Information on EC 3.1.3.4 - phosphatidate phosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.1.3.4
-
RECOMMENDED NAME
GeneOntology No.
phosphatidate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
the active site of plasma membrane LPP-1, LPP-2, and LPP-3 is outside the cell, the conserved phosphatase family amino acids are essential for catalytic activity
-
a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
catalytic site structure within the transverse plane of the vacuole membrane, overview
-
a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
catalytic site structure within the transverse plane of the vacuole membrane, overview
Saccharomyces cerevisiae W303-1A
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Ether lipid metabolism
-
-
Glycerolipid metabolism
-
-
Glycerophospholipid metabolism
-
-
Metabolic pathways
-
-
Sphingolipid metabolism
-
-
stigma estolide biosynthesis
-
-
triacylglycerol biosynthesis
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3-sn-phosphatidate phosphohydrolase
-
-
3-sn-phosphatidate phosphohydrolase
-
-
acid phosphatidyl phosphatase
-
-
-
-
DGPP phosphatase
-
-
DGPP phosphatase
Saccharomyces cerevisiae W303-1A
-
-
-
diacylglycerol diphosphate phosphatase
-
-
diacylglycerol diphosphate phosphatase
Saccharomyces cerevisiae W303-1A
-
-
-
diacylglycerol pyrophosphate phosphatase
-
-
diacylglycerol pyrophosphate phosphatase
Saccharomyces cerevisiae W303-1A
-
-
-
DPP1
Saccharomyces cerevisiae W303-1A
-
-
-
DPPL1
Q8NEB5
-
DPPL2
Q5VZY2
-
Dri-42
-
i.e. LPP-3
Dri42
-
i.e. isozyme LPP3
ecto-PAPase
-
-
-
-
ecto-phosphatidic acid phosphohydrolase
-
-
-
-
Germ cell guidance factor
-
-
-
-
Ippalpha
Q9K3P6
-
Ippalpha
Streptomyces coelicolor ATCC BAA-471
Q9K3P6
-
-
Ippbeta
Q9EWX3
-
Ippbeta
Streptomyces coelicolor ATCC BAA-471
Q9EWX3
-
-
Lazaro phosphatidic acid phosphatase
-
-
lipid phosphate phosphatase
-
-
lipid phosphate phosphatase
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
-
lipid phosphate phosphatase
-
-
lipid phosphate phosphatase
-
-
lipid phosphate phosphatase
-
-
lipid phosphate phosphatase
Q32ZL2
-
lipid phosphate phosphatase
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
lipid phosphate phosphatase
-
-
lipid phosphate phosphatase
-
-
lipid phosphate phosphatase 1
-
-
lipid phosphate phosphatase 3
-
-
lipid phosphate phosphatase 3
-
-
lipid phosphate phosphatase-1
-
-
lipid phosphate phosphatase-1
-
-
lipid phosphate phosphatase-1
-
-
lipid phosphate phosphatase-2
-
-
lipid phosphate phosphatase-2
-
-
lipid phosphate phosphatase-3
-
-
lipid phosphate phosphatase-3
-
-
lipid phosphate phosphatase-related protein
-
-
lipid phosphate phosphatase-related protein type 1
Q8TBJ4
-
lipid phosphate phosphatase-related protein type 2
Q96GM1
-
lipid phosphate phosphatase-related protein type 3
Q6T4P5
-
lipid phosphate phosphatase-related protein type 4
Q7Z2D5
-
lipid phosphate phosphohydrolase
-
-
lipid phosphate phosphohydrolase
-
-
lipidphosphatase-related protein 1
Q8TBJ4
-
lipin
-
-
lipin 1beta
-
-
lipin 3
-
-
lipin Pah1p/Smp2p
-
-
lipin-1
Q9XXT5
-
lipin-1
Q14693
-
lipin-1
Mus musculus C57BL/6J
-
-
-
lipin-1alpha
-
isoform
lipin-1alpha
-
-
lipin-1alpha
-
isoform
lipin-1gamma
-
isoform
lipin-1gamma
-
isoform
lipin-2
Mus musculus C57BL/6J
-
-
-
Lipin1
-
-
Lipin1
B7STY8
-
lipin1alpha
-
-
lipin1beta
-
-
LLP2
-
-
LPA phosphatase
-
-
LPIN1
-
-
LPP
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
-
LPP
Q32ZL2
-
LPP
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
LPP1
Q8TBJ4
-
LPP1-encoded lipid phosphatase
-
-
LPP2
Q8TBJ4
-
LPP3
Q8TBJ4
-
LPPR2
Q96GM1
-
LPR-1
Q8TBJ4
-
LPR-2
Q96GM1
-
LPR-3
Q6T4P5
-
LPR-4
Q7Z2D5
-
LPR1
Q8TBJ4
-
lysophosphatidic acid phosphatase
-
-
Mg2+-dependent PA1 phosphatase
-
-
Mg2+-dependent phosphatidate phosphatase
-
-
Mg2+-dependent phosphatidate phosphatase
Mus musculus C57BL/6J
-
-
-
Mg2+-dependent phosphatidate phosphatase
-
-
PA phosphatase
-
-
-
-
PA phosphatase
-
-
PA phosphatase
-
-
PA phosphatase
Saccharomyces cerevisiae W303-1A
-
-
-
PA-P
-
-
PA-PSP
-
-
pah1
-
isoform
PAH2
-
isoform
PAP
-
-
-
-
PAP
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
-
PAP
Q5VZY2, Q8NEB5
-
PAP
Mus musculus C57BL/6J
-
-
-
PAP
Saccharomyces cerevisiae W303-1A
-
-
-
PAP-2
-
-
PAP-2b
-
-
PAP2
-
-
PAP2-like protein
A5HKK6
-
PAP2-like protein
Geobacillus toebii T-85
A5HKK6
-
-
PAP2a
-
-
PAP2d
Q32ZL2
-
PAP2L2
A5HKK6
-
PAP2L2
Geobacillus toebii T-85
A5HKK6
-
-
phosphatidate phosphatase
-
-
phosphatidate phosphatase
-
-
phosphatidate phosphatase
Q5VZY2, Q8NEB5
-
phosphatidate phosphatase
-
-
phosphatidate phosphatase
Mus musculus C57BL/6J
-
-
-
phosphatidate phosphatase
-
-
phosphatidate phosphatase
-
-
phosphatidate phosphatase type-1
-
-
phosphatidate phosphatase-1
-
-
phosphatidate phosphatase-1
-
-
phosphatidate phosphatase-1
-
-
phosphatidate phosphatases
-
-
phosphatidate phosphohydrolase
-
-
-
-
phosphatidate phosphohydrolase
-
-
phosphatidate phosphohydrolase
-
-
phosphatidate phosphohydrolase 1
-
-
phosphatidic acid phosphatase
-
-
-
-
phosphatidic acid phosphatase
-
-
phosphatidic acid phosphatase
-
-
phosphatidic acid phosphatase
-
-
phosphatidic acid phosphatase
-
-
phosphatidic acid phosphatase
-
-
phosphatidic acid phosphatase 2a
-
-
phosphatidic acid phosphatase type 2
Q32ZL2
-
phosphatidic acid phosphatase-1
-
-
phosphatidic acid phosphatases
-
-
phosphatidic acid phosphohydrolase
-
-
-
-
phosphatidic acid phosphohydrolase
-
-
phosphatidic acid phosphohydrolase
-
-
phosphatidic acid phosphohydrolase 1
-
-
phosphatidic acid phosphohydrolase-1
-
-
plasticity related gene 1
Q7Z2D5
-
plasticity related gene 3
Q6T4P5, Q8TBJ4
-
plasticity related gene 4
Q96GM1
-
presqualene diphosphate phosphatase
-
-
PRG-1
-
plasticity-related gene-1
PRG-1
Q7Z2D5
-
PRG-1
-
plasticity-related gene-1
PRG-3
Q8TBJ4
-
PRG3
Q8TBJ4
-
RHA1_ro00075
Q0SKM5
gene name
SCO1102
Q9K3P6
gene name
SCO1102
Streptomyces coelicolor ATCC BAA-471
Q9K3P6
gene name
-
SCO1753
Q9EWX3
gene name
SCO1753
Streptomyces coelicolor ATCC BAA-471
Q9EWX3
gene name
-
type 2b phosphatidic acid phosphatase
-
-
Wunen protein
-
-
-
-
Mg2+-dependent phosphatidic acid phosphatase
-
-
additional information
Q6NLA5, Q6NQL6
plastidic PAPs in Arabidopsis belong to a distinct lipid phosphate phosphatase LPP subfamily with prokaryotic origin
additional information
-
the enzyme belongs to the group of lipid phosphate phosphatases
additional information
-
the enzyme belongs to the lipid phosphate phosphatase family
additional information
A5HKK6
the enzyme belongs to the type 2 phosphatidic acid phosphatase superfamily
additional information
Geobacillus toebii T-85
A5HKK6
the enzyme belongs to the type 2 phosphatidic acid phosphatase superfamily
-
additional information
-
the enzyme belongs to the lipid phosphate phosphatase family
additional information
-
the enzyme belongs to the lipin family
additional information
Q5VZY2, Q8NEB5
cf. EC 3.1.3.B2
additional information
-
the enzyme belongs to the lipid phosphate phosphatase family
additional information
-
the enzyme belongs to the lipin family
additional information
-
the enzyme is a member of the lipin family
additional information
-
the enzyme belongs to the lipid phosphate phosphatase family
additional information
-
the enzyme belongs to the lipin family
additional information
-
cf. EC 3.1.1.34
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
additional information
-
the enzyme belongs to the lipin family
CAS REGISTRY NUMBER
COMMENTARY
