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Information on EC 3.1.3.4 - phosphatidate phosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32567
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3.1.3.4 phosphatidate phosphataseIUBMB Comments
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
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Word Map
- 3.1.3.4
- phospholipid
- triacylglycerols
- phospholipase
-
lipins
- phosphatidylcholine
- triglyceride
- propranolol
- adipose
-
lysophosphatidic
- glycerolipids
- acyltransferase
- adipocyte
-
lipogenesis
-
lipogenic
- sphingosine
- pkc
- steatosis
- lipodystrophy
- rhabdomyolysis
- cytidylyltransferase
-
mg2+-independent
- sphingosine-1-phosphate
- phosphatidylethanol
-
diradylglycerol
-
bromoenol
-
transphosphatidylation
-
kennedy
- cdp-diacylglycerol
- sn-glycerol
-
argonaut
- 1,2-diacylglycerol
-
sphingoid
-
srebf1
-
dgats
-
pirnas
- glycerolphosphate
- pc-plc
-
plectonema
-
ctp:phosphocholine
-
plasticity-related
- acaca
-
prophenoloxidase
-
cholinephosphotransferase
-
phosphatidylcholine-specific
- sn-glycerol-3-phosphate
- medicine
- analysis
- drug development
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phosphatidate phosphohydrolase, lipin-1, lpin1, pap-1, lipin1, phosphatidate phosphatase, lipin 1, prg-1, phosphatidic acid phosphohydrolase, pa phosphatase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-sn-phosphatidate phosphohydrolase
-
-
acid phosphatidyl phosphatase
-
-
-
-
ecto-PAPase
-
-
-
-
ecto-phosphatidic acid phosphohydrolase
-
-
-
-
Germ cell guidance factor
-
-
-
-
PA phosphatase
PAP
phosphatidate phosphohydrolase
-
-
-
-
phosphatidic acid phosphatase
phosphatidic acid phosphohydrolase
-
-
-
-
SMP2
Wunen protein
-
-
-
-
additional information
PA phosphatase
-
-
-
-
PA phosphatase
-
-
PAP
-
-
-
-
phosphatidic acid phosphatase
-
-
-
-
additional information
-
cf. EC 3.1.3.B2, the enzyme is a member of the lipid phosphate phosphatase superfamily
additional information
-
the enzyme belongs to the DXDX(T/V) phosphatase family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
catalytic site structure within the transverse plane of the vacuole membrane, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
diacylglycerol-3-phosphate phosphohydrolase
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
CAS REGISTRY NUMBER
COMMENTARY
9025-77-8
-
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-acyl-sn-glycerol 3-phosphate + H2O
1-acyl-sn-glycerol + phosphate
-
less than 15% of the activity with phosphatidic acid
-
-
?
dicaproyl phosphatidate + H2O
1,2-dicaproyl-sn-glycerol + phosphate
-
best substrate of the 104-kDa enzyme form
-
-
?
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 phosphatidate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
-
?
dipalmitoyl phosphatidate + H2O
1,2-dipalmitoyl-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
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
-
-
?
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
-
-
?
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
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
-
-
?
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-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
-
-
?
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
?
-
-
the enzyme is homologous to mammalian lipin
-
-
?
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 contains the DXDX(T/V) active site motif
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme also shows diacylglycerol lipase activity, EC 3.1.1.34, overview
-
-
?
additional information
?
-
-
the LPP1-encoded enzyme has broad substrate specificity
-
-
?
additional information
?
-
-
lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators to modulate gene expression in lipid metabolism
-
-
?
additional information
?
-
-
PAP1 activity is conferred by the DxDxT motif of the C-Lip domain contained in all lipin family members
-
-
?
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
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
-
-
?
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
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
-
-
?
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
-
-
?
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
-
-
?
