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Information on EC 3.1.3.106 - 2-lysophosphatidate phosphatase
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EC Tree
3.1.3.106 2-lysophosphatidate phosphataseIUBMB Comments
The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae. The enzyme from yeast, but not from the plants, requires Mg2+.
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Word Map
- 3.1.3.106
- phosphatases
- monoacylglycerol
- phospholipid
- acyltransferases
-
circadian
- glycerophospholipid
-
littermates
- diacylglycerol
-
rhythms
-
lplats
-
oscillate
- lysophospholipid
- phosphatidylcholine
-
kennedy
- propranolol
- n-ethylmaleimide
- choline
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lpa phosphatase, phosphatidate phosphohydrolase 1, at3g03520, lysophosphatidic acid phosphatase type 6, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-acyl-sn-glycerol 3-phosphatase
-
-
-
-
Acp6
CPC3
-
-
-
-
lipid phosphate phosphatase
lipin
lipin-1
lipin-3
LPA phosphatase
LPP
lysophosphatidic acid phosphatase
PAP1
Phm8
phosphatidate phosphohydrolase 1
Phm8
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 1-acyl-sn-glycerol 3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
1-acyl-sn-glycerol 3-phosphate phosphohydrolase
The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae. The enzyme from yeast, but not from the plants, requires Mg2+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoyl-sn-glycerol + phosphate
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phosphate + H2O
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycerol + phosphate
1-lauroyl-2-lysophosphatidate + H2O
1-lauroyl-sn-glycerol + phosphate
-
-
-
-
?
1-myristoyl-2-lysophosphatidate + H2O
1-myristoyl-sn-glycerol + phosphate
-
-
-
-
?
1-myristoyl-sn-glycerol 3-phosphate + H2O
1-myristoylglycerol + phosphate
-
-
-
?
1-oleoyl-2-lysophosphatidate + H2O
oleic acid + sn-glycerol 3-phosphate
-
-
-
-
?
1-palmitoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-palmitoyl-sn-glycerol + phosphate
-
-
-
-
?
1-palmitoyl-2-lysophosphatidate + H2O
1-palmitoyl-sn-glycerol + phosphate
-
-
-
-
?
1-stearoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-stearoyl-sn-glycerol + phosphate
-
-
-
-
?
1-stearoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-stearoylglycerol + phosphate
-
-
-
?
1-stearoyl-2-lysophosphatidate + H2O
1-stearoyl-sn-glycerol + phosphate
-
-
-
-
?
myristoyl-sn-glycerol3-phosphate + H2O
myristoyl-sn-glycerol + phosphate
best substrate
-
-
?
stearoyl-sn-glycerol 3-phosphate + H2O
stearoyl-sn-glycerol + phosphate
-
-
-
-
?
stearoyl-sn-glycerol-3-phosphate + H2O
stearoyl-sn-glycerol + phosphate
-
-
-
?
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoyl-sn-glycerol + phosphate
-
-
-
-
?
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoyl-sn-glycerol + phosphate
-
-
-
?
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phosphate + H2O
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycerol + phosphate
-
-
-
-
?
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phosphate + H2O
1-hexanoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycerol + phosphate
-
-
-
-
?
1-oleoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
-
?
1-oleoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
?
1-oleoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
-
?
1-oleoyl-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
?
1-oleoyl-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
-
best substrate
-
-
?
oleoyl-sn-glycerol 3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
-
-
-
-
?
oleoyl-sn-glycerol 3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
about 2fold the activity of stearoyl-sn-glycerol 3-phosphate
-
-
?
oleoyl-sn-glycerol-3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
-
-
-
-
?
oleoyl-sn-glycerol-3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
-
-
-
-
?
palmitoyl-sn-glycerol 3-phosphate + H2O
palmitoyl-sn-glycerol + phosphate
-
-
-
-
?
palmitoyl-sn-glycerol 3-phosphate + H2O
palmitoyl-sn-glycerol + phosphate
-
-
-
?
additional information
?
-
-
the purified recombinant enzyme does not hydrolyze sphingosine 1-phosphate, diacylglycerol diphosphate, glycerol-3-phosphate, lysophosphatidylcholine, lysophosphatidylethanolamine and phosphatidate
-
-
?
additional information
?
-
-
the enzyme is specific to lysophosphatidic acid and does not utilize any other substrate such as glycerol-3-phosphate, phosphatidic acid, or p-nitrophenylphosphate
-
-
?
additional information
?
-
no substrates: cardiolipin, tetraoleoylbisphosphatidic acid, ceramide 1-phosphate or sphingosine 1-phosphate. The enzyme shows a slight activity towards phosphatidic acid (dioleolyl) and p-nitrophenyl phosphate in the neutral pH range around 7.5 and in the acidic pH range around 5.5, respectively
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells
-
-
?
additional information
?