9025-77-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acholeplasma laidlawii A
A
-
-
Manually annotated by BRENDA team
ecotype Columbia-0
-
-
Manually annotated by BRENDA team
isozyme LPPbeta; ecotype Columbia-0, Arabidopsis contains five homologs of cyanobacterial LPP
SwissProt
Manually annotated by BRENDA team
isozyme LPPdelta; ecotype Columbia-0
SwissProt
Manually annotated by BRENDA team
isozyme LPPepsilon2; ecotype Columbia-0, Arabidopsis contains five homologs of cyanobacterial LPP
SwissProt
Manually annotated by BRENDA team
isozyme LPPgamma; ecotype Columbia-0, Arabidopsis contains five homologs of cyanobacterial LPP
SwissProt
Manually annotated by BRENDA team
This UniProt-ID has been deleted; ecotype Columbia-0, Arabidopsis contains five homologs of cyanobacterial LPP
-
-
Manually annotated by BRENDA team
isozymes LPP1, LPP-2, and LPP-3
-
-
Manually annotated by BRENDA team
gene Iaza or Iazaro
-
-
Manually annotated by BRENDA team
genes Wun and Wun2
-
-
Manually annotated by BRENDA team
strain T-85
UniProt
Manually annotated by BRENDA team
Geobacillus toebii T-85
strain T-85
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
DPPL1; isozyme DPPL1
UniProt
Manually annotated by BRENDA team
DPPL2; isozyme DPPL2
UniProt
Manually annotated by BRENDA team
gene PAP2a
-
-
Manually annotated by BRENDA team
genes Lpin1, Lpin2, and Lpin3
-
-
Manually annotated by BRENDA team
isozymes LPP1, LPP-2, and LPP-3
-
-
Manually annotated by BRENDA team
isozymes LPP1-3
-
-
Manually annotated by BRENDA team
isozymes LPP1-3, several splicing variants of LPP1
-
-
Manually annotated by BRENDA team
isozymes PAP-1 and PAP-2
-
-
Manually annotated by BRENDA team
LPR-2 or PRG-4; PRG-4 or LPR-2
SwissProt
Manually annotated by BRENDA team
LPR-3; LPR-3
SwissProt
Manually annotated by BRENDA team
LPR1
SwissProt
Manually annotated by BRENDA team
PRG-1 or LPR-4; PRG-1 or LPR-4
SwissProt
Manually annotated by BRENDA team
PRG-3 or LPR-1; isozyme PRG-3 or LPR-1
SwissProt
Manually annotated by BRENDA team
transcript PAP2d_v1, PAP2 protein fragment; PAP2d, transcript PAP2d_v1
SwissProt
Manually annotated by BRENDA team
transcript PAP2d_v2, PAP2 protein; PAP2d, transcript PAP2d_v2
-
-
Manually annotated by BRENDA team
; heterozygous BALB/cByJ-fld/+ mice
Uniprot
Manually annotated by BRENDA team
C57BL/6J and ob/ob mice
-
-
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
gene LIPIN1
-
-
Manually annotated by BRENDA team
genes Lpin1 and Lpin2
-
-
Manually annotated by BRENDA team
genes Lpin1, Lpin2, and Lpin3
-
-
Manually annotated by BRENDA team
isozyme LPP-1
-
-
Manually annotated by BRENDA team
isozymes LPP1, LPP-2, and LPP-3
-
-
Manually annotated by BRENDA team
isozymes LPP1-3, several splicing variants of LPP1
-
-
Manually annotated by BRENDA team
male C57BL/6 mice
-
-
Manually annotated by BRENDA team
nondiabetic C57BL6 and CD-1 mice, and diabetic NOD mice and Pd-NOD mice, gene lipin1
-
-
Manually annotated by BRENDA team
several isozymes, e.g. isozyme PAP2A, i.e. LPP-1
-
-
Manually annotated by BRENDA team
three lipins, C57BL/6J and BALB/cByJ-Lpin1+/fld mice
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
C57BL/6J mice
-
-
Manually annotated by BRENDA team
2 different phosphatidate phosphatidases: PAP-1 and PAP-2
-
-
Manually annotated by BRENDA team
isozyme PAP-2; isozymes PAP-1 and PAP-2
-
-
Manually annotated by BRENDA team
isozymes LPP1, LPP-2, and LPP-3
-
-
Manually annotated by BRENDA team
isozymes LPP1-3, several splicing variants of LPP1
-
-
Manually annotated by BRENDA team
a single lipin homolog, Smp2
-
-
Manually annotated by BRENDA team
gene PAH1, formerly SMP2
-
-
Manually annotated by BRENDA team
isozymes PAP1 and PAP2, encoded by genes PAH1, formerly known as SMP2, and DPP1 and LPP1, respectively
-
-
Manually annotated by BRENDA team
several strains, isozyme PAH1
-
-
Manually annotated by BRENDA team
several strains, overview
-
-
Manually annotated by BRENDA team
strain W303-1A, gene DPP1
-
-
Manually annotated by BRENDA team
two genes DPP1 and LPP1 encode Mg2+-independent phosphatidic acid phosphatase activities
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae W303-1A
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae W303-1A
strain W303-1A, gene DPP1
-
-
Manually annotated by BRENDA team
isoform Ippalpha
UniProt
Manually annotated by BRENDA team
isoform Ippbeta
UniProt
Manually annotated by BRENDA team
Streptomyces coelicolor ATCC BAA-471
isoform Ippalpha
UniProt
Manually annotated by BRENDA team
Streptomyces coelicolor ATCC BAA-471
isoform Ippbeta
UniProt
Manually annotated by BRENDA team
cv. 1183
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Q9XXT5
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
-
suppression of cardiac PAP1 activity/lipin expression may contribute to metabolic dysfunction of the diabetic heart
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
Saccharomyces cerevisiae W303-1A
-
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
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
-
atrial tissue displays PAP1 activity that is 33% lower in those having type 2 diabetes mellitus than in non-diabetic controls
physiological function
-
compared to non-diabetic littermates, left ventricular PAP1 activity is 29% lower in 8-months-old Zucker diabetic fatty rats. Left ventricular PAP1 activities are 2.1fold (diabetic fatty rats) and 3.6fold (non-diabetic rats) higher than the respective atrial activities
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
Q9XXT5
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
B7STY8
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
-
lipins are essential regulators of fat metabolism, adipogenesis, and organelle biogenesis
physiological function
-
lysophosphatidate phosphatase plays a significant role in supplying the phosphate during phosphate-deficient conditions
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
-
the low expression of lipid phosphate phosphatase in many tumor cells makes them hypersensitive to growth promoting and survival signals that are provided by lysophosphatidate, S1P, platelet-derived growth factor and epidermal growth factor. The intracellular actions of the enzyme controls cell migration, division, angiogenesis and chemoresistance. Increased LPP1 expression attenuates lysophosphatidate-induced migration of fibroblasts
physiological function
P34913
bifunctional enzyme displaying C-terminal epoxide hydrolase and N-terminal phosphatase activity. The phosphatase activity represents a 20-60% of lysophosphatidic acid cellular hydrolysis, especially in the cytosol
physiological function
Q0SKM5
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
Streptomyces coelicolor ATCC BAA-471
-
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
Mus musculus C57BL/6J
-
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
Saccharomyces cerevisiae W303-1A
-
phosphatidate phosphatase activity is essential in protecting cells from palmitoleic acid (fatty acid)-induced toxicity
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1,2-diacyl-sn-glycerol-3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
-
1,2-dioleoyl-sn-glycerol 3-phosphate + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1,2-dipalmitoyl-sn-glycerol 3-phosphate + H2O
1,2-dipalmitoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-acyl-sn-glycerol 3-phosphate + H2O
1-acyl-sn-glycerol + phosphate
show the reaction diagram
-
less than 15% of the activity with phosphatidic acid
-
-
?