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
-
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
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
Mg2+
-
dependent on
Mg2+
-
required for the 45000 Da enzyme form, maximal activity at 1 mM
Mg2+
-
two membrane-associated forms, 45000 Da and 104000 Da, of the Mg2+-dependent phosphatidate phosphatase
additional information
-
Lpp1p contains ten cysteine residues, whereas Dpp1p and Pah1p contain only three
additional information
-
the enzyme is Mg2+-independent and shows no divalent cation requirement for activity
additional information
-
enzyme forms Dpp1 and Lpp1 are independent from Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DMSO
-
addition to the reaction mixture results in a dose-dependent inhibition of PAP1 activity, 25% loss of PAP1 activity at a 1% concentration
Mg2+
-
inhibition of reaction with diacylglycerol diphosphate. Little effect on reaction with lysophosphatidic acid and phosphatidic acid
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
propanolol
-
inhibition of the 45000 Da enzyme form and the 104000 Da enzyme form
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
Ca2+
-
IC50: 15 mM, reaction with phosphatidic acid. IC50: 7.1 mM, reaction with diacylglycerol diphosphate. IC50: 8.2 mM, reaction with lysophosphatidic acid
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
-
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 diphosphate
-
competitive with respect to 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
-
inhibition of the 45-kDa and 104-kDa enzyme forms
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
-
the yeast DPP1-encoded PAP2 activity is insensitive to NEM, whereas LPP1-encoded PAP2 activity is sensitive to NEM
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 with respect to diacylglycerol diphosphate
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
Zn2+
-
PAP2 activity is also inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
Zn2+
-
zinc depletion increases the enzyme activity in vivo, stress condition of zinc depletion induces DPP1 expression
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cardiolipin
-
PAH1-encoded PAP activity is enhanced by the phospholipids CDP-diacylglycerol, phosphatidylinositol, and cardiolipin
CDP-diacylglycerol
-
PAH1-encoded PAP activity is enhanced by the phospholipids CDP-diacylglycerol, phosphatidylinositol, and cardiolipin
phosphatidylinositol
-
PAH1-encoded PAP activity is enhanced by the phospholipids CDP-diacylglycerol, phosphatidylinositol, and cardiolipin
Triton X-100
-
the 45000 Da enzyme form shows maximal activity at 5 mM
Triton X-100
-
the 45-kDa and 104-kDa enzyme forms are dependent on Triton X-100 for activity
Triton X-100
-
activates by forming a mixed micelle with the lipid substrate PA, providing a membrane mimic for catalysis
additional information
-
expression of the DPP1 gene, which encodes DGPP phosphatase, is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase, induction by zinc depletion is mediated by the transcription factor Zap1p, which binds to a zinc-responsive element in the DPP1 promoter
-
additional information
-
the transcription factor Zap1p binds the DPP1 promoter and induces the expression of DGPP phosphatase, stress condition of zinc depletion induces DPP1 expression
-
additional information
-
dephosphorylation of lipin Pah1p by the Nem1p-Spo7p complex enables the amphipathic helix to anchor Pah1p onto the nuclear/endoplasmic reticulum membrane allowing the production of diacylglycerol for lipid biosynthesis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
phosphatidic acid
-
wild type enzyme, pH and temperature not specified in the publication
additional information
additional information
-
Km-value for phosphatidic acid: 0.05 mol%, Km-value for diacylglycerol diphosphate: 0.07 mol%, KM-value for lysophosphatidate : 0.08 mol%
-
additional information
additional information
-
steady-state kinetics, recombinant wild-type and mutant PAH1, overview
-
additional information
additional information
-
kinetic analysis, PA phosphatase activity on phosphatidate is cooperative
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki-value for phosphatidic acid competitive with respect to diacylglycerol diphosphate : 0.12 mol%. Ki-value for diacylglycerol diphosphate competitive with respect to phosphatidic acid: 0.12 mol%
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.2
Ca2+
Saccharomyces cerevisiae
-
IC50: 15 mM, reaction with phosphatidic acid. IC50: 7.1 mM, reaction with diacylglycerol diphosphate. IC50: 8.2 mM, reaction with lysophosphatidic acid
1.2
Co2+
Saccharomyces cerevisiae
-
IC50: 0.029 mM, reaction with phosphatidic acid. IC50: 1.1 mM, reaction with diacylglycerol diphosphate. IC50: 1.2 mM, reaction with lysophosphatidic acid
0.091
Mn2+
Saccharomyces cerevisiae
-
IC50: 0.066 mM, reaction with phosphatidic acid. IC50: 0.01 mM, reaction with diacylglycerol diphosphate. IC50: 0.091 mM, reaction with lysophosphatidic acid
0.17
NEM
Saccharomyces cerevisiae
-