-
-
no substrates: dipalmitoyl phosphatidic acid, distearoyl phosphatidic acid
-
-
?
additional information
?
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
no substrate: phosphatidylglycerol phosphate
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in epithelial cells
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-oleoyl-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
-
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
-
best substrate
-
-
?
myristoyl-sn-glycerol3-phosphate + H2O
myristoyl-sn-glycerol + phosphate
best substrate
-
-
?
stearoyl-sn-glycerol 3-phosphate + H2O
stearoyl-sn-glycerol + phosphate
-
-
-
-
?
stearoyl-sn-glycerol-3-phosphate + H2O
stearoyl-sn-glycerol + phosphate
-
-
-
?
oleoyl-sn-glycerol 3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
-
-
-
-
?
oleoyl-sn-glycerol 3-phosphate + H2O
oleoyl-sn-glycerol + phosphate
about 2fold the activity of stearoyl-sn-glycerol 3-phosphate
-
-
?
palmitoyl-sn-glycerol 3-phosphate + H2O
palmitoyl-sn-glycerol + phosphate
-
-
-
-
?
palmitoyl-sn-glycerol 3-phosphate + H2O
palmitoyl-sn-glycerol + phosphate
-
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in human bronchial epithelial cells
-
-
?
additional information
?
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
-
no substrate: glycerol 3-phosphate. Activity increases with the length of acyl chain to a peak value on 14:0-lysophosphatidic acid. Activity gradually decreases, when the substrate length is increased above the optimal 14:0-lysophosphatidic acid
-
-
?
additional information
?
-
-
LPP is involved in regulation of bioactive lipids acting in signalling pathways, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in epithelial cells
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
-
in absence of Mg2+ activity towards 1-stearoyl-2-lyso-sn-glycerol 3-phosphate acid is significantly decreased
additional information
-
cations like Mg2+, Mn2+, and Ca2+ have no effect on the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme activity is insensitive to non-specific phosphatase inhibitors such as sodium o-vanadate and sodium fluoride
-
additional information
-
not inhibitory: 1-palmitoyl-sn-glycerol, 1-hexadecanol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CHAPS
activity is completely dependent on the presence of detergents such as Triton X-100, CHAPS, cholate and octyl-beta-glucoside
cholate
activity is completely dependent on the presence of detergents such as Triton X-100, CHAPS, cholate and octyl-beta-glucoside
Insulin
-
insulin therapy increases both PAP1 activity and lipin mRNA expression in diabetic patients
-
octylgucoside
activity is completely dependent on the presence of detergents such as Triton X-100, CHAPS, cholate and octyl-beta-glucoside
additional information
-
incubation with phospholipids or neutral lipids has no effect on the enzyme activity
-
Triton X-100
activity is completely dependent on the presence of detergents such as Triton X-100, CHAPS, cholate and octyl-beta-glucoside
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Diabetes Mellitus
Suppression of cardiac phosphatidate phosphohydrolase 1 activity and lipin mRNA expression in Zucker diabetic fatty rats and humans with type 2 diabetes mellitus.
Diabetes Mellitus, Type 2
Suppression of cardiac phosphatidate phosphohydrolase 1 activity and lipin mRNA expression in Zucker diabetic fatty rats and humans with type 2 diabetes mellitus.
Ovarian Neoplasms
A gonadotropin-releasing hormone-responsive phosphatase hydrolyses lysophosphatidic acid within the plasma membrane of ovarian cancer cells.
Starvation
Functional characterization of lysophosphatidic acid phosphatase from Arabidopsis thaliana.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0286
oleoyl-sn-glycerol 3-phosphate
-
pH 7.0, 30°C, presence of Triton X-100
0.0479
palmitoyl-sn-glycerol 3-phosphate
-
pH 7.0, 30°C, presence of Triton X-100
0.0393
stearoyl-sn-glycerol 3-phosphate
-
pH 7.0, 30°C, presence of Triton X-100
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.1
substrate oleoyl-sn-glycerol 3-phosphate, in Triton X-100 mixed micelles, pH 7.5, 37°C
858
-
substrate oleoyl-sn-glycerol 3-phosphate, pH 7.0, 30°C, presence of Triton X-100
additional information
additional information
-
recombinant activity of wild-type and mutant enzymes in transformed cells
additional information
-
recombinant activity of wild-type and mutant enzymes in transformed cells
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
presence of lipin-1 and lipin-3, lipin-2 is absent. Marked differences in cardiac distribution of PAP1
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the active site of the enzyme is on the outer surface of plasma membranes, or the lumenal surface of internal membranes
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function