1-acyl-sn-glycerol 3-phosphate + H2O
1-acyl-sn-glycerol + phosphate
show the reaction diagram
-
at 9.1% of the activity with phosphatidic acid
-
-
?
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-arachidonoylglycerol + phosphate
show the reaction diagram
P34913
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
1-lauroyl-2-lysophosphatidate + H2O
1-lauroyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-myristoyl-2-lysophosphatidate + H2O
1-myristoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-myristoyl-sn-glycerol 3-phosphate + H2O
1-myristoylglycerol + phosphate
show the reaction diagram
P34913
-
-
-
?
1-oleoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-oleoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-oleoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-oleoylglycerol + phosphate
show the reaction diagram
P34913
-
-
-
?
1-oleoyl-2-lysophosphatidate + H2O
oleic acid + sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-palmitoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-lysophosphatidate + H2O
1-palmitoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate + H2O
1-stearoyl-2-arachidonoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-stearoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-lysophosphatidate + H2O
1-stearoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
1-stearyl-2-lyso-sn-glycerol 3-phosphate + H2O
1-stearylglycerol + phosphate
show the reaction diagram
P34913
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
fluorescent substrate derivative
-
-
?
5'-AMP + H2O
?
show the reaction diagram
-
8.6% of the activity with phosphatidic acid
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
Q14693
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
A5HKK6
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q14693
lipin-1 is negatively regulated by phosphorylation during mitosis
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
lipin-2 is negatively regulated by phosphorylation during mitosis
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in lipid synthesis and cell signalling
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
Geobacillus toebii T-85
A5HKK6
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
7.2% of the activity with phosphatidic acid
-
-
?
attophos A + H2O
?
show the reaction diagram
P34913
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
about 10% of the activity with phosphatidic acid
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
-
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
-
-
?
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
Q8TBJ4
LPP1 but not LPR1
-
-
?
ceramide-1-phosphate + H2O
?
show the reaction diagram
-
isoenzyme PAP-2a and PAP-2b
-
-
?
diacylglycerol diphosphate + H2O
?
show the reaction diagram
-
-
-
?
diacylglycerol diphosphate + H2O
?
show the reaction diagram
Q5VZY2, Q8NEB5
preferred substrate of isozyme DPPL1
-
-
?
diacylglycerol diphosphate + H2O
?
show the reaction diagram
Q5VZY2, Q8NEB5
preferred substrate of isozyme DPPL2
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
-
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, 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
show the reaction diagram
-
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
show the reaction diagram
Saccharomyces cerevisiae W303-1A
-
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, 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
? + phosphate
show the reaction diagram
Geobacillus toebii, Geobacillus toebii T-85
A5HKK6
preferred substrate
-
-
?
dicaproyl phosphatidate + H2O
1,2-dicaproyl-sn-glycerol + phosphate
show the reaction diagram
-
best substrate of the 104-kDa enzyme form
-
-
?
didecanoyl phosphatidic acid + H2O
1,2-didecanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
didecanoyl phosphatidic acid + H2O
1,2-didecanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dihexanoyl phosphatidic acid + H2O
1,2-dihexanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dihexanoyl phosphatidic acid + H2O
1,2-dihexanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dihydro-sphingosine-1-phosphate + H2O
dihydro-sphingosine + phosphate
show the reaction diagram
-
all LPPs
-
-
?
dimyristoyl phosphatidic acid + H2O
1,2-dimyristoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dimyristoyl phosphatidic acid + H2O
1,2-dimyristoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dioctanoyl phosphatidic acid + H2O
1,2-dioctanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dioctanoyl phosphatidic acid + H2O
1,2-dioctanoyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
dioleoyl phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dioleoyl phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dipalmitoyl phosphatidate + H2O
1,2-dipalmitoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dipalmitoyl phosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
distearoyl phosphatidic acid + H2O
1,2-distearoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
DL-alpha-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
about 10% of the activity with phosphatidic acid
-
-
?
FTY720-phosphate + H2O
FTY720 + phosphate
show the reaction diagram
-
LPP3
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
at 5.2% of the activity with phosphatidic acid
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
about 10% of the activity with phosphatidic acid
-
-
?
glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
all LPPs
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
Q8TBJ4
LPP1 but not LPR1
-
-
?
lysophosphatidate + H2O
?
show the reaction diagram
-
-
-
-
?
lysophosphatidate + H2O
?
show the reaction diagram
-
-
-
-
?
lysophosphatidate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
lysophosphatidate + H2O
?
show the reaction diagram
-
isoenzyme PAP-2a and PAP-2b
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
best substrate
-
-
?
lysophosphatidic acid + H2O
?
show the reaction diagram
-
-
-
?
lysophosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
?
show the reaction diagram
Q5VZY2, Q8NEB5
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
-
-
?
lysophosphatidic acid + H2O
mono-oleoyl-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
octanoyl lysophosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
oleoyl phosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
about 10% of the activity with phosphatidic acid
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
preferred substrate
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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, 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
show the reaction diagram
Saccharomyces cerevisiae W303-1A
-
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, 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
?
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
Q5VZY2, Q8NEB5
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
highly specific for
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
membrane-bound phosphatidic acid and aqueously dispersed phosphatidic acid
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
phosphatidic acid pure or in mixed micelles with phosphatidylcholine
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
lipin-1, lipin-2, and lipin-3
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
diacylglycerol is the necessary precursor for the synthesis of triacylglycerols, phosphatidylcholine and phosphatidylethanolamine
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
Acholeplasma laidlawii A
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
Mus musculus C57BL/6J
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
Saccharomyces cerevisiae W303-1A
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
Q8TBJ4
LPP1 but not LPR1
-
-
?
phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
Q91ZP3
insulin and epinephrine control lipin 1 primarily by changing localization rather than intrinsic PAP activity, overview
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
show the reaction diagram
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
-
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
show the reaction diagram
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
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
phosphate + diacylglycerol
show the reaction diagram
Q91ZP3
-
-
-
?
phosphatidic acid + H2O
? + phosphate
show the reaction diagram
Geobacillus toebii, Geobacillus toebii T-85
A5HKK6
preferred substrate
-
-
?
sphingosine 1-phosphate + H2O
?
show the reaction diagram
-
poor substrate
-
?
sphingosine 1-phosphate + H2O
?
show the reaction diagram
-
hydrolysis by isoenzyme PAP-2b, no hydrolysis by isoenzyme PAP-2a
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
all LPPs
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
Q8TBJ4
LPP1 but not LPR1
-
-
?
lysophosphatidic acid + H2O
? + phosphate
show the reaction diagram
Geobacillus toebii, Geobacillus toebii T-85
A5HKK6
-
-
-
?
additional information
?
-
-
-
-
-
-
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
?
-
-
the functional role of the enzyme in lamellar bodies is proposed in relation to glycerophospholipd metabolism
-
-
-
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 is involved in de novo synthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine
-
-
-
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
?
-
-
the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
-
-
-
additional information
?
