
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in glycerolipid synthesis, diacylglycerol is direct precursor of triacylglycerol, phosphoatidylcholine, and phosphatidylethanolamine. Pah1p regulates nuclear membrane growth during cell cycle. Phosphorylation plays an important role in modulation of enzyme activity, overview
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?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
key enzyme in the regulation of lipid synthesis, it PAP generates a pool of diacylglycerol used for protein kinase C activation, and attenuates the signaling functions of phosphatidic acid
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-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
-
the enzyme is involved in lipid synthesis and cell signalling
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-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
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?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
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?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
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-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
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?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
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?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
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-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
-
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
biochemical regulation of PA phosphatases involving phospholipids, nucleotides ATP and CTP and the cAMP-dependent protein kinase A, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction, overview, PA phosphatase activity is regulated by biochemical and genetic mechanisms in a reciprocal manner with the regulation of the phospholipid biosynthetic enzyme phosphatidylserin synthase, overview
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-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
preferred substrate
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-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
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-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it then removes the phosphate from phosphatidate to form diacylglycerol, zinc-mediated regulation, overview
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-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
-
ir
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
lipid phosphate phosphatase-1 regulates lysophosphatidate-induced fibroblast migration by controlling phospholipase D2-dependent phosphatidate generation, LPP1 expression decreases PLD activity and PA accumulation after stimulating fibroblasts with either LPA or PDGF, but PLD-dependent PA formation Is only required for LPA-induced fibroblast migration, overview
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-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
lipid phosphate phosphatase enzymes may play a role in signal transduction by terminating signaling events of lipid phosphates
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?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
-
PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate, isozyme PAP1 plays a role in the transcriptional regulation of phospholipid synthesis, overview
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?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
-
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-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
the plastidic phosphatidic acid phosphatase dephosphorylates phosphatidic acid to yield diacylglycerol, which is a precursor for galactolipids, a primary and indispensable component of photosynthetic membranes
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-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
-
-
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
-
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
-
-
?
sphingosine-1-phosphate + H2O
sphingosine + phosphate
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
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?
additional information
?
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the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
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?
additional information
?
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the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
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?
additional information
?
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LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, Wunen and Wunen2 are essential for germ cell development, overview
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?
additional information
?
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the enzyme dephosphorylates bioactive lipid messengers, modifying or attenuating their activities, it plays a pivotal role in primordial germ cell migration and survival during embryogenesis
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?
additional information
?
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the enzyme is involved in phototransduction, the enzyme acts synergistically with the diacylglycerol kinase, encoded by gene rdgA, both regulating response termination during phototransduction, regulation of phototransduction and phosphatidyl inositol 4,5-bisphosphate lipid signaling cascade, overview
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?
additional information
?
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Wunen and Wunen2 are involved in regulation of bioactive lipids and in survival and migration of germ cells, physiological roles of LPP isozymes
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-
?
additional information
?
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mutations in laza causes a reduction in the light response and faster termination kinetics, loss of laza suppressed the severity of the phenotype caused by mutation of the diacylglycerol kinase, RDGA, retinal degeneration resulting from overexpression of the phospholipase D is suppressed by elimination of Laza, the flies have a requirement for a PLD/PAP-dependent pathway for achieving the maximal light response, since the Drosophila phototransduction cascade serves as a paradigm for characterizing the regulation of sensory signaling and TRP channels in vivo
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?
additional information
?
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activation of cytosolic phospholipase A 2 and attendant arachidonic acid release by phorbol esters in WISH cells requires prior generation of diacylglycerol by phosphatidate phosphohydrolase
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?
additional information
?
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the enzyme from plasma membrane increases in liver fibrosis but not regeneration. Stimulation of phosphatidate phosphohydrolase with its effect on the diacylglycerol/phosphatidate ratio may play a role in transduction of the fibrosis signal
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?
additional information
?
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critical roles of the enzyme in cell growth and differentiation
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?
additional information
?
-
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the enzyme may play an important role in regulating inflammatory cell responses to extracellular phosphatidic acid in biological system
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?
additional information
?
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role of PAP-1 as a key enzyme for cell integrity and survival
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?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids, physiological roles of LPP isozymes
-
-
?
additional information
?
-
-
regulation of cell survival by lipid phosphate phosphatases involves the modulation of intracellular phosphatidic acid and sphingosine 1-phosphate pools, the enzyme reduces the stimulation of the p42/p44 MAPK signalling pathway by sphingosine 1-phosphate and lysophosphatidic acid
-
-
?
additional information
?
-
-
expression of phosphatidic acid phosphatase 2a, which hydrolyzes lipids to generate diacylglycerol, is regulated by p73, a member of the p53 family, overview
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-
?
additional information
?
-
-
increasing LPP2 activity causes premature cyclin A expression and decreased LPP2 expression delays cyclin A expression, overview
-
-
?
additional information
?
-
-
phosphatidic acid phosphohydrolase, PAP, catalyzes the dephosphorylation of phosphatidic acid to diacylglycerol, the second messenger responsible for activation of protein kinase C
-
-
?
additional information
?
-
-
phosphatidic acid phosphohydrolase-1 is required for lipopolysaccharide-induced cyclooxygenase-2 expression in human U937 macrophages or P388D1 cells, inhibition of PAP-1 results in a decrease in LPS-induced COX-2 mRNA transcript production, COX-2 protein expression, and prostaglandin E2 release, regulation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the activation of 5-lipoxygenase in polymorphonuclear leukocytes together with phospholipase D via diacylglyceride generation, PLD/PA-P pathway, overview
-
-
?
additional information
?
-
-
lipin-1 operates as a transcriptional coactivator in the nucleus together with nuclear receptors and coactivators to modulate gene expression in lipid metabolism. Lipin-1 levels are reduced in adipocytes from obesive persons. Lipin-2 mutations are involved in human diseases such as cutaneous inflammation, osteomyelitis and dyserythropoietic anemia, muations of lipin-1 cause recurrent acute myoglobinuria
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, LPP-1 regulates lysophosphatidic acid- and platelet-derived-growth-factor-induced cell migration via the p42/p44 MAPK pathway, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids, physiological roles of LPP isozymes
-
-
?
additional information
?
-
-
the enzyme regulates the level of phosphorylated lipids acting as growth factors or second messengers, the enzyme is involved in lipid signaling pathways
-
-
?
additional information
?
-
-
lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
-
-
?
additional information
?
-
-
the enzyme is regulated by estrogens in the liver and the uterus, E2 downregulates the enzyme in the uterus via the estrogen receptor in a primary response, overview
-
-
?
additional information
?
-
-
hyperactivation of TORC2 exacerbates insulin resistance by enhancing expression of LIPIN1, a mammalian phosphatidic acid phosphatase for diacylglycerol synthesis, overview
-
-
?
additional information
?
-
-
lipin 2 is dynamically regulated in liver but is not a target gene of PGC-1alpha
-
-
?
additional information
?
-
-
lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators, e.g. PPARgamma coactivator 1alpha, i.e. PGC-1alpha, to modulate gene expression in lipid metabolism
-
-
?
additional information
?
-
-
phosphatidic acid phosphohydrolase 1 and protein kinase C are required for Toll-like receptor-4-mediated group IVA phospholipase A2 activation, regulation, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in de novo synthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine
-
-
?
additional information
?
-
-
the Mg2+-dependent enzyme of rat lung is involved in pulmonary glycerolipid biosynthesis
-
-
?
additional information
?
-
-
the activity associated with the cytosol has a role in phosphocholine biosynthesis in rat lung
-
-
?
additional information
?
-
-
the enzyme catalyzes the final steps in the reesterification of fatty acids to triacylglycerols
-
-
?
additional information
?
-
-
key enzyme involved in glycerolipid synthesis where it converts phosphatidic acid to diacylglycerol. PAP-1 is involved in phospholipid biosynthesis
-
?
additional information
?
-
-
rate-limiting enzyme for triglyceride synthesis, short-term administration of conjugated linoleic acid reduces activity 20%
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, physiological roles of enzyme activity at the cell surface and intracellularly, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids, physiological roles of LPP isozymes
-
-
?
additional information
?
-
-
the enzyme activity is involved in generation of phosphatidic acid and diaclyglycerol implicated in signal transduction, and in aging, overview
-
-
?
additional information
?
-
-
phosphatidic acid phosphohydrolase, PAP, catalyzes the dephosphorylation of phosphatidic acid to diacylglycerol, the second messenger responsible for activation of protein kinase C
-
-
?
additional information
?
-
-
expression of lipin-1 cells stimulates glycerolipid synthesis and secretion in McA-RH7777, overview
-
-
?
additional information
?
-
-
lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators, e.g. PPARgamma coactivator 1alpha, i.e. PGC-1alpha, to modulate gene expression in lipid metabolism
-
-
?
additional information
?
-
-
the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
-
-
?
additional information
?
-
-
the 45000 Da enzyme form and 104000 Da enzyme form are induced when cells enter the stationary phase of growth
-
-
?
additional information
?
-
-
the enzyme plays an important role in regulating lipid synthesis in Saccharomyces cerevisiae, the enzyme is also involved in cell signaling mechanisms as part of the phospholipase D-phosphatidate phosphatase pathway
-
?
additional information
?
-
-
lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
-
-
?
additional information
?
-
-
the enzyme plays a major role in the synthesis of triacylglycerols and phospholipids in Saccharomyces cerevisiae, the PAH1 gene product is essential for its roles in lipid metabolism and cell physiology, role of PAH1-encoded PAP1 in lipid synthesis, pathway, overview
-
-
?
additional information
?
-
-
lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators to modulate gene expression in lipid metabolism
-
-
?
additional information
?
-
-
the diacylglycerol formed by the enzyme is used as a substrate for galactolipid synthesis on the inner envelope membrane
-
-
?
additional information
?
-
-
the functional role of the enzyme in lamellar bodies is proposed in relation to glycerophospholipd metabolism
-
-
?