IC50: 0.23 mM, reaction with phosphatidic acid. IC50: 0.12 mM, reaction with diacylglycerol diphosphate. IC50: 0.17 mM, reaction with lysophosphatidic acid
1.3
Phenylglyoxal
Saccharomyces cerevisiae
-
at 30°C, in 50 mM Tris-HCl buffer, pH 7.5, 1 mM MgCl2, and 0.2 mM substrate
2.5
Phenylglyoxal
Saccharomyces cerevisiae
-
IC50: 7 mM, reaction with phosphatidic acid. IC50: 3.4 mM, reaction with diacylglycerol diphosphate. IC50: 2.5 mM, reaction with lysophosphatidic acid
0.2
propranolol
Saccharomyces cerevisiae
-
at 30°C, in 50 mM Tris-HCl buffer, pH 7.5, 1 mM MgCl2, and 0.2 mM substrate
7.17
propranolol
Saccharomyces cerevisiae
-
IC50: 2.51 mM, reaction with phosphatidic acid. IC50: 1.68 mM, reaction with diacylglycerol diphosphate. IC50: 7.17 mM, reaction with lysophosphatidic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
-
recombinant vacuole membranes of intact vacuoles from overexpressing transgenic mutant DTY1
7
-
recombinant vacuole membranes of Triton X-100-ruptured vacuoles from overexpressing transgenic mutant DTY1
additional information
-
recombinant wild-type and mutant PAH1, assay in presence of Triton X-100 at 2 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
pH 5.0: about 40% of maximal activity, pH 8.0: about 40% of maximal activity, reaction with lysophosphatidic acid
5.5 - 8
-
pH 5.0: about 45% of maximal activity, pH 8.0: about 35% of maximal activity, reaction with diacylglycerol diphosphate
5.5 - 9
-
pH 5.0: about 55% of maximal activity, pH 9.0: about 80% of maximal activity, reaction with phosphatidic acid
7 - 9
-
pH 7.0: 83% of maximal activity, pH 9.0: about 36% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
translocates onto the cytosolic side of intracellular membranes
-
associated, the enzyme contains six putative transmembrane domains, the catalytic site is oriented to the cytosolic face of the vacuole membrane
-
-
-
two membrane-associated forms, 45000 Da and 104000 Da, of the Mg2+-dependent phosphatidate phosphatase
-
lipid phosphate phosphatase enzymes possess a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
-
recruitment of the yeast lipin (Pah1p) is regulated by PA levels onto the nuclear/endoplasmic reticulum membrane. Recruitment requires the transmembrane protein phosphatase complex Nem1p-Spo7p
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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
malfunction
metabolism
physiological function
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
the enzyme plays a major role in controlling the utilization of phosphatidate for the synthesis of triacylglycerol or membrane phospholipids
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
-
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
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
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
-
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
104000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
124000
-
1 * 95000, about, PAH1, sequence calculation, 1 * 124000, PAH1, SDS-PAGE
45000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
75000
91000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
95000
-
1 * 95000, about, PAH1, sequence calculation, 1 * 124000, PAH1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
monomer
additional information
monomer
-
1 * 95000, about, PAH1, sequence calculation, 1 * 124000, PAH1, SDS-PAGE
additional information
-
lipid phosphate phosphatase enzymes possess a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane, the conserved arginine residue in domain 1 and the conserved histidine residues in domains 2 and 3 are essential for catalytic activity
additional information
-
lipin contains the DXDX(T/V) active site motif
additional information
-
PAP1 contains the catalytic motif DIDGT at residues 398402 and a conserved Gly80 residue
additional information
-
PAP1 enzyme has a DxDxT catalytic motif within a haloacid dehalogenase- like domain, the DPP1-and LPP1-encoded PAP2 enzymes contain a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
additional information
-
the enzyme has six putative transmembrane domains and a hydrophilic region that contains a phosphatase motif required for its catalytic activity, membrane topology, overview
additional information
-
yeast PAH1 protein sequence contains a haloacid dehalogenase domain, which includes a DXDXT motif found in a superfamily of Mg2+-dependent phosphatases
additional information
-
PAP1 activity is conferred by the DxDxT motif of the C-Lip domain contained in all lipin family members
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
proteolytic modification
-
the 91-kDa enzyme is a proteolysis product of a 104-kDa enzyme form, the 104-kDa PA phosphatase is not a precursor of the 45-kDa enzyme form
phosphoprotein
phosphorylation at sites Ser110, Ser114, Ser168, Ser602, Thr723, Ser744, and Ser748 is managed by protein kinase-cyclin complex Pho85p-Pho80p. The phosphorylation of recombinant isoform Pah1p is time- and dose-dependent and dependent on the concentrations of ATP and Pah1p. Phosphorylation reduces the catalytic efficiency 6fold and reduces 3fold its interaction with liposomes. Alanine mutations of the seven sites ablates the inhibitory effect of phosphorylation. Loss of Pho85p-Pho80p phosphorylation reduces Pah1p abundance. Lack of Nem1p-Spo7p, the phosphatase complex that dephosphorylates Pah1p at the nuclear/endoplasmic reticulum membrane, stabilizes Pah1p abundance