-
-
the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
-
-
-
additional information
?
-
-
critical roles of the enzyme in cell growth and differentiation
-
-
-
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 may play an important role in regulating inflammatory cell responses to extracellular phosphatidic acid in biological system
-
-
-
additional information
?
-
-
the Mg2+-dependent enzyme of rat lung is involved in pulmonary glycerolipid biosynthesis
-
-
-
additional information
?
-
-
the diacylglycerol formed by the enzyme is used as a substrate for galactolipid synthesis on the inner envelope membrane
-
-
-
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
?
-
-
role of PAP-1 as a key enzyme for cell integrity and survival
-
?
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
?
-
Q32ZL2
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, 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, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in epithelial cells
-
-
-
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
?
-
-
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
?
-
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
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
?
-
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
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, Wunen and Wunen2 are essential for germ cell development, overview
-
-
-
additional information
?
-
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
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
?
-
-
the enzyme activity is involved in generation of phosphatidic acid and diaclyglycerol implicated in signal transduction, and in aging, 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
?
-
-
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
?
-
-
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
?
-
-
substrate specificities of isozymes
-
-
-
additional information
?
-
-
the enzyme is homologous to mammalian lipin
-
-
-
additional information
?
-
-
the enzyme is homologous to murine lipid phosphate phosphatase isozyme LPP-1
-
-
-
additional information
?
-
-
Wunen does not interact with its counterpart Wunen-2
-
-
-
additional information
?
-
-
Wunen does not interact with Wunen2
-
-
-
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
?
-
-
lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
-
-
-
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
?
-
-
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 in the activation of 5-lipoxygenase in polymorphonuclear leukocytes together with phospholipase D via diacylglyceride generation, PLD/PA-P pathway, overview
-
-
-
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
?
-
-
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
?
-
Q8TBJ4
LPR1 does not hydrolyze phospholipid substrates under conditions that readily support LPP1 activity
-
-
-
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
?
-
-
expression of lipin-1 cells stimulates glycerolipid synthesis and secretion in McA-RH7777, 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 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
?
-
-
lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators to modulate gene expression in lipid metabolism
-
-
-
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
?
-
-
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
?
-
-
endogenous LPP2 and LPP3 form a complex
-
-
-
additional information
?
-
-
PAP1 activity is conferred by the DxDxT motif of the C-Lip domain contained in all lipin family members
-
-
-
additional information
?
-
A5HKK6
recombinant PAP2L2 shows a broad substrate specificity
-
-
-
additional information
?
-
-
the catalytic site is arranged into three distinct domains: one substrate recognition site and two catalytic sites
-
-
-
additional information
?
-
-
the purified recombinant enzyme does not hydrolyze sphingosine 1-phosphate, diacylglycerol diphosphate, glycerol-3-phosphate, lysophosphatidylcholine, lysophosphatidylethanolamine and phosphatidate
-
-
-
additional information
?
-
-
no substrates: dipalmitoyl phosphatidic acid, distearoyl phosphatidic acid
-
-
-
additional information
?
-
Geobacillus toebii T-85
A5HKK6
recombinant PAP2L2 shows a broad substrate specificity
-
-
-
additional information
?
-
Acholeplasma laidlawii A
-
the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
A5HKK6
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q14693
lipin-1 is negatively regulated by phosphorylation during mitosis
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
lipin-2 is negatively regulated by phosphorylation during mitosis
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in lipid synthesis and cell signalling
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
Geobacillus toebii T-85
A5HKK6
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
-
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
-
-
?
lysophosphatidate + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
best substrate
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
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
diacyl-sn-glycerol + phosphate
show the reaction diagram
-
preferred substrate
-
-
?
phosphatidate + H2O
diacyl-sn-glycerol + phosphate
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
-
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
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
Q91ZP3
insulin and epinephrine control lipin 1 primarily by changing localization rather than intrinsic PAP activity, overview
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
show the reaction diagram
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
-
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
show the reaction diagram
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
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
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
the functional role of the enzyme in lamellar bodies is proposed in relation to glycerophospholipd metabolism
-
-
-
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 is involved in de novo synthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine
-
-
-
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
?
-
-
the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
-
-
-
additional information
?
-
-
the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
-
-
-
additional information
?
-
-
critical roles of the enzyme in cell growth and differentiation
-
-
-
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 may play an important role in regulating inflammatory cell responses to extracellular phosphatidic acid in biological system
-
-
-
additional information
?
-
-
the Mg2+-dependent enzyme of rat lung is involved in pulmonary glycerolipid biosynthesis
-
-
-
additional information
?
-
-
the diacylglycerol formed by the enzyme is used as a substrate for galactolipid synthesis on the inner envelope membrane
-
-
-
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
?
-
-
role of PAP-1 as a key enzyme for cell integrity and survival
-
?
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
?
-
Q32ZL2
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, 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, overview, LPP-1 regulates the lysophosphatidic acid-induced calcium release, NF-kappaB activation and interleukin-8 secretion in epithelial cells
-
-
-
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
?
-
-
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
?
-
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
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
?
-
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
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, Wunen and Wunen2 are essential for germ cell development, overview
-
-
-
additional information
?
-
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
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
?
-
-
the enzyme activity is involved in generation of phosphatidic acid and diaclyglycerol implicated in signal transduction, and in aging, 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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
lipin-1 Smp2 exhibits phosphatidate phosphatase type-1 activity, which plays a key role in glycerolipid synthesis
-
-
-
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
?
-
-
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 in the activation of 5-lipoxygenase in polymorphonuclear leukocytes together with phospholipase D via diacylglyceride generation, PLD/PA-P pathway, overview
-
-
-
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
?
-
-
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
?
-
-
expression of lipin-1 cells stimulates glycerolipid synthesis and secretion in McA-RH7777, 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 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
?
-
-
lipin-1 operates as a transcriptional coactivator together with nuclear receptors and coactivators to modulate gene expression in lipid metabolism
-
-
-
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
?