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2,2'-dithiodipyridine
-
9 mM, 90% inhibition of Mg2+-dependent enzyme, 16% inhibition of Mg2+-independent enzyme
4,4'-dithiodipyridine
-
9.0 mM, 96% inhibition of Mg2+-dependent enzyme, 20% inhibition of Mg2+-independent enzyme
4-chlormercuriphenylsulfonic acid
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.2 mM, 80% inhibition of Mg2+-dependent enzyme, no inhibition of Mg2+-independent enzyme
cystamine dihydrochloride
-
1 mM, 25% inhibition of Mg2+-dependent enzyme, 8% inhibition of Mg2+-independent enzyme
diacylglycerol diphosphate
DMSO
-
addition to the reaction mixture results in a dose-dependent inhibition of PAP1 activity, 25% loss of PAP1 activity at a 1% concentration
epinephrine
promotes dephosphorylation of lipin, but has no effect on PAP activity, markedly decreases amounts of lipin and PAP activity in the soluble fraction
ethanol
-
inhibition of PAP-1
lysophosphatidic acid
-
-
lysophosphatidylethanolamine
-
-
lysophosphatidylglycerol
-
-
N,N'-p-phenylenedimaleimide
-
0.4 mM, 44% inhibition of Mg2+-dependent enzyme, 7% inhibition of Mg2+-independent enzyme
Na3VO4
-
2 mM, about 90% inhibition
oleate
-
reversed by phosphatidic acid and albumin
oleic acid
promotes dephosphorylation of lipin, but has no effect on PAP activity, markedly decreases amounts of lipin and PAP activity in the soluble fraction
p-chloromercuriphenylsulfonic acid
p-nitrophenyl phosphate
-
inhibits hydrolysis of phosphatidic acid
palmitate
-
1 mM, 30% inhibition
phosphatidate
-
conpetitive versus diacylglycerol diphosphate
phosphatidylcholine
-
slight inhibition of cytosolic activity
phosphatidylglycerol
-
0.7 mg/ml, 75% inhibition
RNAi2
reduces expression levels of LPR1 by ca. 60% in SK-OV-3 cells
-
SDS
1%, strong inhibition
shRNA
-
lipin 2 shRNA treatment significantly reduces hepatocyte PAP-1 activity in both wild-type and fld hepatocytes
-
spermidine trihydrochloride
-
7% inhibition at equimolar concentration of substrate, PAP-2
sphingomyelin
-
72% inhibition at equimolar concentration with pure phosphatidic acid. No effect with equimolar concentrations of phosphatidic acid mixed with phosphatidylcholine
sphingosine 1-phosphate
-
-
thimerosal
-
0.5 mM, 85% inhibition of Mg2+-dependent enzyme, 12% inhibition of Mg2+-independent enzyme
vanadate
10 mM, strong inhibition
Zwitterionic phospholipids
-
slight inhibition
-
1,2-diacylglycerol
-
-
ATP
-
half-maximal inhibition at 0.2 mM
ATP
-
complex inhibition of the 104-kDa enzyme form, inhibition of the 45-kDa enzyme form, inhibition by nucleotides involves the chelation of Mg2+ ions
ATP
-
the mechanism of inhibition by ATP is complex, affecting both the Vmax and Km for phosphatidic acid, competitive to Mg2+ and involving the chelation of the cofactor
bromoenol lactone
-
bromoenol lactone-induced apoptosis is accompanied by a very strong inhibition of PAP-1-regulated events, such as incorporation of choline into phospholipids and de novo incorporation of arachidonic acid into triacylglycerol
bromoenol lactone
-
inhibition of PAP-1
bromoenol lactone
-
i.e. BEL OR U-73122
bromoenol lactone
-
selective inhibition of PAP1
Ca2+
-
1 mM, 10% inhibition
Ca2+
-
activity with aqueously dispersed phosphatidic acid
Ca2+
-
inhibition at optimal concentrations of Mg2+
Ca2+
-
10 mM, 60% inhibition of PAP-2
Ca2+
-
IC50: 15 mM, reaction with phosphatidic acid. IC50: 7.1 mM, reaction with diacylglycerol diphosphate. IC50: 8.2 mM, reaction with lysophosphatidic acid
chlorpromazine
-
-
chlorpromazine
-
competitive inhibition at optimal concentrations of Mg2+
chlorpromazine
-
55% inhibition at equimolar concentration of substrate, PAP-2
Co2+
-
IC50: 0.029 mM, reaction with phosphatidic acid. IC50: 1.1 mM, reaction with diacylglycerol diphosphate. IC50: 1.2 mM, reaction with lysophosphatidic acid
CTP
-
-
CTP
-
complex inhibition of the 104-kDa enzyme form, inhibition of the 45-kDa enzyme form, inhibition by nucleotides involves the chelation of Mg2+ ions
CTP
-
the mechanism of inhibition by CTP is complex, affecting both the Vmax and Km for phosphatidic acid, competitive to Mg2+ and involving the chelation of the cofactor
diacylglycerol
-
-
diacylglycerol
-
DPP1-encoded PAP2 enzyme is inhibited by CDP-DAG
diacylglycerol diphosphate
-
competitive with respect to phosphatidic acid
diacylglycerol diphosphate
-
conpetitive versus phosphatidate
diacylglycerol diphosphate
-
-
EDTA
-
50 mM, 70% inhibition
EDTA
-
inhibition of hydrolysis of phosphatidate bound to microsomal membrane or phosphatidate in sonicated dispersion of organic solvent-disrupted microsomes, no effect on hydrolysis of phosphatidate dispersed in sonicated microsomal lipid
EDTA
-
inhibits activity with membrane-bound phosphatidic acid in the cytosol by 65%, the activity with aqueously dispersed phosphatidic acid is inhibited 10%
EDTA
-
1.0-2.0 mM, complete loss of cytosolic activity, reduced microsomal activity
EDTA
-
complete inhibition at 2 mM
F-
-
50 mM, 80% inhibition
F-
-
activity with aqueously dispersed phosphatidic acid
F-
-
50 mM, 90% inhibition
Insulin
markedly decreases the amounts of lipin and PAP activity in microsomes, effects of insulin are attenuated by rapamycin or by inhibiting PI 3 kinase
-
Insulin
-
phosphorylation inhibits activity, lipin 1 is phosphorylated in response to insulin treatment in adipocytes in an mTOR-dependent manner
-
Mg2+
about 75% inhibition at 20 mM, isozyme LPPgamma; about 95% inhibition at 20 mM, isozyme LPPepsilon1
Mg2+
-
2.5 mM, slight inhibition
Mg2+
-
at high concentrations, activity with aqueously dispersed phosphatidic acid
Mg2+
-
15 mM MgCl2, 10-20% inhibition of PAP-2
Mg2+
-
inhibition of reaction with diacylglycerol diphosphate. Little effect on reaction with lysophosphatidic acid and phosphatidic acid
Mn2+
-
above 0.1 mM, when assayed in presence of 5 mM MgCl2
Mn2+
-
activity with aqueously dispersed phosphatidic acid
Mn2+
-
IC50: 0.066 mM, reaction with phosphatidic acid. IC50: 0.01 mM, reaction with diacylglycerol diphosphate. IC50: 0.091 mM, reaction with lysophosphatidic acid
N-ethylmaleimide
-
-
N-ethylmaleimide
-
inhibition of the 45-kDa and 104-kDa enzyme forms
N-ethylmaleimide
-
potent inhibitor
NaF
-
-
NaF
-
5 mM, 21% inhibition of reaction with phosphatidic acid, 30% inhibition of reaction with diacylglycerol diphosphate and 44% inhibition of the reaction with lysophosphatidic acid
NEM
-
inhibition of cytosolic and light membrane activity
NEM
-
the enzyme from plasma membrane is insensitive to inhibition, the enzyme from cytosol and microsomes is sensitive to NEM
NEM
inhibition of isozyme DPPL1; inhibition of isozyme DPPL2
NEM
-
inhibition of PAP-1
NEM
-
the Mg2+-dependent enzyme is inhibited, the Mg2+-independent enzyme is unaffected
NEM
-
1 mM, 80% inhibition of Mg2+-dependent enzyme, 10% inhibition of Mg2+-independent enzyme
NEM
-
the Mg2+-dependent enzyme form is inhibited, the Mg2+-independent enzyme form is not inhibited
NEM
-
2 mM, complete inhibition of PAP-1. NEM, up to 8 mM has little effect on PAP-2
NEM
-
isozyme PAP1 is sensitive to NEM, while isozyme PAP2 is not
NEM
-
70% inhibition of isozyme PAP-1; 70% inhibition of isozyme PAP-1, 30% inhibition of isozyme PAP-2
NEM
-
45000 Da enzyme form, at 1 mM
NEM
-
IC50: 0.23 mM, reaction with phosphatidic acid. IC50: 0.12 mM, reaction with diacylglycerol diphosphate. IC50: 0.17 mM, reaction with lysophosphatidic acid
NEM
-
potent inhibition of LPP1
NEM
-
the yeast DPP1-encoded PAP2 activity is insensitive to NEM, whereas LPP1-encoded PAP2 activity is sensitive to NEM
p-chloromercuriphenylsulfonic acid
-
45000 Da enzyme form, at 1 mM
p-chloromercuriphenylsulfonic acid
-
-
PCMB
-
-
PCMB
-
0.05 mM, 90% inhibition
Phenylglyoxal
-
inhibition of the 45-kDa and 104-kDa enzyme forms
Phenylglyoxal
-
inhibition of the 45000 Da enzyme form and the 104000 Da enzyme form
Phenylglyoxal
-
IC50: 7 mM, reaction with phosphatidic acid. IC50: 3.4 mM, reaction with diacylglycerol diphosphate. IC50: 2.5 mM, reaction with lysophosphatidic acid
Phenylglyoxal
-
is an arginine reactive compound, inhibits PAP1 activity in dose-dependent manner
phosphatidic acid
-
competitive inhibition
phosphatidic acid
-
competitive with respect to diacylglycerol diphosphate
phosphatidic acid
-
substrate inhibition
phytosphingosine
-
-
phytosphingosine
-
inhibition of PAH1
propanolol
-
slight stimulation
propanolol
-
effective inhibitor of type 1 phosphatidic acid phosphatase, modest inhibitor of phosphatidic acid phosphatase PAP-2a, PAP-2b and PAP-2c
propanolol
-
inhibition of the 45000 Da enzyme form and the 104000 Da enzyme form
propranolol
-
inhibition of PAP-1
propranolol
-
moderately effective inhibitor of LPP activity
propranolol
-
inhibition of the 45-kDa and 104-kDa enzyme forms
propranolol
-
IC50: 2.51 mM, reaction with phosphatidic acid. IC50: 1.68 mM, reaction with diacylglycerol diphosphate. IC50: 7.17 mM, reaction with lysophosphatidic acid
propranolol
-
interacts with the Mg2+-binding site of the enzyme, inhibits PAP1 activity in dose-dependent manner
siRNA
-
rat2 fibroblasts treated with siRNA for LPP2 show a ca. 60% decrease in mRNA for the targeted LPP
-
siRNA
-
rat2 fibroblasts treated with siRNA for LPP1 show about a 60% decrease in mRNA for the targeted LPP
-
siRNA
-
decrease of LPP1 mRNA by ca. 90%, knockdown of endogenous LPP1 activity by about 50% and increase of lyso-phosphatidic acid-induced migration
-
spermine
-
above 1 mM
spermine
-
55% inhibition at equimolar concentration of substrate, PAP-2
sphinganine
-
-
sphinganine
-
inhibition of PAH1
sphingosine
-
-
sphingosine
-
93% inhibition at equimolar concentration with pure phosphatidic acid. 29% inhibition with equimolar concentrations of phosphatidic acid mixed with phosphatidylcholine
sphingosine
-
inhibition of PAH1
Triton X-100
-
-
Triton X-100
-
slight depression of activity with aqueously dispersed phosphatidic acid
Tween 20
-
hydrolysis of phosphatidate bound to microsomal membrane in presence of optimal concentration of 8 mM
Zn2+
-
-
Zn2+
-
above 0.1 mM, when assayed in presence of 5 mM MgCl2
Zn2+
-
zinc depletion increases the enzyme activity in vivo, stress condition of zinc depletion induces DPP1 expression
Zn2+
-
PAP2 activity is also inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
additional information
-
light inhibition of PAP2 in ROS is a transducin-mediated mechanism
-
additional information
-
light regulation of the lipid phosphate phosphatases, overview
-
additional information
-
no inhibition by NEM
-
additional information
the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide
-
additional information
the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide
-
additional information
the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide
-
additional information
-
the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide; the enzyme is insensitive to N-ethylmaleimide
-
additional information
-
caspase3/7 inhibitor N-acetyl-Asp-Glu-Val-Asp-CHO blocks cellular effects of lysophosphatidic acid and sphingosine 1-phosphate on p42/p44 MAPK pathway
-
additional information
-
no inhibition by NEM
-
additional information
-
CHAPS-insoluble LPP1 is resistant to the actin-disrupting drug cytochalasin D. CHAPS-resistant floating complexes containing LPP1 are sensitive to cholesterol depletion
-
additional information
-
insensitive to inhibition by the alkylating agent N-ethyl maleimide
-
additional information
-
the presqualene diphosphate phosphatase is a potent Mg2+-independent, NEM-insensitive type II PAP
-
additional information
mitotic phosphorylation of lipin 1 inhibits its phosphatidic acid phosphatase activity
-
additional information
-
presence of EDTA or EGTA does not significantly affect enzyme activity
-
additional information
-
no inhibition by NEM
-
additional information
epinephrine and oleic acid promote dephosphorylation of lipin 1, insulin and epinephrine control lipin primarily by changing localization rather than intrinsic PAP activity, overview
-
additional information
-
PAP-1 chemical inhibition does not reduce the synergistic activation of group IVA phospholipase A2
-
additional information
-
mitotic phosphorylation of lipin 2 inhibits its phosphatidic acid phosphatase activity
-
additional information
-
phosphorylation inhibits activity, phosphorylation of lipin 1 on multiple sites correlates with a decrease of its microsomal-bound pool
-
additional information
no inhibition by N-ethylmaleimide
-
additional information
-
no inhibition by N-ethylmaleimide
-
additional information
-
no inhibition by NEM
-
additional information
-
insensitive to inhibition by the alkylating agent N-ethyl maleimide
-
additional information
-
no effect on the enzyme forms by choline
-
additional information
-
phosphorylation of Pah1p inhibits its PAP1 activity. Pah1p is phosphorylated in vivo on at least 12 sites, including seven Ser/Thr-Pro (S/T-P) motifs. Pah1p is phosphorylated in mitotic cells in a Cdk1/Cdc28p-dependent manner. Mutations in the Nem1p-Spo7p complex result in hyperphosphorylation of Pah1p
-
additional information
-
the isozymes are not affected by wounding or by treatment with jasmonic acid
-
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malfunction
-
catalytically deficient FLAG-tagged H223L LPP1 mutant can form an oligomer with wild-type LPP1, whereby wild-type LPP1 activity is preserved in the oligomer
malfunction
-
deletion of PAH1 leads to the accumulation of phosphatidic acid but also the concomitant reduction of 1,2-diacyl-sn-glycerol and triacylglycerol levels and changes in phosphatidylethanolamine and phosphatidylcholine amounts. Mammalian lipins can rescue the yeast pah1DELTA mutant. A septuple S/T-P Pah1p phosphorylation null mutant displays higher specific activity when compared to the wild-type enzyme. Mutations in Pah1p result in transcriptional derepression of UAS(INO)-containing genes. Overexpression of the more active septuple S/T-P Pah1p phosphorylation null mutant causes inositol auxotrophy, which can be rescued by the deletion of the Opi1p repressor. Pah1DELtAopi1DELTA double mutant exhibits a synergistic effect on the transcriptional derepression of two UAS(INO)-containing genes, INO1 and OPI3. PAH1 mutants display irregularly shaped nuclei with long stacks of membranes that contain nuclear pores and appear to be in contact with the nuclear envelope. Inactivation of the phosphatidic acid signals downstream of Pah1p by either deleting the transcriptional activator Ino2p or overexpressing the repressor Opi1p, can restore normal nuclear shape in nem1DELTA spo7DELTA or pah1DELTA deletion mutants
malfunction
-
depletion of LPP3 results in destabilization of beta-catenin, which in turn reduces fibronectin synthesis and deposition, which results in inhibition of endothelial cell migration. Reexpression of beta-catenin but not p120-catenin in LPP3-depleted endothelial cells restores de novo synthesis of fibronectin, which mediates endothelial cell migration and formation of branching point structures. LPP3-RAD mutant, which is defective for integrin binding and a LPP3-PD mutant, which is defective for phosphatase activity stimulate lymphoid enhancer binding factor 1-dependent transcription 3- or 5fold, respectively. The LPP3 mutant that lacks both adhesion and lipid phosphatase domains (hLPP3-RAD+PD) fails to stimulate luciferase activity
malfunction
-
double mutant pah1pah2 plants have decreased phosphatidic acid hydrolysis, thus affecting the eukaryotic pathway of galactolipid synthesis. Upon phosphate starvation, pah1pah2 plants are severely impaired in growth and membrane lipid remodeling. PAP activity in the supernatant fraction of pah1pah2 mutant leaves is decreased by approximately 40% as compared to that in wild-type leaves. Defect in PAP activity in vivo in rosette leaves of pah1pah2 mutants. Relative amount of phosphatidic acid increases to 1.61fold in pah1pah2 double mutants as compared to the wild-type. 26% increase in phosphatidic acid levels in pah1pah2 plants as compared to wild-type plants. The transgenic plants (35S::PAH1-GFP, pah1pah2 and 35S::PAH2-GFP, pah1pah2) recover the phenotype observed in pah1pah2 mutant. Endoplasmic reticulum-localized eukaryotic pathway of membrane lipid metabolism is compromised in pah1pah2 double mutants
malfunction
-
downregulating LPIN-1 by RNAi results in the appearance of membrane sheets and other abnormal structures in the peripheral endoplasmic reticulum. Lpin-1 RNAi causes defects in nuclear envelope breakdown, abnormal chromosome segregation and irregular nuclear morphology. RNAi of lipin results in reduced body size and defects in lipid storage
malfunction
-
in fat pads from mice deficient for lipin 1 (fld mice) and in 3T3-L1 adipocytes depleted of lipin 1 there is increased expression of several nuclear factor of activated T-cells target genes including TNFalpha, resistin, FABP4 and PPARgamma. Lipin 1 with the highly conserved amino-terminal NLIP domain deleted (DELTAN) is capable of both interaction and repression
malfunction
-
in mutants where both Wun and wun2 are disrupted, germ cells scatter throughout the embryo and eventually die
malfunction
-
knockdown of endogenous lipin-1 expression decreases the secretion of newly synthesized triglycerides
malfunction
-
lipin 1 deficiency does not affect PAP-1 activity in neonatal mice and leads to hepatic triglyceride accumulation. Loss of lipin 2 markedly impairs hepatocyte PAP-1 activity but does not affect basal rates of triglyceride synthesis. Lipin 2 knockdown abrogates triglyceride synthesis under conditions of increased fatty acid availability
malfunction
-
lipin 1 gene is mutated in the fatty liver dystrophy mouse, which displays features of generalized lipodystrophy, characterized by significant reduction in the adipose tissue mass and in the cellular lipid droplet content
malfunction
-
lipin-1 deficiency causes lipodystrophy, neonatal fatty liver, peripheral neuropathy, insulin resistance, and increased susceptibility to atherosclerosis
malfunction
-
lipin-1 deficiency in rare human patients, causes acute myoglobinuria in childhood, does not result in lipodystrophy in these individuals. Muscle sample from a patient with lipin-1 deficiency reveals elevated phosphatidate levels. Rare patients with lipin-2 deficiency have a complex phenotype known as Majeed syndrome, characterized by recurrent osteomyelitis, fever, and anemia
malfunction
-
lipin-1 deficiency produces lipodystrophy. In fatty liver dystrophy mice, occurrence of fatty liver and hypertriglyceridemia during the neonatal period, and peripheral neuropathy, which progresses throughout adulthood. Fatty liver dystrophy mice are lipodystrophic, develop insulin resistance, and have increased susceptibility to atherosclerosis. Lipin-2 cannot compensate for lipin-1 function in adipose tissue of fatty liver dystrophy mice
malfunction
-
LPP1 hypomorph mice (Ppap2atr/tr) have depleted LPP1 expression in most tissues. Lysophosphatidate concentrations in the plasma are higher in Ppap2atr/tr mice compared with controls. Embryos from LPP3 knockout mice fail to form a chorio-allantoic placenta and yolk sac vasculature and some embryos show shortening of the anterior-posterior axis similar to axin deficiency, a critical regulator of Wnt signaling. LPP2 knockout mice are fertile and viable with no obvious phenotype
malfunction
-
mutations affecting lipin-1 and lipin-2 cause human disease. Human lipodystrophic subjects do not show causative mutations in the LPIN1 gene. Mutations in LPIN1 in patients with recurrent acute myoglobinuria in childhood. Distinct inactivating mutations in patients from several ethnic backgrounds and at dispersed locations throughout the lipin-1 protein structure. LPIN1 polymorphisms are associated with numerous metabolic traits, like insulin and/or glucose levels, resting metabolic rate, and systolic blood pressure. LPIN1 polymorphisms associated with response of type 2 diabetic patients to rosiglitazone. LPIN1 polymorphism can cause an amino acid substitution within the C-LIP domain, which is associated with statin-induced myopathy
malfunction
-
nuclear localization is abrogated by mutating the consensus sumyolation motifs. Sumoylation site mutant of lipin-1alpha loses the capacity to coactivate the transcriptional (co-) activators PGC-1alpha and MEF2, consistent with its nuclear exclusion
malfunction
RNAi downregulation of lpin-1 for 48 hours or longer results in 100% embryonic lethality on N2 worms. Inactivation of lpin-1 promotes bi-nucleation. Co-depletion of lpin-1 and lamin significantly rescues the effect of lpin-1 depletion on nuclear envelope breakdown
malfunction
-
symptoms of the Majeed syndrome result from a loss of lipin-2 PAP activity. Loss of lipin-2 PAP activity in erythrocytes and lymphocytes may contribute to the anemia and inflammation phenotypes observed in Majeed syndrome patients
malfunction
-
yeast DELTAdpp1DELTAlpp1DELTApah1 mutant is complemented by Arabidopsis phosphatidate phosphatases PAH1 and PAH2 in vivo
malfunction
-