phosphoprotein
residues Ser677, Ser769, Ser773, and Ser788 are major sites of phosphorylation by protein kinase C. Prephosphorylation with protein kinase C reduces Pah1p subsequent phosphorylation with protein kinase A and vice versa. Prephosphorylation with kinase Pho85p-Pho80p has an inhibitory effect on its subsequent phosphorylation with protein kinase C. Prephosphorylation with protein kinase C has no effect on the subsequent phosphorylation with Pho85p-Pho80p
phosphoprotein
-
lipin is phosphorylated by human Dullard, a protein that participates in a unique phosphatase cascade regulating nuclear membrane biogenesis, and this cascade is conserved from yeast to mammals
phosphoprotein
-
Pah1p is phosphorylated in vivo, phosphorylation is required for the efficient transcriptional derepression of key enzymes involved in phospholipid biosynthesis, the phosphorylation-deficient Pah1p exhibits higher phosphatidic acid phosphatase-specific activity than the wild-type Pah1p, indicating that phosphorylation of Pah1p at residues S110, S114, S168, S602, T723, S744, and S748 controls phosphatidic production
phosphoprotein
-
the 45-kDa PA phosphatase is phosphorylated by protein kinase A, while the purified 104-kDa PA phosphatase is not a substrate, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction
phosphoprotein
-
PAP PAH1 is a target for multiplec protein kinases, including cyclin-dependent kinase Cdk1, Pho85, and Dbf2-Mob1. PAP is phosphorylated by Cdk1 in a cell cycle-dependent manner, a purified phosphorylation-deficient Ser/Thr 3 Ala septuple mutant enzyme exhibits elevated PAP activity
phosphoprotein
-
phosphorylation, e.g. by Nem1p, plays an important role in modulation of enzyme activity, overview
phosphoprotein
-
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
phosphoprotein
-
the enzyme is phosphorylated by cyclin-dependent kinase 1
phosphoprotein
-
the enzyme translocates from the cytosol to the nuclear/endoplasmic reticulum membrane through phosphorylation and dephosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D398E
the mutant shows less than 0.1% compared to wild type enzyme
D400E
the mutant shows less than 0.1% compared to wild type enzyme
S110A
phosphorylation site mutant, mutation diminishes inhibitory effects of phosphorylation by Pho85p-Pho80p
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
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
D398E
D400E
G80R
S110A/S114A/S168A/S602A/T723A/S744A/S748A
-
site-directed mutagenesis, phosphorylation of the mutant is completely abolished
S168A/S602A/T723A/S744A/S748A
-
site-directed mutagenesis, the mutant shows reduce dphosphorylation
additional information
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
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
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
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30
-
inhibition of the 45-kDa and 104-kDa enzyme forms, unstable above
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, the 45000 Da enzyme form is stable for 3 months, the 104000 Da enzyme form is degraded to a 91000 Da enzyme form and retains full activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
45-kDA, 91-kDA, and 104-kDa enzyme forms to homogeneity from membranes by sodium cholate solubilization of total membranes and subsequent anion exchange, affinity and hydroxylapatite chromatography followed by another step of anion exchange chromatgrphy and gel filtration, cytosolic enzyme form to homogeneity by ammonium sulfate and polyethylene glycol fractionation, steps followed by anion exchange chromatography, gel filtration, and adsorption chromatography
-
recombinant His-tagged wild-type and mutant isozyme PAH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 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
-
overexpression in Spodoptera frugiperda Sf9 cells using the baculovirus expression system, and in Saccharomyces cerevisiae using multicopy plasmids
-
subcloning and expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha and BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced throughout growth and the induction in the stationary phase is stimulated by inositol supplementation. The Ino2p/Ino4p/Opi1p regulatory circuit and transcription factors Gis1p and Rph1p mediated this regulation
wild type cells supplemented with palmitoleic acid exhibit an induction in phosphatidate phosphatase activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the PAP1 colorimetric assay with pure enzyme and a water-soluble phosphatidate substrate is applicability to a 96-well format, which may facilitate a large-scale screen of PAP1 inhibitors (or activators)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hosaka, K.; Yamashita, S.