-
Acholeplasma laidlawii A
-
the enzyme is proposed to catalyze the first enzymatic step in the important glucolipid pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
CaCl2, stimulates
Ca2+
-
stimulates
Ca2+
-
moderate inhibition of cytosolic and particulate activity
Ca2+
-
lipin 1-mediated repression of nuclear factor of activated T-cells transcriptional activity occurs after nuclear factor of activated T-cells mobilization and activation by calcium
Ca2+
-
may partly substitute for Mg2+ in binding to to serine/threonine protein phosphatase-1 catalytic subunit
Co(NO3)2
-
0.3 mM, about 3fold stimulation
Co2+
-
stimulates
Fe2+
-
stimulates
Fe3+
-
stimulates
Mg2+
-
MgCl2, 110-167fold stimulation
Mg2+
-
stimulates hydrolysis of phosphatidate bound to microsomal membrane or phosphatidate in sonicated dispersion of organic solvent-disrupted microsomes, optimal concentration: 8 mM, no effect on hydrolysis of phosphatidate dispersed in sonicated microsomal lipid
Mg2+
-
MgCl2 stimulates activity with membrane-bound phosphatidic acid in the cytosol by 7%, the activity with aqueously dispersed phosphatidic acid is inhibited 80%
Mg2+
-
below 5 mM, slight stimulation of cytosolic activity, inhibition at higher concentrations
Mg2+
-
required; required for activity by all enzyme forms
Mg2+
-
adipose tissue contains 2 different enzyme forms: a Mg2+-dependent form and a Mg2+-independent form
Mg2+
-
two Mg2+-independent isoenzymes: phosphatidic acid phosphatase PAP-1a and PAP-2b
Mg2+
-
independent of Mg2+
Mg2+
-
markedly potentiates the cytosolic but not the particulate activity
Mg2+
-
stimulates
Mg2+
-
the enzyme exists in a Mg2+-dependent enzyme form and a Mg2+-independent enzyme form
Mg2+
-
required for the 45000 Da enzyme form, maximal activity at 1 mM
Mg2+
-
independent of Mg2+
Mg2+
-
PAP-1 is dependent on
Mg2+
-
two membrane-associated forms, 45000 Da and 104000 Da, of the Mg2+-dependent phosphatidate phosphatase
Mg2+
-
isozyme PAP1
Mg2+
-
-
Mg2+
-
isozyme PAP-1, dependent on
Mg2+
-
PAP-1, dependent on
Mg2+
Q91ZP3
dependent on; required
Mg2+
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
50% inhibition at 10-20 mM, isozyme LPPepsilon2
Mg2+
-
all lipins are dependent on Mg2+
Mg2+
-
-
Mg2+
-
required
Mg2+
-
required
Mg2+
-
colorimetric assay
Mg2+
-
depends on
Mg2+
-
assay buffer
Mg2+
-
dependent on
Mg2+
-
dependent on
Mg2+
-
dependent on
Mg2+
-
dependent on
Mg2+
-
lipin-1 binding to to serine/threonine protein phosphatase-1 catalytic subunit depends on presence of Mg2+
Mg2+
-
in absence of Mg2+ activity towards 1-stearoyl-2-lyso-sn-glycerol 3-phosphate acid is significantly decreased
Mn2+
-
slight stimulation
Mn2+
-
slight stimulation
Mn2+
-
may substitute for Mg2+ in binding to to serine/threonine protein phosphatase-1 catalytic subunit
ZnSO4
-
0.3 mM, about 2.5fold stimulation
MnSO4
-
0.3 mM, about 3fold stimulation
additional information
-
no metal-ion requirement
additional information
-
Mg2+-independent enzyme
additional information
-
no requirement for Mg2+
additional information
-
the enzyme is Mg2+-independent and shows no divalent cation requirement for activity
additional information
Q5VZY2, Q8NEB5
isozyme DPPL1 is Mg2+-independent; isozyme DPPL2 is Mg2+-independent
additional information
-
independent of divalent metal ions
additional information
-
Lpp1p contains ten cysteine residues, whereas Dpp1p and Pah1p contain only three
additional information
-
the presqualene diphosphate phosphatase is a potent Mg2+-independent, NEM-insensitive type II PAP
additional information
A5HKK6
no requirement for Mg2+
additional information
-
cations like Mg2+, Mn2+, and Ca2+ have no effect on the enzyme activity
additional information
-
is Mg2+ independent
additional information
-
activity is independent of Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,2-diacylglycerol
-
-
1,2-diacylglycerol
-
-
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate
P34913
32% inhibition
-
1-myristoyl-2-lyso-sn-glycerol 3-phosphate
P34913
63% inhibition
-
1-oleoyl-2-lyso-sn-glycerol 3-phosphate
P34913
24% inhibition
1-palmitoyl-2-lyso-sn-glycerol 3-phosphate
-
40 microM, about 50% inhibition
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
amphiphilic amines
-
-
-
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
Be2+
-
-
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
bromoenol lactone
-
-
Butane-2,3-dione
-
-
Ca2+
-
1 mM, 10% inhibition
Ca2+
-
activity with aqueously dispersed phosphatidic acid
Ca2+
-
inhibition at optimal concentrations of Mg2+
Ca2+
-
-
Ca2+
-
IC50: 15 mM, reaction with phosphatidic acid. IC50: 7.1 mM, reaction with diacylglycerol diphosphate. IC50: 8.2 mM, reaction with lysophosphatidic acid
Ca2+
-
10 mM, 60% inhibition of PAP-2
ceramide 1-phosphate
-
-
chlorpromazine
-
-
chlorpromazine
-
competitive inhibition at optimal concentrations of Mg2+
chlorpromazine
-
-
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
-
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
cystamine dihydrochloride
-
1 mM, 25% inhibition of Mg2+-dependent enzyme, 8% inhibition of Mg2+-independent enzyme
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
-
-
dihydrosphingosine
-
-
dimethylsphingosine
-
-
DMSO
-
addition to the reaction mixture results in a dose-dependent inhibition of PAP1 activity, 25% loss of PAP1 activity at a 1% concentration
dodecyl phosphate
P34913
99% inhibition
-
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
epinephrine
Q91ZP3
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
F-
-
50 mM, 80% inhibition
F-
-
activity with aqueously dispersed phosphatidic acid
F-
-
50 mM, 90% inhibition
F-
-
NaF
F-
-
enzyme form PAP2
F-
-
NaF
geranyl diphosphate
P34913
30% inhibition
Insulin
Q91ZP3
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
-
lauric acid
-
40 microM, about 60% inhibition
linoleate
-
-
lysophosphatidic acid
-
-
lysophosphatidylcholine
-
-
lysophosphatidylethanolamine
-
-
lysophosphatidylglycerol
-
-
Mg2+
-
2.5 mM, slight inhibition
Mg2+
-
at high concentrations, activity with aqueously dispersed phosphatidic acid
Mg2+
-
above 5 mM
Mg2+
-
MgCl2
Mg2+
-
inhibition of reaction with diacylglycerol diphosphate. Little effect on reaction with lysophosphatidic acid and phosphatidic acid
Mg2+
-
15 mM MgCl2, 10-20% inhibition of PAP-2
Mg2+
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
about 75% inhibition at 20 mM, isozyme LPPgamma; about 95% inhibition at 20 mM, isozyme LPPepsilon1
Mn2+
-
above 0.1 mM, when assayed in presence of 5 mM MgCl2
Mn2+
-
activity with aqueously dispersed phosphatidic acid
Mn2+
-
-
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,N'-p-phenylenedimaleimide
-
0.4 mM, 44% inhibition of Mg2+-dependent enzyme, 7% inhibition of Mg2+-independent enzyme
N-acetyl-ceramide-phosphate
P34913
30% inhibition
-
N-ethylmaleimide
-
inhibition of the 45-kDa and 104-kDa enzyme forms
Na3VO4
-
2 mM, about 90% inhibition
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
-
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
-
no inhibition
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
-
the Mg2+-dependent enzyme form is inhibited, the Mg2+-independent enzyme form is not inhibited
NEM
-
45000 Da enzyme form, at 1 mM
NEM
-
no inhibition
NEM
-
no inhibition
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
-
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
-
potent inhibition of LPP1
NEM
Q5VZY2, Q8NEB5
inhibition of isozyme DPPL1; inhibition of isozyme DPPL2
NEM
-
inhibition of PAP-1
NEM
-
the yeast DPP1-encoded PAP2 activity is insensitive to NEM, whereas LPP1-encoded PAP2 activity is sensitive to NEM
octylglucoside
-
-
oleate
-
reversed by phosphatidic acid and albumin
oleic acid
Q91ZP3
promotes dephosphorylation of lipin, but has no effect on PAP activity, markedly decreases amounts of lipin and PAP activity in the soluble fraction
oleoyl-CoA
-
-
p-Chloromercuriphenylsulfonic acid
-
45000 Da enzyme form, at 1 mM
p-Chloromercuriphenylsulfonic acid
-
-
p-nitrophenyl phosphate
-
inhibits hydrolysis of phosphatidic acid
palmitate
-
1 mM, 30% inhibition
palmitic acid
-
40 microM, about 80% inhibition
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
-
-
Phenylglyoxal
-
is an arginine reactive compound, inhibits PAP1 activity in dose-dependent manner
phosphatidate
-
conpetitive versus diacylglycerol diphosphate
phosphatidic acid
-
competitive inhibition
phosphatidic acid
-
competitive with respect to diacylglycerol diphosphate
phosphatidic acid