cells lacking phosphatidate phosphatase are sensitive to exogenous fatty acids in the order of toxicity palmitoleic acid > oleic acid > palmitic acid
malfunction
-
fatty liver dystrophy mice carrying mutations within the lipin 1 gene display life-long deficiency in adipogenesis, insulin resistance, neonatal hepatosteatosis and hypertriglyceridemia, as well as increased atherosclerosis susceptibility. Lipin-1 deficiency results in the activation of the sterol regulatory element binding protein 1 and its target genes as well as in very high expression levels of stearoyl-CoA desaturase-1 and apoA-IV. Acute lipin-1 deficiency in the mouse liver abolishes fasting-induced activation of Ppara and several PPARalpha/PGC-1alpha target genes, such as Acadvl, Acadm and Fabp1
malfunction
-
lack of wun2 in germ cells results in germ cell death
malfunction
-
lipid phosphate phosphatase-3-knockdown inhibits both U-87 and U-118 glioblastoma cell proliferation in culture and tumor growth in xenograft assays. Lipid phosphate phosphatase-3-knockdown reduces beta-catenin, cyclin-D1, and CD133 expression, with a concomitant increase in phosphorylated beta-catenin
malfunction
-
lipin-1 deficiency in humans is not associated with lipodystrophy. In HeLa cells, knockdown of lipin-2 results in increased phosphatidate phosphatase activity, apparently as a result of compensatory upregulation of lipin-1
malfunction
-
partitioning of substrate between the prokaryotic and eukaryotic pathways is perturbed in the pah1 pah2-1 double mutant. Both the total lipid content and the phospholipid content of pah1 pah2-1 mutant leaves and roots is greater than wild type on a per unit fresh weight basis
malfunction
-
the inhibition of stomatal opening is less sensitive to abscisic acid in lipid phosphate phosphatase 2-deficient plants than in wild type plants. Lipid phosphate phosphatase 2-deficient plants accumulate more phosphatidic acid than wild type and have a higher phosphatidic acid kinase activity
malfunction
-
cell death-inducing stresses are required for defense activation in DS1-phosphatidic acid phosphatase-silenced Nicotiana benthamiana
malfunction
-
enzyme deletion causes multiple phenotypes, especially severe hyphal defects, increased sensitivity to cell wall stress, and reduced virulence in mice
malfunction
LPP3 deficiency, specifically targeted at vascular cell types, induces endothelial permeability, promotes leukocyte adhesion to endothelial cells and stimulates smooth muscle cell proliferation. Hepatocyte-specific Plpp3 deficiency, by modulating the plasma lipidome, exacerbates atherosclerosis development in Apoe-/-x01mice
malfunction
LPP3 deficiency, specifically targeted at vascular cell types, induces endothelial permeability, promotes leukocyte adhesion to endothelial cells, and stimulates smooth muscle cell proliferation
malfunction
LPP3 silencing in human primary aortic endothelial cells enhances secretion of inflammatory cytokines, leucocyte adhesion, cell survival, and migration and impairs angiogenesis, whereas wild-type LPP3 overexpression reversed these effects and induces apoptosis
malfunction
-
cells lacking phosphatidate phosphatase are sensitive to exogenous fatty acids in the order of toxicity palmitoleic acid > oleic acid > palmitic acid
-
metabolism
isoform lipin-1 binds to serine/threonine protein phosphatase-1 catalytic subunit through a HVRF binding motif. Mutating the HVRF motif in the highly conserved N terminus of lipin-1 greatly decreases serine/threonine protein phosphatase-1 catalytic subunit interaction. Mutations of other residues in the N terminus of lipin-1 also modulate serine/threonine protein phosphatase-1 catalytic subunit binding. Serine/threonine protein phosphatase-1 catalytic subuni binds poorly to a phosphomimetic mutant of lipin-1 andbinds well to the non-phosphorylatable lipin-1 mutant. Mutating the HVRFmotif also abrogates the nuclear translocation and phosphatidate phosphatase activity of lipin-1
metabolism
isoform Pah1p is a bona fide substrate of protein kinase C. The phosphorylation reaction is time- and dose-dependent and dependent on the concentrations of ATP and Pah1p. The stoichiometry of the reaction is 0.8 mol of phosphate/mol of Pah1p. Unlike its phosphorylations by Pho85p-Pho80p and protein kinase A, which cause a significant reduction in phosphatidate phosphatase activity, the phosphorylation of Pah1p by protein kinase C has a small stimulatory effect on the enzyme activity. Protein kinase C does not have a major effect on Pah1p location or its function in triacylglycerol synthesis
metabolism
isoform Pah1p is stabilized in mutants with impaired proteasome and ubiquitination functions. The pre1 pre2 mutations that eliminate nearly all chymotrypsin-like activity of the 20 S proteasome have the greatest stabilizing effect on enzyme levels. Alteration in phosphatidate and/or diacylglycerol levels might be the signal that triggers Pah1p degradation
metabolism
-
target of rapamycin complex TORC1 inhibits the function of phosphatidate phosphatase Pah1, to prevent the accumulation of triacylglycerol. TORC1 regulates Pah1 in part indirectly by controlling the phosphorylation status of Nem1 within the Pah1-activating, heterodimeric Nem1-Spo7 protein phosphatase module
metabolism
-
the activity of the enzyme controls the expression of phosphatidylserine synthase for membrane phospholipid synthesis
metabolism
-
the enzyme is involved in triacylglycerol biosynthesis during lipogenesis
metabolism
the enzyme plays a major role in controlling the utilization of phosphatidate for the synthesis of triacylglycerol or membrane phospholipids
metabolism
the enzyme regulates phosphatidylcholine biosynthesis in Arabidopsis by phosphatidic acid-mediated activation of CTP:phosphocholine cytidylyltransferase activity
metabolism
-
the enzyme is involved in triacylglycerol biosynthesis during lipogenesis
-
metabolism
-
the activity of the enzyme controls the expression of phosphatidylserine synthase for membrane phospholipid synthesis
-
metabolism
-
the enzyme plays a major role in controlling the utilization of phosphatidate for the synthesis of triacylglycerol or membrane phospholipids
-
physiological function
-
activation of fibroblasts by lysophosphatidate causes a translocation of Mg2+-dependent PAP activity to the membrane fraction within 2 min when the production of phosphatidic acid and diacylglycerol is increased by lysophosphatidate and platelet-derived growth factor. Translocations of PAP1 activity probably results from the increased presence of phosphatidic acid in membranes
physiological function
-
decreases the growth, survival, and tumorigenesis of ovarian cancer cells. LPP3 contains an exposed arginine-glycine-aspartate (RGD) cell adhesion sequence. LPP3 expression increases cell/cell interactions through alphavbeta3 and anti-alpha5beta1 integrins. LPP1 regulates lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells
physiological function
-
dimerization of LPP is not required for biological activity. Wun and wun2 act redundantly in germ cells as repellant factors that guide migrating germ cells in embryos. Overexpression of wun or wun2 in somatic tissues causes germ cell repulsion and death
physiological function
-
ectopic expression of lipin-1 in L6 myotube increases carnitine palmitoyltransferase-1 and delta-aminolevulinate synthase gene expression
physiological function
-
endogenous 14-3-3 proteins interact with lipin-1alpha in HEK293 cells, overexpression of 14-3-3 promotes the cytoplasmic localization of lipin-1 in 3T3-L1 adipocytes. Effect of 14-3-3 is mediated through a serine-rich domain in lipin-1. Insulin stimulates interaction with 14-3-3 and cytoplasmic localization of lipin-1alpha in 3T3-L1 adipocytes
physiological function
-
endogenous LPP2 and LPP3 form a complex. Endogenous LPP2 and LPP3 form homo- and hetero-oligomers, which differ in their subcellular localization and which may confer differing spatial regulation of phosphatidic acid and sphingosine 1-phosphate signalling
physiological function
-
enhanced expression of lipin-1 in a hepatocyte cell line leads to stimulation of triglyceride synthesis and secretion
physiological function
-
enhanced expression of lipin-1 is involved in exercise-induced mitochondrial enzyme adaptations, possibly through 5'-AMP-activated protein kinase- and beta2-adrenergic receptor-related mechanisms
physiological function
-
has essential roles in lipid droplet and phospholipid metabolism
physiological function
-
has essential roles in lipid droplet and phospholipid metabolism. Pah1p and its regulators are required for the maintenance of a spherical nuclear shape. Pah1p carries an acidic stretch at the C-terminal end. PAH1/SMP2 are independently identified as a dosage suppressor of the spo7DELTA and nem1DELTA deletions. Pah1p has a key signalling function in the transcriptional regulation of genes encoding phospholipid biosynthetic enzymes. Pah1p may have roles in the biogenesis of membrane-bound organelles
physiological function
-
key role for lipin-1 in adipocyte differentiation and lipid biosynthesis
physiological function
-
key role for LPP3 in orchestrating phosphatase and tensin-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling in endothelial cell migration, cell-cell adhesion, and formation of branching point structures. In subconfluent endothelial cells, LPP3 induces expression of fibronectin via beta-catenin/lymphoid enhancer binding factor 1 signaling in a phosphatase and tensin homologue-dependent manner. In confluent endothelial cells, depletion of p120-catenin restores LPP3-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling. In confluent endothelial cells, depletion of p120-catenin restores LPP3-mediated beta-catenin/lymphoid enhancer binding factor 1 signaling. C-terminal domain of LPP3 regulates the expression of p120ctn and VE-cadherin as well as formation of branching point structures. LPP1 and LPP2 have no effect on luciferase (lymphoid enhancer binding factor 1) activity, whereas LPP3 yields an 9fold increase in luciferase activity. LPP1 and LPP2 show no change in basal phosphorylation of beta-catenin
physiological function
-