Partial purification and properties of phosphatidate phosphatase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
796
102-109
1984
Saccharomyces cerevisiae
Carman, G.M.
Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli
Biochim. Biophys. Acta
1348
45-55
1997
Saccharomyces cerevisiae, Escherichia coli
Morlock, K.R.; McLaughlin, J.J.; Lin, Y.P.; Carman, G.M.
Phosphatidate phosphatase from Saccharomyces cerevisiae. Isolation of 45- and 104-kDa forms of the enzyme that are differentially regulated by inositol
J. Biol. Chem.
266
3586-3593
1991
Saccharomyces cerevisiae
Kocsis, M.G.; Weselake, R.J.
Phosphatidate phosphatases of mammals, yeast, and higher plants
Lipids
31
785-802
1996
Arachis hypogaea, Saccharomyces cerevisiae, Vicia faba, Vigna radiata, Rattus norvegicus, Sus scrofa
Furneisen, J.M.; Carman, G.M.
Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1484
71-82
2000
Saccharomyces cerevisiae
Wu, W.I.; Carman, G.M.
Kinetic analysis of sphingoid base inhibition of yeast phosphatidate phosphatase
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312
373-380
2000
Saccharomyces cerevisiae
Han, G.S.; Wu, W.I.; Carman, G.M.
The Saccharomyces cerevisiae lipin homologue is a Mg2+-dependent phosphatidate phosphatase enzyme
J. Biol. Chem.
281
9210-9218
2006
Saccharomyces cerevisiae, Homo sapiens
Oshiro, J.; Han, G.S.; Carman, G.M.
Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1635
1-9
2003
Saccharomyces cerevisiae
Han, G.S.; Johnston, C.N.; Carman, G.M.
Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae
J. Biol. Chem.
279
5338-5345
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
O'Hara, L.; Han, G.S.; Peak-Chew, S.; Grimsey, N.; Carman, G.M.; Siniossoglou, S.
Control of phospholipid synthesis by phosphorylation of the yeast lipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase
J. Biol. Chem.
281
34537-34548
2006
Saccharomyces cerevisiae
Donkor, J.; Sariahmetoglu, M.; Dewald, J.; Brindley, D.N.; Reue, K.
Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns
J. Biol. Chem.
282
3450-3457
2007
Saccharomyces cerevisiae, Mus musculus
Han, G.S.; Siniossoglou, S.; Carman, G.M.
The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity
J. Biol. Chem.
282
37026-37035
2007
Saccharomyces cerevisiae
Carman, G.M.; Wu, W.I.
Lipid phosphate phosphatases from Saccharomyces cerevisiae
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434
305-315
2007
Saccharomyces cerevisiae
Kim, Y.; Gentry, M.S.; Harris, T.E.; Wiley, S.E.; Lawrence, J.C.; Dixon, J.E.
A conserved phosphatase cascade that regulates nuclear membrane biogenesis
Proc. Natl. Acad. Sci. USA
104
6596-6601
2007
Saccharomyces cerevisiae
Carman, G.M.; Han, G.S.
Roles of phosphatidate phosphatase enzymes in lipid metabolism
Trends Biochem. Sci.
31
694-699
2006
Saccharomyces cerevisiae
Carman, G.M.; Han, G.
Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis
J. Biol. Chem.
284
2593-2597
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
Reue, K.; Brindley, D.N.
Thematic Review Series: Glycerolipids. Multiple roles for lipins/phosphatidate phosphatase enzymes in lipid metabolism
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49
2493-2503
2008
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
Havriluk, T.; Lozy, F.; Siniossoglou, S.; Carman, G.
Colorimetric determination of pure Mg2+-dependent phosphatidate phosphatase activity
Anal. Biochem.
373
392-394
2008
Saccharomyces cerevisiae
Nakamura, Y.; Koizumi, R.; Shui, G.; Shimojima, M.; Wenk, M.R.; Ito, T.; Ohta, H.
Arabidopsis lipins mediate eukaryotic pathway of lipid metabolism and cope critically with phosphate starvation
Proc. Natl. Acad. Sci. USA
106
20978-20983
2009
Arabidopsis thaliana, Saccharomyces cerevisiae
Siniossoglou, S.
Lipins, lipids and nuclear envelope structure
Traffic
10
1181-1187
2009
Saccharomyces cerevisiae, Mus musculus, Rattus norvegicus
Fakas, S.; Qiu, Y.; Dixon, J.L.; Han, G.S.; Ruggles, K.V.; Garbarino, J.; Sturley, S.L.; Carman, G.M.
Phosphatidate phosphatase activity plays key role in protection against fatty acid-induced toxicity in yeast
J. Biol. Chem.
286
29074-29085
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
Karanasios, E.; Han, G.S.; Xu, Z.; Carman, G.M.; Siniossoglou, S.
A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase
Proc. Natl. Acad. Sci. USA
107
17539-17544
2010
Saccharomyces cerevisiae
Choi, H.S.; Su, W.M.; Han, G.S.; Plote, D.; Xu, Z.; Carman, G.M.
Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism
J. Biol. Chem.
287
11290-11301
2012
Saccharomyces cerevisiae (P32567), Saccharomyces cerevisiae
Pascual, F.; Soto-Cardalda, A.; Carman, G.M.
PAH1-encoded phosphatidate phosphatase plays a role in the growth phase- and inositol-mediated regulation of lipid synthesis in Saccharomyces cerevisiae
J. Biol. Chem.
288
35781-35792
2013
Saccharomyces cerevisiae (P32567), Saccharomyces cerevisiae
Su, W.M.; Han, G.S.; Carman, G.M.
Cross-talk phosphorylations by protein kinase C and Pho85p-Pho80p protein kinase regulate Pah1p phosphatidate phosphatase abundance in Saccharomyces cerevisiae
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289
18818-18830
2014
Saccharomyces cerevisiae (P32567), Saccharomyces cerevisiae
Pascual, F.; Hsieh, L.S.; Soto-Cardalda, A.; Carman, G.M.
Yeast Pah1p phosphatidate phosphatase is regulated by proteasome-mediated degradation
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289
9811-9822
2014
Saccharomyces cerevisiae (P32567), Saccharomyces cerevisiae
Dubots, E.; Cottier, S.; Peli-Gulli, M.P.; Jaquenoud, M.; Bontron, S.; Schneiter, R.; De Virgilio, C.
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9
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Saccharomyces cerevisiae
Carman, G.M.; Han, G.S.
Phosphatidate phosphatase regulates membrane phospholipid synthesis via phosphatidylserine synthase
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67
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2018
Saccharomyces cerevisiae
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63
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Saccharomyces cerevisiae (P32567)
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Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis
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284
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Saccharomyces cerevisiae
Han, G.S.; Carman, G.M.
Yeast PAH1-encoded phosphatidate phosphatase controls the expression of CHO1-encoded phosphatidylserine synthase for membrane phospholipid synthesis
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292
13230-13242
2017
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
Park, Y.; Han, G.S.; Carman, G.M.
A conserved tryptophan within the WRDPLVDID domain of yeast Pah1 phosphatidate phosphatase is required for its in vivo function in lipid metabolism
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292
19580-19589
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Saccharomyces cerevisiae (P32567), Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A (P32567)
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294
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Saccharomyces cerevisiae
EXTERNAL LINKS (specific for EC-Number 3.1.3.4)
Transporter Classification Database (TCDB): 9.B.105.3.2
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