-
substrate inhibition
phosphatidylcholine
-
slight inhibition of cytosolic activity
phosphatidylglycerol
-
0.7 mg/ml, 75% inhibition
phosphatidylinositol
-
-
phosphatidylserine
-
-
phytosphingosine
-
-
phytosphingosine
-
inhibition of PAH1
Propanolol
-
effective inhibitor of type 1 phosphatidic acid phosphatase, modest inhibitor of phosphatidic acid phosphatase PAP-2a, PAP-2b and PAP-2c
Propanolol
-
-
Propanolol
-
inhibition of the 45000 Da enzyme form and the 104000 Da enzyme form
Propanolol
-
slight stimulation
Propanolol
-
partial
Propanolol
-
-
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
-
inhibition of PAP-1
propranolol
-
-
propranolol
-
moderately effective inhibitor of LPP activity
propranolol
-
-
propranolol
-
interacts with the Mg2+-binding site of the enzyme, inhibits PAP1 activity in dose-dependent manner
RNAi2
Q8TBJ4
reduces expression levels of LPR1 by ca. 60% in SK-OV-3 cells
-
SDS
A5HKK6
1%, strong inhibition
shRNA
-
lipin 2 shRNA treatment significantly reduces hepatocyte PAP-1 activity in both wild-type and fld hepatocytes
-
siRNA
-
decrease of LPP1 mRNA by ca. 90%, knockdown of endogenous LPP1 activity by about 50% and increase of lyso-phosphatidic acid-induced migration
-
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
-
Sodium cholate
-
-
spermidine trihydrochloride
-
7% inhibition at equimolar concentration of substrate, PAP-2
spermine
-
above 1 mM
spermine
-
55% inhibition at equimolar concentration of substrate, PAP-2
sphinganine
-
inhibition of PAH1
sphingomyelin
-
72% inhibition at equimolar concentration with pure phosphatidic acid. No effect with equimolar concentrations of phosphatidic acid mixed with phosphatidylcholine
sphingosine
-
-
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
sphingosine 1-phosphate
-
-
stearic acid
-
about 20% inhibition
Stearylamine
-
-
thimerosal
-
0.5 mM, 85% inhibition of Mg2+-dependent enzyme, 12% inhibition of Mg2+-independent enzyme
Triton X-100
-
slight depression of activity with aqueously dispersed phosphatidic acid
Triton X-100
-
-
Tween 20
-
hydrolysis of phosphatidate bound to microsomal membrane in presence of optimal concentration of 8 mM
Tween 20
-
-
veranda
A5HKK6
10 mM, strong inhibition
-
Zn2+
-
above 0.1 mM, when assayed in presence of 5 mM MgCl2
Zn2+
-
-
Zn2+
-
-
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
Zn2+
A5HKK6
strong inhibition
Zwitterionic phospholipids
-
slight inhibition
-
monoacylglycerol
-
-
additional information
-
no effect on the enzyme forms by choline
-
additional information
-
light inhibition of PAP2 in ROS is a transducin-mediated mechanism
-
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
Q91ZP3
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
-
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
-
PAP-1 chemical inhibition does not reduce the synergistic activation of group IVA phospholipase A2
-
additional information
A5HKK6
no inhibition by N-ethylmaleimide
-
additional information
-
mitotic phosphorylation of lipin 1 inhibits its phosphatidic acid phosphatase activity
-
additional information
-
mitotic phosphorylation of lipin 2 inhibits its phosphatidic acid phosphatase activity
-
additional information
-
light regulation of the lipid phosphate phosphatases, overview
-
additional information
-
the isozymes are not affected by wounding or by treatment with jasmonic acid
-
additional information
-
the enzyme activity is insensitive to non-specific phosphatase inhibitors such as sodium o-vanadate and sodium fluoride
-
additional information
-
phosphorylation inhibits activity, phosphorylation of lipin 1 on multiple sites correlates with a decrease of its microsomal-bound pool
-
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
-
not inhibitory: 1-palmitoyl-sn-glycerol, 1-hexadecanol
-
additional information
-
presence of EDTA or EGTA does not significantly affect enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
half-maximal stimulation at 0.2 mM
androgen
-
highly induces LPP1 expression in LNCaP cells
-
cardiolipin
-
activation, antagonized by sphinganine
cardiolipin
-
PAH1-encoded PAP activity is enhanced by the phospholipids CDP-diacylglycerol, phosphatidylinositol, and cardiolipin
CDP
-
stimulates
CDP-diacylglycerol
-
-
CDP-diacylglycerol
-
PAH1-encoded PAP activity is enhanced by the phospholipids CDP-diacylglycerol, phosphatidylinositol, and cardiolipin
chlorpromazine
-
stimulates in absence of added Mg2+
deoxycholate
-
Triton X-100 or deoxycholate required
epinephrine
Q91ZP3
promotes dephosphorylation of lipin, but has no effect on PAP activity, markedly increases amounts of lipin and PAP activity in microsomes
GDP
-
stimulates
Insulin
Q91ZP3
increases the phosphorylation of multiple sites, markedly increases the amounts of lipin and PAP activity in the soluble fraction, effects of insulin are attenuated by rapamycin or by inhibiting PI 3 kinase
-
Insulin
-
insulin therapy increases both PAP1 activity and lipin mRNA expression in diabetic patients
-
oleic acid
-
stimulates
oleic acid
Q91ZP3
promotes dephosphorylation of lipin, but has no effect on PAP activity, markedly increases amounts of lipin and PAP activity in microsomes
phosphatidylcholine
-
stimulation
phosphatidylethanolamine
-
stimulation
phosphatidylglycerol
-
essential for optimal activity, responsible for a better solubilization of the substrate by CHAPS. The possibility of a specidic role as aphysiological activator cannot be ruled out
phosphatidylinositol
-
activation, antagonized by sphinganine
phosphatidylinositol
-
PAH1-encoded PAP activity is enhanced by the phospholipids CDP-diacylglycerol, phosphatidylinositol, and cardiolipin
Polyamines
-
activate in presence of Mg2+, no activation in absence of Mg2+
-
putrescine
-
activate in presence of Mg2+, no activation in absence of Mg2+. Effective at 2-5 mM
spermidine
-
activates in presence of Mg2+, no activation in absence of Mg2+. Effective at 1 mM
spermidine
-
stimulates
spermine
-
activates in presence of Mg2+, no activation in absence of Mg2+. Effective at 0.5-1 mM, inhibitory at higher concentrations
spermine
-
stimulates
sphingosine 1-phosphate
-
activates overall cell lipid phosphate phosphatase activities by about 13%
taurocholate
-
stimulates
Triton X-100
-
stimulates
Triton X-100
-
5.5fold increase in activity with membrane-bound phosphatidic acid
Triton X-100
-
the 45-kDa and 104-kDa enzyme forms are dependent on Triton X-100 for activity
Triton X-100
-
Triton X-100 or deoxycholate required
Triton X-100
-
plasma membrane-associated activity is absolutely dependent on detergent
Triton X-100
-
the 45000 Da enzyme form shows maximal activity at 5 mM
Triton X-100
-
activates by forming a mixed micelle with the lipid substrate PA, providing a membrane mimic for catalysis
Triton X-100
-
about 60% stimulation, optimum activity at 0.02%
Tween 20
-
increases hydrolysis of phosphatidate bound to microsomal membrane or phosphatidate in sonicated dispersion of organic solvent-disrupted microsomes, little effect on hydrolysis of phosphatidate dispersed in sonicated microsomal lipid
methyltrienolone
-
induces LPP1 expression
additional information
-
no effect on the enzyme forms by choline
-
additional information
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
treatment of HeLa cells with the epidermal growth factor leads to 3fold increased LPP-3 expression, while LPP-1 expression is unaffected, LPP-1 expression is increased in prostate adenocarcinoma cells treated with androgens
-
additional information
-
p73beta binding to DNA is essential for PAP2a expression
-
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
-
increasing the catalytic activity of LPP1 decreases the pertussis toxin-sensitive stimulation of fibroblast migration by lyso-phosphatidic acid and an lyso-phosphatidic acid-receptor agonist, that can not be dephosphorylated
-
additional information
Q91ZP3
fasting increases Mg2+-dependent PAP activity in livers from wild type animals by 2fold; insulin increases the phosphorylation of multiple sites e.g. at Ser106, insulin and epinephrine control lipin primarily by changing localization rather than intrinsic PAP activity, overview
-
additional information
Q8TBJ4
regulation of filopodia by LPR1 is not mediated by cdc42 or Rif, and is independent of the Arp2/3 complex
-
additional information
-
hyperactivated TORC2 enhances expression of lipin1. Diet-induced or genetic obesity increases LIPIN1 expression in mouse liver, and TORC2 is responsible for its transcriptional activation