lipin 1 is a potentially important link between triacylglycerol synthesis and adipose tissue inflammation. Lipin 1 represses nuclear factor of activated T-cells c4 transcriptional activity through protein-protein interaction and in the context of at least two different composite elements. Specific residues required for interaction with lipin 1 are contained within the RHD/DNA binding domain and carboxy terminus of nuclear factor of activated T-cells c4. Lipin 1 is present at the promoters of nuclear factor of activated T-cells c4 transcriptional targets in vivo. Lipin 1 protein and total PAP activity are decreased with increasing adiposity in the visceral, but not subcutaneous, fat pads of ob/ob mice. Lipin 1 can act to repress or activate transcription factors. Lipin 1 interacts with nuclear factor of activated T-cells c4 bound to DNA and is present at the promoters of nuclear factor of activated T-cells target genes. Lipin 1 recruits a histone deacetylase to repress nuclear factor of activated T-cells c4 transcription
physiological function
-
lipin 1 may play a role in blood pressure regulation, especially in men. The minor allele of rs10495584 is nominally associated with lower mean systolic and diastolic blood pressures in men, but not in women
physiological function
-
lipin 1beta appears to be involved in the pathogenesis of insulin resistance in polycystic ovary syndrome
physiological function
-
lipin 2 plays an important role as a hepatic PAP-1 enzyme. Lipin 2 overexpression increases PAP-1 activity in HepG2 cells. Increased hepatic expression of lipin 2 plays a role in increased hepatic triglyceride synthesis rates in ob/ob mice
physiological function
-
lipin is needed for lipid storage and development. Lipin activity is needed for normal nuclear structure in dividing cells
physiological function
-
lipin proteins serve an important role in regulating the balance of lipid intermediates, including phosphatidic acid and diacylglycerol, and maintenance of cellular lipid homeostasis
physiological function
-
lipin-1 accounts for all of the PAP activity in adipose tissue and skeletal muscle, but only part of the activity in liver, heart, kidney, and brain. Enhanced lipin-1 expression in adipose tissue or skeletal muscle promotes obesity. Lipin-2 and/or lipin-3 are capable of promoting VLDL synthesis and secretion
physiological function
-
lipin-1 may be a mediator of glucocorticoid effects in conditions such as fasting and obesity, genetic variations in this response may contribute to interindividual variations in lipin-1 expression levels. Glucocorticoid-induced Lpin1 regulation leads to increased protein and PAP1 activity
physiological function
-
lipin-1alpha may act as a sumoylation-regulated transcriptional coactivator in brain. Sumoylated forms of lipin-1 in muscle and liver are only marginally present. Lipin-1 (including both the alpha and beta isoforms) is modified by sumoylation at two consensus sumoylation sites, is sumoylated at relatively high levels in brain. No sumoylation of the related proteins lipin-2 and lipin-3
physiological function
-
lipin-2 expression in adipose tissue may compensate for lack of lipin-1
physiological function
-
lipin-2 has transcriptional coactivator activity for peroxisome proliferator-activated receptor-response elements similar to lipin-1. Lipin-1A activates PPRE-luciferase expression ca. 2fold
physiological function
-
lipin1 reinforces the positive feedback loop between CCAAT/enhancer-binding protein alpha and peroxisome proliferator-activated receptor gamma2, which is essential for adipogenesis and the maintenance of adipocyte functions. Lipin1 is necessary and accelerates 3T3-L1 adipocyte differentiation. Lipin1 maintains the expression of adipocyte functional genes in 3T3-L1 mature adipocytes. Lipin1 functions by interacting with and activating peroxisome proliferator-activated receptor gamma2
physiological function
lpin-1 affects dynamics of the peripheral endoplasmic reticulum. The enzyme has no detectable effect on nuclear envelope assembly and expansion, but is crucially required for nuclear envelope breakdown and lamin depolymerization during mitosis. Lpin-1 acts independently of nuclear pore complexes and the transmembrane nucleoporin gp210
physiological function
-
LPP1 forms both homo- and hetero-oligomers. Full catalytic activity is not required for oligomerization
physiological function
-
LPP2 forms a complex with the 32 kDa form of LPP3, but not with the 34 kDa form. LPP oligomers may regulate compartmentalized pools of sphingosine 1-phosphate and phosphatidic acid and contribute to the spatial signalling by these lipids within cells
physiological function
-
LPP3 contains arginine-glycine-glutamate (RGE) cell adhesion sequence, but murine LPP3 also interacts with alpha5beta1 and alphavalpha3 integrins. Transgenic mice that overexpress LPP1 demonstrate no significant differences in circulating lysophosphatidate concentrations compared with control mice. LPP3 functions as a Wnt signaling antagonist. Mice that overexpress LPP1 have decreased birth weight, sparse curly hair, and defective spermatogenesis causing infertility. LPP1 controls lysophosphatidate removal from the blood, which increases circulating lysophosphatidate levels. LPP2 regulates the timing of S-phase entry, but it is not essential for cell cycle progression
physiological function
-
LPP3 contains arginine-glycine-glutamate (RGE) cell adhesion sequence. LPP2 activity regulates S-phase entry of the cell cycle in rat2 fibroblasts
physiological function
-
LPP3 yields an 8fold increase in luciferase (lymphoid enhancer binding factor 1) activity
physiological function
-
PAH1 and PAH2 are the phosphatidate phosphatase responsible for the eukaryotic pathway of galactolipid synthesis. Membrane lipid remodeling mediated by these two enzymes is an essential adaptation mechanism to cope with phosphate starvation. Complements yeast DELTAdpp1DELTAlpp1DELTApah1 in vivo
physiological function
-
physiologically relevant increases in LPP1 activity in mouse embryonic fibroblasts (isolated from transgenic mice with 20 gene copies of LPP1) reduces lysophosphatidic acid- and platelet-derived growth factor-activation of ERK-1/2 and migration, resulting from down-regulation of typical proteinkinase C isoform(s) which are required for regulation of cell migration
physiological function
-
stable overexpression of LPP1 or LPP2 reduces sphingosine 1-phosphate, lysophosphatidic acid- and thrombin-induced activation of ERK-1/2
physiological function
-
sterol-mediated regulation of lipin 1 gene transcription modulates triglyceride accumulation
physiological function
the lipin1 gene may have a crucial effect on body lipid accumulation in pigs, whereas the lipin-beta isoform may play an important role in intramuscular fat deposition in obese pigs
physiological function
-
wunen generates a phospholipid gradient and thereby repels germ cells towards higher phospholipid levels and away from the midline. Wunen/wunen-2 also governs the death of mis-migrating germ cells and survival of pole cells which compete for a common phospholipid substrate with somatic cells
physiological function
-
forced expression of lipid phosphate phosphatase-3 in human colon tumor (SW-480) cells potentiates tumor growth via increased beta-catenin stability and cyclin-D1 synthesis. Elevated expression of lipid phosphate phosphatase-3 has no tumorigenic effects on primary cells. Lipid phosphate phosphatase-3 regulates glioblastoma cell migration
physiological function
-
isoform lipin-1gamma plays a specialized role in regulating brain lipid metabolism
physiological function
-
lipid phosphate phosphatase 2 is a part of abscisic acid signalling and participates to the regulation of stomatal movements
physiological function
-
lipid phosphate phosphatase mediates germ cell-germ cell repulsion, this repulsion is necessary for germ cell dispersal and proper transepithelial migration at the onset of migration and for the equal sorting of the germ cells between the two embryonic gonads during their migration
physiological function
-
lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1
physiological function
-
lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1
physiological function
-
lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1
physiological function
-
lipins are essential regulators of fat metabolism, adipogenesis, and organelle biogenesis
physiological function
-
phosphatidate phosphatase activity is essential in protecting cells from palmitoleic acid (fatty acid)-induced toxicity
physiological function
-
phosphatidic acid phosphatase enzymes, PAH1 and PAH2, are capable of repressing phospholipid biosynthesis at the endoplasmic reticulum in Arabidopsis thaliana. PAH1/2 play a role in the provision of eukaryotic substrate for galactolipid synthesis in leaves
physiological function
-
the lipin 1 polybasic motif is critical for lipin1beta function in phospholipid and neutral lipid metabolism. Lipin1beta also functions as transcriptional coactivator. Both the transcriptional and metabolic functions of lipin 1 are required for full complementation of the adipogenic differentiation of lipin-deficient MEF cells. Lipin1 is also an amplifier of PGC-1alpha, a nuclear coactivator of PPAR-alpha responsive gene transcription
physiological function
conditional deletion of the enzyme gene leads to a decrease in the content of diacylglycerol and triacylglycerol, whereas its overexpression in both Rhodococcus jostii RHA1 and Rhodococcus opacus PD630 promotes an increase up to 10 to 15% by cellular dry weight in triacylglycerol content. Expression in the nonoleaginous strain Rhodococcus fascians F7 promotes an increase in total fatty acid content up to 7% at the expense of free fatty acid, diacylglycerol, and triacylglycerol fractions. Coexpression with Atf2 gene encoding wax ester/diacylglycerol acyltransferase results in a fourfold increase in total fatty acid content by a further increase of the free fatty acid and triacylglycerol fractions
physiological function
expression of the gene in yeast complements the temperature-sensitive growth phenotype of the phosphatidic acid phosphatase deficient strain GHY58. In Streptomyces coelicolor, disruption of either isoform lppalpha or lppbeta has no effect on triacylglycerol accumulation. The simultaneous mutation of both genes provokes a drastic reduction in de novo triacylglycerol biosynthesis as well as in total triacylglycerol content. Overexpression of Lppalpha and Lppbeta in the wild type strain of Streptomyces coelicolor leads to a significant increase in triacylglycerol production. Membrane proteins isolated from an Escherichia coli strain expressing Lppalpha and Lppbeta display a considerable increase in phosphatidic acid phosphatase activity compared with the control strain
physiological function
isoform Pah1p regulates lipid synthesis and composition throughout growth. An enzyme deletion mutant shows dramatic reductions in the synthesis of triacylglycerols and diacylglycerols and increases in synthesis of phospholipids, fatty acids, and ergosterol esters when compared with the wild type control. Pahip is dephosphorylated by the Nem1p-Spo7p protein phosphatase complex. Nem1 deletion mutant cells exhibit defects in triacylglycerol synthesis and lipid metabolism that mirror those imparted by the Pah1 deletion mutation
physiological function
-
isoform PAH2 possesses the minimal function of phosphatidate phosphatase protein family in respiration. The enzyme is not essential for the normal growth and survival of Tetrahymena
physiological function
lipid phosphate phosphatase 3 regulates adipocyte sphingolipid synthesis, but not developmental adipogenesis or diet-induced obesity in mice
physiological function
LPP3 activity is crucial for vascular and heart development
physiological function
LPP3 activity is crucial for vascular and heart development
physiological function
LPP3 is a negative regulator of inflammatory cytokines, leucocyte adhesion, cell survival, and migration in human primary aortic endothelial cells, suggesting a protective role of LPP3 against endothelial dysfunction in humans
physiological function
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
physiological function
LPP3 regulates intracellular and extracellular lysophosphatidic acid and sphingosine-1-phosphate signalling through the dephosphorylation of these bioactive lipids
physiological function
-
the enzyme activity is required to support hepatitis C virus infection
physiological function
-
the enzyme plays an important role in hyphal growth, adaptability to environmental stresses, and virulence
physiological function
-
isoform PAH2 possesses the minimal function of phosphatidate phosphatase protein family in respiration. The enzyme is not essential for the normal growth and survival of Tetrahymena
-
physiological function
-
lipin-2 has transcriptional coactivator activity for peroxisome proliferator-activated receptor-response elements similar to lipin-1. Lipin-1A activates PPRE-luciferase expression ca. 2fold
-
physiological function
-
expression of the gene in yeast complements the temperature-sensitive growth phenotype of the phosphatidic acid phosphatase deficient strain GHY58. In Streptomyces coelicolor, disruption of either isoform lppalpha or lppbeta has no effect on triacylglycerol accumulation. The simultaneous mutation of both genes provokes a drastic reduction in de novo triacylglycerol biosynthesis as well as in total triacylglycerol content. Overexpression of Lppalpha and Lppbeta in the wild type strain of Streptomyces coelicolor leads to a significant increase in triacylglycerol production. Membrane proteins isolated from an Escherichia coli strain expressing Lppalpha and Lppbeta display a considerable increase in phosphatidic acid phosphatase activity compared with the control strain
-
physiological function
-
isoform PAH2 possesses the minimal function of phosphatidate phosphatase protein family in respiration. The enzyme is not essential for the normal growth and survival of Tetrahymena
-
physiological function
-
phosphatidate phosphatase activity is essential in protecting cells from palmitoleic acid (fatty acid)-induced toxicity
-
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H223L
-
mutated in C3 domain, catalytically deficient Myc-tagged R127K LPP1 and FLAG-tagged H223L LPP1 can form oligomers
R127K
-
mutated in C1 domain, catalytically deficient Myc-tagged R127K LPP1 and FLAG-tagged H223L LPP1 can form oligomers
D248T
-
site-directed mutagenesis, a monomeric, catalytically inactive mutant enzyme form
D712E/D714E
catalytically inactive. Mutant binds to serine/threonine protein phosphatase-1 catalytic subunit to the same extent as wild-type
F87A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit
I67A/I69A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to a decrase in binding to serine/threonine protein phosphatase-1 catalytic subunit
L58A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
L80A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit
R127K/H223L
-
negligible LPP1 activity, although each mutant is still able to form oligomers
S734L
-
Majeed mutation in lipin-2, which alters a serine residue that is located in the C-LIP domain downstream of the enzyme active site and coactivator motifs. Mutation completely abolishes PAP activity in both lipin-1 and lipin-2 backgrounds
V57A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
V64A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
D398E
-
catalytically inactive PAP enzymes with a mutation in a conserved NLIP domain residue fail to complement phenotypes caused by the pah1DELTA mutation
D400E
-
catalytically inactive PAP enzymes with a mutation in a conserved NLIP domain residue fail to complement phenotypes caused by the pah1DELTA mutation
D679
-
mutation of the PAP motif, abolishes PAP activity
D679E
-
mutation in lipin-1alpha, does not lead to a diminished sumoylation
G170A
-
38% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
G80R
-
catalytically inactive PAP enzymes with a mutation in a conserved NLIP domain residue fail to complement phenotypes caused by the pah1DELTA mutation
I233T
-
94% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
I706F
-
lacks enzymatic activity, retains the ability to interact with and repress nuclear factor of activated T-cells c4 transcriptional activity
I707F
-
lacks enzymatic activity, retains the ability to interact with and repress nuclear factor of activated T-cells c4 transcriptional activity
I723F
-
lacks enzymatic activity, is unable to interact with nuclear factor of activated T-cells c4 and has no repressive effect on reporter gene activity
IL693FF
-
mutation of the coactivator motif, abolishes PAP activity
K566R/K596R
-
blocks lipin-1alpha sumoylation. In embryonic cortical neurons or SH-SY5Y clones, almost completely loses its nuclear localization compared to wild-type, although its cytoplasmic localization remains unchanged. Retains Mg2+-dependent phosphatase activity for phosphatidic acid (C8), but not for lysophosphatidic acid (C18:1)
K599R/K626R
-
lipin-1beta mutant, is not modified by SUMO-1 in an in vitro sumoylation reaction
L106S
-
85% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
L724F
-
lacks enzymatic activity, is unable to interact with nuclear factor of activated T-cells c4 and has no repressive effect on reporter gene activity
N142Q
-
89% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate, mutation decreases the molecular weight by about 4000 Da
N276Q
-
112% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
S106A
increases electrophoretic mobility of lipin but abolishes the shift in electrophoretic mobility produced by insulin
S731D
-
PAP deficiency, does not result from impaired membrane association. Exhibits normal membrane localization
S731L
-
lipin-2 mutant, protein expression at similar levels as the wild-type, thus lack of PAP activity is not related to reduced protein levels or protein stability. PAP deficiency does not result from impaired membrane association. Shows no reduction in membrane association, in multiple trials exhibits a trend toward increased membrane localization compared with wild-type lipin-2, particularly in the absence of oleate. Shows identical coactivator activity to wild-type lipin-1A and lipin-2
T116I
-
91% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
T122S
-
97% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
T5P
-
85% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
Y168F
-
87% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
Y221W
-
51% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
D679
-
mutation of the PAP motif, abolishes PAP activity
-
IL693FF
-
mutation of the coactivator motif, abolishes PAP activity
-
S731D
-
PAP deficiency, does not result from impaired membrane association. Exhibits normal membrane localization
-
S731L
-
lipin-2 mutant, protein expression at similar levels as the wild-type, thus lack of PAP activity is not related to reduced protein levels or protein stability. PAP deficiency does not result from impaired membrane association. Shows no reduction in membrane association, in multiple trials exhibits a trend toward increased membrane localization compared with wild-type lipin-2, particularly in the absence of oleate. Shows identical coactivator activity to wild-type lipin-1A and lipin-2
-
R217K
-
inactive, mutant shows no decrease of lyso-phosphatidic acid-induced fibroblast migration
S110A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
S110A/S114A/S168A/S602A/T723A/S744A/S748A
-
site-directed mutagenesis, phosphorylation of the mutant is completely abolished
S114A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
S168A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
S168A/S602A/T723A/S744A/S748A
-
site-directed mutagenesis, the mutant shows reduce dphosphorylation
S602A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
S744A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
S748A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
T723A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
W637A
the mutant is not functional in vivo though the mutation does not compromise the PAH1-encoded enzyme activity
W637E
the mutant is not functional in vivo though the mutation does not compromise the PAH1-encoded enzyme activity
W637F
the mutation does not compromise the PAH1-encoded enzyme activity
W637R
the mutant is not functional in vivo though the mutation does not compromise the PAH1-encoded enzyme activity
W637A
-
the mutant is not functional in vivo though the mutation does not compromise the PAH1-encoded enzyme activity
-
W637E
-
the mutant is not functional in vivo though the mutation does not compromise the PAH1-encoded enzyme activity
-
W637F
-
the mutation does not compromise the PAH1-encoded enzyme activity
-
W637R
-
the mutant is not functional in vivo though the mutation does not compromise the PAH1-encoded enzyme activity
-
R214K
-
site-directed mutagenesis
R214K
-
knock-down of endogenous LPP2 in fibroblasts delays cyclin A accumulation and entry into S-phase of the cell cycle. Cells overexpressing LPP2(R214K)-GFP show no significant change in LPP activity
D712E
-
catalytically inactive mutant
D712E
-
lacks enzymatic activity, does not affect the interaction of lipin 1 and PPARalpha, but eliminates the ability of lipin 1 to interact with nuclear factor of activated T-cells c4. Also fails to repress nuclear factor of activated T-cells c4 transcriptional activity