-
additional information
-
hepatic lipin 2 protein content is markedly increased by lipin 1 deficiency, food deprivation, and obesity, often independent of changes in steady-state mRNA levels. Fasting induces expression of Lpin1 and Lpin2 in wild-type and PGC-1alpha-deficient mice
-
additional information
-
light regulation of the lipid phosphate phosphatases, overview
-
additional information
-
the enzyme expression is drought-stimulated. Transcripts accumulate in response to water deficit, including progressive dehydration of whole plants and rapid desiccation of detached leaves. The isozymes are not affected by wounding or by treatment with jasmonic acid
-
additional information
-
incubation with phospholipids or neutral lipids has no effect on the enzyme activity
-
additional information
-
is N-ethylmaleimide insensitive
-
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
0.5954
1,2-diacyl-sn-glycerol-3-phosphate
-
pH 6.5, 53C
0.0059
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate
-
pH 7.0, 37C
-
0.013
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
-
0.0051
1-myristoyl-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
0.0062
1-oleoyl-2-lyso-sn-glycerol 3-phosphate
-
pH 7.0, 37C
0.0069
1-oleoyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
0.003
1-palmitoyl-2-lyso-sn-glycerol 3-phosphate
-
pH 7.0, 37C
0.0064
1-stearoyl-2-lyso-sn-glycerol 3-phosphate
-
pH 7.0, 37C
-
0.0042
1-stearyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
-
0.024
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphate
-
pH 7.5, 37C, crude enzyme preparation
0.041
diacylglycerol diphosphate
Q5VZY2, Q8NEB5
pH 6.5, 37C, recombinant isozyme DPPL1
0.104
diacylglycerol diphosphate
Q5VZY2, Q8NEB5
pH 6.5, 37C, recombinant isozyme DPPL2
1.4
dioctanoyl phosphatidic acid
-
-
0.295
lysophosphatidic acid
Q5VZY2, Q8NEB5
pH 6.5, 37C, recombinant isozyme DPPL1
0.0054
phosphatidic acid
-
-
0.032
phosphatidic acid
-
enzyme form PAP2B
0.05
phosphatidic acid
-
-
0.05
phosphatidic acid
-
-
0.062
phosphatidic acid
-
-
0.08
phosphatidic acid
-
enzyme form PT
0.098
phosphatidic acid
-
in presence of various polyamines
0.1
phosphatidic acid
-
phosphatidate dispersed in sonicated microsomal lipid
0.14
phosphatidic acid
-
-
0.16
phosphatidic acid
-
enzyme forms D250 and E
0.16
phosphatidic acid
-
phosphatidate bound to microsomal membrane
0.16
phosphatidic acid
-
without polyamines
0.277
phosphatidic acid
Q5VZY2, Q8NEB5
pH 6.5, 37C, recombinant isozyme DPPL1
0.43
phosphatidic acid
-
wild type enzyme, pH and temperature not specified in the publication
0.506
phosphatidic acid
Q5VZY2, Q8NEB5
pH 6.5, 37C, recombinant isozyme DPPL2
0.67
phosphatidic acid
-
without ATP
0.67
phosphatidic acid
-
-
1.2
phosphatidic acid
-
in presence of 2 mM ATP
0.58
lysophosphatidic acid
Q5VZY2, Q8NEB5
pH 6.5, 37C, recombinant isozyme DPPL2
additional information
additional information
-
kinetic analysis, PA phosphatase activity on phosphatidate is cooperative
-
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
-
kinetics of the PAP1 activities of the three lipin proteins, surface dilution kinetic model using micelles of Triton X-100, each lipin exhibits a strong positive cooperativity for phosphatidic acid
-
additional information
additional information
-
kinetic model
-
additional information
additional information
A5HKK6
kinetics of the recombinant His6-tagged PAP2L2
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
250
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
-
354
1-myristoyl-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
177
1-oleoyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
125
1-stearyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20000
1-arachidonoyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
0
76000
1-myristoyl-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
90555
25000
1-oleoyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
160549
33000
1-stearyl-2-lyso-sn-glycerol 3-phosphate
P34913
pH 7.0, 30C
0
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+
-
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+
-
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+
-
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
-
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
-
at 30C, in 50 mM Tris-HCl buffer, pH 7.5, 1 mM MgCl2, and 0.2 mM substrate
2.5
Phenylglyoxal
-
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
-
at 30C, in 50 mM Tris-HCl buffer, pH 7.5, 1 mM MgCl2, and 0.2 mM substrate
7.17
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00035
-
LPP3 activity against FTY720-P
0.00285
-
LPP3 activity against sphingosine 1-phosphate
0.1175
-
-
1.4
-
recombinant vacuole membranes of intact vacuoles from overexpressing transgenic mutant DTY1
5.2
-
pure enzyme, radioactive assay
5.6
-
pure enzyme, colorimetric assay
7
-
recombinant vacuole membranes of Triton X-100-ruptured vacuoles from overexpressing transgenic mutant DTY1
15.8
-
-
33.3
A5HKK6
purified recombinant His6-tagged PAP2L2
312
-
pH 6.5, 53C
additional information
-
-
additional information
-
enzyme assay
additional information
-
recombinant activity of wild-type and mutant enzymes in transformed cells
additional information
-
recombinant wild-type and mutant PAH1, assay in presence of Triton X-100 at 2 mM
additional information
-
-
additional information
-
development of a HPLC-fluorescence detection method, overview
additional information
-
expression levels in uteri and livers of nondiabetic C57BL6 and CD-1 mice, and diabetic NOD mice and Pd-NOD mice, overview
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
enzyme associated with the protein bodies
5
-
assay at, with substrate lysophosphatidic acid
5.1
-
cytosolic enzyme
5.6
-
enzyme from particulate fraction
6 - 6.5
-
and the major activity peak at pH 7.5-8.0, aqueously dispersed phosphatidic acid, cytosolic activity
6 - 7
-
45-kDa enzyme form
6 - 7
-
45000 Da enzyme form
6 - 8
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
isozyme LPPgamma, broad optimum
6
-
phosphatidic acid mixed with phosphatidylcholine, PAP-2
6.5 - 7.5
-
membrane-bound phosphatidic acid, microsomal enzyme
6.5
-
and a minor peak of activity at pH 7.5-8, aqueously dispersed phosphatidic acid, microsomal enzyme
6.5
-
pure phosphatidic acid, PAP-2
6.5
-
assay at
6.5
Q5VZY2, Q8NEB5
assay at; assay at
6.5
-
assay at
6.5
-
assay at
6.5
-
assay at
7 - 7.4
-
-
7 - 8
-
75-kDa enzyme form
7
-
104-kDa enzyme form
7
-
reaction with diacylglycerol diphosphate or lysophosphatidate
7
Q91ZP3
assay at
7
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
isozyme LPPepsilon1; isozyme LPPepsilon2
7
-
assay at
7
-
assay at
7.1
-
assay at
7.4 - 7.6
-
-
7.4 - 8
-
membrane-bound phosphatidic acid, cytosolic enzyme
7.5 - 8
-
and a distinct optimum at pH 6.0-6.5, aqueously dispersed phosphatidic acid, cytosolic enzyme
7.5
-
-
7.5
-
enzyme from endoplasmic reticumum
7.5
-
reaction with phosphatidic acid
7.5
-
assay at
7.5
-
assay at, with substrate phosphatidic acid
7.5
-
assay at
7.5
-
assay at
7.5
A5HKK6
assay at
8
-
dephosphorylation of phosphatidic acid and p-nitrophenyl phosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
isozyme LPPepsilon1; isozyme LPPepsilon2; isozyme LPPgamma
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
6 - 8
-
pH 6.0: about 40% of maximal activity, pH 8.0: about 25% of maximal activity
7 - 9
-
pH 7.0: 83% of maximal activity, pH 9.0: about 36% of maximal activity
7.2 - 8.2
-
pH 7.2: 76% of maximal activity, pH 8.2: 74% of maximal activity
7.5 - 10
-
pH 7.5: about 30% of maximal activity, pH 10.0: about 25% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
30
Q91ZP3
assay at
30
-
assay at
30
-
assay at
30
-
assay at
37
-
assay at
37
Q5VZY2, Q8NEB5
assay at; assay at
37
-
assay at
37
-
assay at
37
-
assay at
65
A5HKK6
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
lipin-1 and lipin-2
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
-
Manually annotated by BRENDA team
-
lipin-1 accounts for all of the PAP1 activity in adipose tissue and skeletal muscle
Manually annotated by BRENDA team
-
PAP1 activity increases during adipogenesis
Manually annotated by BRENDA team
-
lipin-2, in circulating red blood cells, at ca. 10% of the levels observed in liver
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
synovium containing, specific expression of DPPL2
Manually annotated by BRENDA team
-