G84R
PAP activity is ca. 20% that of the wild-type enzyme
G84R
site-directed mutagenesis, the mutant shows a 80% reduced activity compared to the wild-type lipin 1
G84R
-
causes lipodystrophy. Mutated residue is a conserved glycine in the N-LIP domain required for enzymatic activity
G84R
-
mutation in lipin-1alpha, does not lead to a diminished sumoylation
H171L
-
2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
H171L
-
site-directed mutagenesis of the C2 domain conserved amino acid residue leads to reduced activity of LPP1
H223L
-
2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
H223L
-
site-directed mutagenesis of the C3 domain conserved amino acid residue leads to reduced activity of LPP1
K120R
-
5% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
K120R
-
site-directed mutagenesis of the C1 domain conserved amino acid residue leads to reduced activity of LPP1
P128I
-
2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
P128I
-
site-directed mutagenesis of the C1 domain conserved amino acid residue leads to reduced activity of LPP1
R127K
-
2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
R127K
-
site-directed mutagenesis of the C1 domain conserved amino acid residue leads to reduced activity of LPP1
R217K
-
2% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
R217K
-
site-directed mutagenesis, inactive mutant
R217K
-
site-directed mutagenesis of the C3 domain conserved amino acid residue leads to reduced activity of LPP1
S169T
-
0.4% of the dephosphorylation activity of the wild-type enzyme with lysophosphatidate as substrate
S169T
-
site-directed mutagenesis of the C2 domain conserved amino acid residue leads to reduced activity of LPP1
D398E
-
inactive
D398E
-
site-directed mutagenesis, the mutant is almost inactive, the activity is independent of the substrate concentration, the mutant shows aberrant regulation of lipid composition
D398E
the mutant shows less than 0.1% compared to wild type enzyme
D400E
-
inactive
D400E
-
site-directed mutagenesis, the mutant is almost inactive, the activity is independent of the substrate concentration, the mutant shows aberrant regulation of lipid composition
D400E
the mutant shows less than 0.1% compared to wild type enzyme
G80R
-
inactive
G80R
-
site-directed mutagenesis, the mutant is almost inactive, the activity is independent of the substrate concentration, the mutant shows aberrant regulation of lipid composition
additional information
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a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
-
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
-
construction of loss-of-function enzyme mutants by transposon mutagenesis, wild-type enzyme overexpression enhances retinal degeneration of the diacylglycerol kinase causing the rdgA phenotype, overview
additional information
introduction of LPP-3 into Drosophila melanogaster germ cells causes aberrant migration and germ cell death
additional information
introduction of LPP-3 into Drosophila melanogaster germ cells causes aberrant migration and germ cell death
additional information
introduction of LPP-3 into Drosophila melanogaster germ cells causes aberrant migration and germ cell death
additional information
introduction of LPP-3 into Drosophila melanogaster germ cells causes aberrant migration and germ cell death
additional information
-
knock-down of LPPs in rat2 fibroblasts, phenotype, overview
additional information
LPR1 variants containing non-conservative substitutions of Ser198 and His200 within the C2 motif and Arg246 from the C3 motif are strongly expressed in transient transfection experiments but fail to induce the formation of filopodia in HeLa cells. In contrast to wild-type LPR1, these mutant LPR1 proteins are exclusively localized to intracellular membranes. LPR1 C-term DELTA43 mutant, is incapable of generating new filopodia, but rather localizes to pre-existing endogenous protrusions extended by these cells. Subcellular distribution of mutant LPR1 C-term DELTA43 between the plasma membrane and intracellular membranes is highly comparable with that of wild-type LPR1
additional information
-
mutations of lipin-1 cause recurrent acute myoglobinuria, lipin-2 mutations are involved in human diseases such as cutaneous inflammation, osteomyelitis and dyserythropoietic anemia
additional information
-
presqualene diphosphate phosphatase, i.e. PA-PSP, overexpression accelerates the synthesis of phosphatidylcholine and causes accumulation of triacylglycerol with concomitant decrease in the rate of phosphatidylinositol synthesis. Co-expression of human CTP:phosphocholine cytidylyltransferase-alpha with PA-PSP enhances the effect of PA-PSP on phosphatidylcholine levels, yet attenuates its effect on triacylglycerol, overview
additional information
mutation of the HVRF binding motif to HARA causes a decrease in binding to serine/threonine protein phosphatase-1 catalytic subunit, blocks nuclear localization and phosphatidate phosphatase activity
additional information
-
construction of LPP3 or LPP1 knockout mice, the embryonic fibroblasts of these transgenic mice show diacylglycerol levels and reduced phosphatidic acid levels
additional information
-
construction of several mouse models overexpressing or lacking LPP isozymes, e.g. overexpression of LPP-1 leads to defects in fertility in female mice and to increased accumulation of diacylglycerol, LPP-2 knockout mice are fertile and viable, whereas LPP-3 knockout mice show a severe phenotype failing to form a chorio-allantoic placenta and yolk sac vasculature, in addition, mutant embryos show a shortening of the anterior-posterior axis, overview, introduction of LPP-1 into Drosophila melanogaster germ cells has no effect on the germ-cell-specific factor in vivo
additional information
-
construction of transgenic mice overexpressing the enzyme, the phenotype includes reduced body size, birth weight, and abnormalities in fur growth, decreased number of hair follicles, disrupted hair structure, and impaired spermatogenesis, phospholipid levels of mutants compared to wild-type mice, overview, ERK1/2 activation is not affected by enzyme overexpression
additional information
-
LPP-1 overexpression mutant shows inhibited cell migration of embryonic fibroblasts by reduction of lysophosphatidic acid- and platelet-derived-growth-factor-induced activation of the p42/p44 MAPK pathway, overview
additional information
-
lipin1-deficient mice show reduce fertility, phenotype, overview
additional information
-
livers of lipin-1-deficient mice exhibit normal PAP1 activity
additional information
-
LPP1 overexpressing fibroblasts show a severe inhibition of LPA-induced migration not mediated through the degradation of extracellular LPA in a woundhealing assay, overview
additional information
removing the COOH-terminal 15 amino acids from lipin does not significantly affect PAP activity, whereas removing an additional 37 amino acids results in a striking reduction in activity. Deleting the entire CLIP domain by COOH-terminal truncation abolishes PAP activity. Deleting the NLIP domain dramatically decreases PAP activity
additional information
the activity of the lipin protein, in which the catalytic Asp in the HAD domain is mutated to Glu, is negligible, lipin 1-deficient fld/fld mice contain much less Mg2+-dependent phosphatidic acid phosphatase activity than tissues from wild type mice, fld phenotype, overview
additional information
-
gene Lpin1 is the mutated gene in the fatty liver dystrophy, fld, in mouse. The phenotypes associated with the pah1DELTA mutation, which also include slow growth, temperature sensitivity, and respiratory deficiency are specifically due to the loss of PAP activity. In addition, mice lacking lipin 1 exhibit peripheral neuropathy that is characterized by myelin degradation, Schwann cell dedifferentiation and proliferation, and a reduction in nerve conduction velocity, These effects are mediated through the MEK/ERK pathway that is activated by elevated levels of PA due to the loss of PAP activity
additional information
-
lipin-1-deficient fld mice show that lipin-1 accounts for all of the PAP1 activity in adipose tissue and skeletal muscle, targeted expression of lipin-1 in adipose tissue of transgenic mice leads to obesity, overview
additional information
-
livers of fld mice lacking lipin 1 exhibit normal PAP-1 activity and a 20fold increase in triglyceride levels, while the hepatic content of phosphatidate is markedly diminished in fld mice. Other phospholipids derived from phosphatidate, phosphatidylglycerol and cardiolipin, are also depleted. Hepatic lipin 2 protein content is markedly increased by lipin 1 deficiency via a posttranscriptional mechanism
additional information
-
overexpression of LIPIN1 disturbs hepatic insulin signaling, knockdown of LIPIN1 ameliorates hyperglycemia and insulin resistance by reducing diacylglycerol and PKC3 activity in db/db mice. TORC2-mediated insulin resistance is partially rescued by concomitant knockdown of LIPIN1, overview
additional information
-
PAP-1 inhibition leads to the loss of cyclooxygenase 2 expression and PGE2 release
additional information
-
mutant lipin-1alpha lacking the serine-rich domain, is excluded from the nucleus
additional information
-
mutation of IL728FF does not affect the interaction with peroxisome proliferator-activated receptor gamma2
additional information
-
lipin-1 siRNA treatment of cells reduces the expression level of lipin-1, overview
additional information
-
construction of a PAH1 mutant with reduced enzyme activity, the mutant grows more slowly and is temperature-sensitive at 37°C, mutant cells show increased phosphatidate levels compared to the wild-type cells, overview
additional information
-
a pah1DELTA deletion mutant shows a phenotype of temperature sensitivity, respiratory deficiency, nuclear/endoplasmic reticulum membrane expansion, derepression of INO1 expression, and alterations in lipid composition
additional information
-
pah1? mutants show a temperature sensitivity phenotype
additional information
-
generation of a pah1DELTA mutant, phenotype, overview
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cloning of two Mg2+-independent isoenzymes, PAP-2a and PAP-2b
-
co-overexpression of lipin with murine LPP-1 in Escherichia coli strain BL21(DE3) as His-tagged enzymes
-
coding sequence of lipin 1b subcloned downstream of the GST tag in the pEBG expression vector, transfected into 293T cells. Adenoviral constructs for HA-tagged lipin 1b
-
expressed as untagged proteins in HUVEC cells or in HEK-293 cells
-
expressed either as untagged proteins or as Flag- or EGFP-tagged enzymes in HUVEC cells or in HEK-293 cells
-
expressed in Escherichia coli BL21-(DE3) cells
-
expressed in HEK293 cells as a green fluorescent fusion protein
-
expressed in P-388D1 cells
-
expression analysis of lipin-1 and lipin-2, recombinant expression of lipin-2 in Hep-G2 cells using an adenoviral vector
-
expression in Escherichia coli
expression in HEK-293 cell
expression of hemagglutinin epitope-tagged phosphatidic acid phosphohydrolase PAP-2a, PAP-2b and PAP-2c in HEK293 cells. Expression of phosphatidic acid phosphohydrolase PAP-2a, PAP-2b and PAP-2c in baculovirus-infected Sf9 insect cells. Expression of PAP-2a but not PAP-2b or PAP-2c results in high levels of cell surface PAP activity in intact insect cells
-
expression of His6-tagged EtLPP1 in HEK293 cells produces immunoreactive proteins with variable molecular sizes, suggesting the presence of multiple forms of enzyme
expression of isozyme DPPL1 in Spodoptera frugiperda Sf9 cells
expression of isozyme DPPL2 in Spodoptera frugiperda Sf9 cells
expression of lipin-1 in HeLa M cells
expression of lipin-1, lipin-2, and lipin-3 in HEK-293 cells
-
expression of lipin-2 in HeLa M cells
-
expression of lipins 1-3 in HEK-293 cells
-
expression of LPP1 in Drosophila melanogaster cells S2
-
expression of Myc-tagged and/or FLAG-tagged LPP1, LLP2, and LLP3 in HEK-293 cells, overview
-
expression of PAP2a in Saos-2 cells, promoter determination and anaylsis, expression in HEK-293T cells, expression regulation anaylsis, overview
-
expression of presqualene diphosphate phosphatase in COS-7 cells, co-expression with CTP:phosphocholine cytidylyltransferase-alpha
-
expression of the gene encoding the enzyme under control of chicken beta-actin promoter in mice embryos
-
expression of wild-type and mutant enzymes in rat2 fibroblasts
-
full-length cDNAs for human lipin-1 transferred to the pCMV/V5-DEST vector. Plasmid DNA transformed and amplified using DH5alpha bacteria, and transfection of L6 myocytes
-
full-length coding sequence of PAH1 and PAH2 cloned into the pDO105 vector at NotI/MluI sites for PAH1 and NotI/PstI sites for PAH2. Vector constructs introduced into a Saccharomyces cerevisiae DELTAdpp1DELTAlpp1DELTApah1 mutant. Transgenic pah1pah2 plants that harbor either 35S::PAH1-GFP or 35S::PAH2-GFP transgenes
-
full-length lipin1beta cDNA amplified and cloned into the pcDNA3.1-V5/His-TOPO expression vector and pSG5-FLAG-tagged expression vector. Peroxisome proliferator-activated receptor gamma2 and lipin1 overexpressed in NIH3T3 cells
-
full-length of the cDNA of lipin1
full-length triple HA-tagged lipin 2 cloned into pCDNA3 expression construct, subcloned into the Ad-track cytomegalovirus vector, and recombined into the Ad-EASY system. Full-length cDNA for lipin 3 from pSPORT-lipin 3 expression vector
-
functional overexpression of GFP-tagged LPPs in rat2 fibroblasts, the transformed cells show reduced proliferation, overview
-
gene DPP1, functional overexpression of HA-tagged enzyme in the DPP1-deficient mutant Saccharomyces cerevisiae strain DTY1 in vacuole membranes, the transcription factor Zap1p binds the DPP1 promoter and induces the expression of DGPP phosphatase
-
gene laza, genetic structure and organiszation, expression analysis and pathway regulation, overview
-
gene LPIN2 is located on chromosome 18p11
-
gene Lpp1, stable overexpression of wild-type and mutant LPP1 enzymes in Rat2 fibroblasts using a retroviral vector and puromycin selection
-
gene PAH1, expression in Escherichia coli
-
gene PAH1, overexpression of His-tagged wild-type and mutant isozyme PAH1 in Escherichia coli strain BL21(DE3), co-expression with human lipin, subcloning in Escherichia coli strain DH5alpha
-
genes Lpin1, Lpin2, and Lpin3, expression analysis reveals distinct gene regulation in the hepatocytes
genes VuPAPalpha and VuPAPbeta, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of VuPAPalpha in Escherichia coli
-
genomic library screening, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His6-tagged PAP2L2 in Escherichia coli
HA-tagged forms of wild-type and mutant lipin proteins overexpressed in HEK-293 cells. Expression of HA-lipin in 3T3-L1 adipocytes by adenoviral mediated gene transfer
HEK293 cells or 3T3-L1 adipocytes transfected with wild-type or mutant lipin-1alpha lacking the serine-rich domain
-
isozyme LPPbeta, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree
isozyme LPPepsilon1, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree, functional complementation of a PAP-deficient yeast DELTAdpp1DELTAlpp1DELTApah1 by the plastidic LPP, phenotype rescue in vivo and in vitro, overview, expression of the isozyme in transgenic Arabidopsis thaliana plants using Agrobacterium tumefaciens-mediated transformation
isozyme LPPepsilon2, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree, functional complementation of a PAP-deficient yeast DELTAdpp1DELTAlpp1DELTApah1 by the plastidic LPP, phenotype rescue in vivo and in vitro, overview, expression of the isozyme in transgenic ARabidopsis thaliana plants using Agrobacterium tumefaciens-mediated transformation
isozyme LPPgamma, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree, functional complementation of a PAP-deficient yeast DELTAdpp1DELTAlpp1DELTApah1 by the plastidic LPP, phenotype rescue in vivo and in vitro, overview, expression of isozyme LPPgamma in transgenic Arabidopsis thaliana plants using Agrobacterium tumefaciens-mediated transformation
isozymes LPPdelta, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree
lipin-1 adenovirus overexpression
-
lpin-1 coding sequences (with introns) and 3' UTR sequences amplified and recombined into pDONR P1P3. Final product pAG-107 reacted with pCR319 (contains the unc-119(+) gene for transformation rescue of unc-119(ed3) mutants) and pAG-108 (including the lpin-1 promoter) to produce pAG-126
-
LPIN1 reporter plasmid transiently transfected into Hep-G2 cells
-
LPP1 and LPR1 expressed in Sf9 cells using a baculovirus vector. Recombinant LPR1 and mutants incorporating a C-terminal EGFP tag expressed in HeLa and COS7 cells. Overexpression of EGFP-LPR1 in SK-OV-3 cells
LPP1 wild-type or mutants inserted into vector pcDNA3.1 with a C-terminal Myc epitope tag or FLAG epitope tag. HEK-293 cells transfected with plasmid construct encoding catalytically deficient Myc-tagged R127K LPP1 and/or FLAG-tagged H223L LPP1 and/or FLAG-tagged and/or Myc-tagged wild-type
-
LPP2 and LPP3 inserted into vector pcDNA3.1 with a C-terminal Myc epitope tag or FLAG epitope tag and transiently transfected into HEK-293 cells
-
NIH3T3 cells stably expressing LPP1-CFP or LPP3-CFP. MDCK cells stably expressing LPP1-GFP and LPP3-GFP. COS-7 and PC-12 cells transiently expressing LPP1
-
overexpression in HEK-293 cells
-
overexpression in Sf-9 insect cells
-
overexpression in Spodoptera frugiperda Sf9 cells using the baculovirus expression system, and in Saccharomyces cerevisiae using multicopy plasmids
-
overexpression of isozyme LPP1 in Rat2 fibroblasts
-
overexpression of LPP-3 in HEK293 cells and in Xenopus laevis dorsal blastomeres of embryos causing a mild ventralizing effect
overexpression of LPP3 and LPP2 in HEK-293 cells, LPP2 and LPP3 are constitutively co-localized with sphingosine kinase 1, SK1, in cytoplasmic vesicles in HEK-293 cells, LPP2, not LPP3, prevents SK1 from being recruited to the perinuclear space upon induction of phospholipase D1
-
overexpression of LPPs in HEK293 cells, expression of LPP3 in Drosophila melanogaster cells S2
-
rat2 fibroblasts infected with adenoviral vectors containing LPP1-myc or LPP1(R217K)-myc. Rat2 fibroblasts stably overexpressing LPP1
-
rat2 fibroblasts transduced and overexpressed with LPP1 and mLPP1-GFP
-
rat2 fibroblasts transduced and overexpressed with LPP2, LPP2-GFP and mutant LPP2(R214K)-GFP
-
rat2 fibroblasts transduced and overexpressed with LPP3-GFP or myc-LPP3
-
separate overexpression of isozymes LPP1, LPP2, or LPP3 in HEK-293 cells reducing lysophosphatidic acid-stimulated p42/p44 MAPK activation
-
subcloning and expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha and BL21(DE3)
-
transcript PAP2d_v1, cDNA library construction, DNA and amino acid sequence determination and analysis, genomic localization of the two splicing variants, expression patterns, expression in Escherichia coli strain DH5alpha
transcript PAP2d_v2, cDNA library construction, DNA and amino acid sequence determination and analysis, genomic localization of the two splicing variants, expression patterns, expression in Escherichia coli strain DH5alpha
transient and stable overexpression in HEK-293 cells, baculovirus vectors for recombinant expression of LPPs in cultured Sf9 cells
-
transient expression of lipin-1 in McA-RH7777 cells specifically influences the rate of incorporation of methionine into apolipoprotein B100, and stimulates its synthesis and secretion, overview
-
V5 epitope-tagged lipin-1 and lipin-2 expression plasmids, transiently transfected into Hepa 16 cells. Wild-type lipin-1A and lipin-2 and mutants lipin-1A-S724L and lipin-2-S731L expressed in HEK-293 cells
-
V5-tagged lipin-1alpha, lipin-1beta, lipin-2 and lipin-3 expression vectors. HEK-293A cells transfected with plasmids expressing V5-tagged proteins. HeLa cells transfected with expression plasmids for V5-lipin-1beta and CFP-SUMO-1 or their mutants. SH-SY5Y cells stably expressing pcDNA3, lipin-1alpha-V5 or lipin-1alpha-K566R/K596R-V5. Cerebrocortical neurons from embryonic day 17 rat embryos transfected either with V5-tagged lipin-1alpha or lipin-1beta, or with the corresponding double sumoylation site mutants
-
wild-type and mutant LPP1, LPP2, and LPP3 cDNAs subcloned into the pLNCX2 retroviral vector directly downstream of the human cytomegalovirus immediate-early promoter. Constructs transfected inot human dermal microvascular endothelial cells. HA-tagged wild-type LPP3 (pLNCX2-HA-WT-hLPP3) stably transfected into HEK-293 cells
-
wild-type transfected inot human dermal microvascular endothelial cells
-
expression in Escherichia coli
expression in Escherichia coli
genes Lpin1, Lpin2, and Lpin3, expression analysis reveals distinct gene regulation in the hepatocytes
-
genes Lpin1, Lpin2, and Lpin3, expression analysis reveals distinct gene regulation in the hepatocytes
-
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