low levels of lipin-2, in bone and bone marrow, at 1020% the levels in liver
Manually annotated by BRENDA team
-
isozyme LPP2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-2 predominantly
Manually annotated by BRENDA team
Q91ZP3
fatty liver dystrophy mice contain dramatically lower levels of Mg2+-dependent PAP activity than wild-type mice
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
isozyme DPPL2
Manually annotated by BRENDA team
-
lipin-1, whereas lipin-1alpha is the predominant form
Manually annotated by BRENDA team
-
lipin-2, in the cortex, hippocampus, thalamus, and hypothalamus
Manually annotated by BRENDA team
-
lipin-1gamma is the main isoform in the brain
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
lipin-2, in the cortex, hippocampus, thalamus, and hypothalamus
-
Manually annotated by BRENDA team
-
isozyme PAP1 in all subcellular fractions, isozyme PAP2 in cytosol
Manually annotated by BRENDA team
-
developing cotyledon
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
lipin-2
-
Manually annotated by BRENDA team
-
ectopic expression
Manually annotated by BRENDA team
-
expression pattern of Wun and Wun2 during embryogenesis
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
isozyme DPPL2
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
specific expression of DPPL2, expression in endothelial cell lines, overview
Manually annotated by BRENDA team
-
rod outer segment
Manually annotated by BRENDA team
-
embryonic, derived from LPP-1 overexpression mutant and wild-type mice
Manually annotated by BRENDA team
-
immortalized cell line
Manually annotated by BRENDA team
-
PAPalpha and PAPbeta
Manually annotated by BRENDA team
-
primary bronchial epithelial cells
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-1a predominantly
Manually annotated by BRENDA team
-
approximately fourfold higher in ventricular myocardium than in atrial tissue
Manually annotated by BRENDA team
Q91ZP3
fatty liver dystrophy mice contain dramatically lower levels of Mg2+-dependent PAP activity than wild-type mice
Manually annotated by BRENDA team
-
ventricular and atrial tissue, isozyme PAP-2, ventricular and atrial tissue, isozymes PAP-1 and PAP-2
Manually annotated by BRENDA team
-
presence of lipin-1 and lipin-3, lipin-2 is absent. Marked differences in cardiac distribution of PAP1
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
-
Manually annotated by BRENDA team
-
epithelial differentiation of intestinal mucosa leads to increased Dri-42/LPP-3 expression
Manually annotated by BRENDA team
-
lipin-2, epithelial cell layer
Manually annotated by BRENDA team
-
isozyme LPP2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-1 predominantly
Manually annotated by BRENDA team
Q91ZP3
fatty liver dystrophy mice contain dramatically lower levels of Mg2+-dependent PAP activity than wild-type mice
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
isozyme DPPL2
Manually annotated by BRENDA team
-
lipin-2, in the cortex, medulla, and papillae
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
lipin-2, in the cortex, medulla, and papillae
-
Manually annotated by BRENDA team
-
PAPalpha and PAPbeta
Manually annotated by BRENDA team
-
polymorphonuclear
Manually annotated by BRENDA team
-
peripheral blood
Manually annotated by BRENDA team
-
isozyme LPP2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-1 predominantly
Manually annotated by BRENDA team
Q91ZP3
fatty liver dystrophy, Mg2+-dependent PAP activity from fatty liver dystrophy mice is approximately half of that measured in wild-type
Manually annotated by BRENDA team
-
expression of both splicing variants of lipin-1
Manually annotated by BRENDA team
-
lipin-1 and high activity of lipin-2
Manually annotated by BRENDA team
-
lipin 2 is enriched in fatty liver dystrophic (fld) mice, whereas lipin 1 and lipin 3 protein is absent
Manually annotated by BRENDA team
-
lipin-2, shows a uniform distribution pattern
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
lipin-2, shows a uniform distribution pattern
-
Manually annotated by BRENDA team
-
fetal and adult
Manually annotated by BRENDA team
-
endothelial cell
Manually annotated by BRENDA team
-
isozyme LPP2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-1 predominantly
Manually annotated by BRENDA team
Q91ZP3
fatty liver dystrophy mice contain dramatically lower levels of Mg2+-dependent PAP activity than wild-type mice
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
-
Manually annotated by BRENDA team
-
Madine-Darby kidney cell line
Manually annotated by BRENDA team
-
embryonic fibroblast cell line
Manually annotated by BRENDA team
-
highest level of lipin-1
Manually annotated by BRENDA team
B7STY8
longissimus dorsi muscle, lipin1 gene and its isoforms
Manually annotated by BRENDA team
-
isozyme PAP-2, isozymes PAP-1 and PAP-2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
expression of PRG-1
Manually annotated by BRENDA team
-
shows reduced LPP1 activity
Manually annotated by BRENDA team
-
isozyme LPP2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-2 predominantly
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
-
Manually annotated by BRENDA team
-
U937, THP-1 and MonoMac
Manually annotated by BRENDA team
-
isozyme LPP2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-1 predominantly
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-2 predominantly
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
specific expression of DPPL2
Manually annotated by BRENDA team
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
LPP-1
Manually annotated by BRENDA team
-
isoenzyme PAP2a
Manually annotated by BRENDA team
-
rod outer segment
Manually annotated by BRENDA team
-
PAPalpha and PAPbeta
Manually annotated by BRENDA team
-
lipin-2, submandibular and submaxillary salivary glands
Manually annotated by BRENDA team
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
high expression of isozyme LPPgamma
Manually annotated by BRENDA team
Q91ZP3
fatty liver dystrophy mice contain dramatically lower levels of Mg2+-dependent PAP activity than wild-type mice
Manually annotated by BRENDA team
-
lipin-1 accounts for all of the PAP1 activity in adipose tissue and skeletal muscle
Manually annotated by BRENDA team
-
low levels of lipin-1, whereas lipin-2 is absent
Manually annotated by BRENDA team
-
lipin-2, in whole spleen and the white blood cell fraction of spleen, at ca. 10% of the levels observed in liver
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
lipin-2, in whole spleen and the white blood cell fraction of spleen, at ca. 10% of the levels observed in liver
-
Manually annotated by BRENDA team
-
PAPalpha and PAPbeta
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
specific expression of DPPL2
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
isozyme DPPL2
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
-
Manually annotated by BRENDA team
-
lipin-2, in squamous keratinized epithelium
Manually annotated by BRENDA team
-
promonocytic leukemia macrophage cell line
Manually annotated by BRENDA team
-
predominantly in the glandular and luminal epithelium, apical region, overview
Manually annotated by BRENDA team
Q5VZY2, Q8NEB5
-
Manually annotated by BRENDA team
additional information
-
tissue distribution
Manually annotated by BRENDA team
additional information
-
isoenzyme PAP-2b is almost ubiquitously in all human tissues, isoenzyme PAP-2a is undetectable in thymus, placenta and leukocytes
Manually annotated by BRENDA team
additional information
-
expression pattern and translocation of Wun and Wun2 during gut development
Manually annotated by BRENDA team
additional information
-
isozymes LPP1 and LPP3 show a wide tissue distribution
Manually annotated by BRENDA team
additional information
-
the expression of LPP1-3 is reduced upon preadipocyte differentiation to adipocytes
Manually annotated by BRENDA team
additional information
-
tissue distribution of PAP2d expression, no expression of PAP2d in leukocytes, small intestine, prostate, ovary, thymus, splen, pancreas, liver, and heart
Manually annotated by BRENDA team
additional information
Q5VZY2, Q8NEB5
DPPL1 is ubiquitously expressed in various tissues and cells, overview
Manually annotated by BRENDA team
additional information
Q5VZY2, Q8NEB5
DPPL2 mRNA is restricted to several tissues, expression in cancer cell lines, overview
Manually annotated by BRENDA team
additional information
-
Swiss 3T3 cell
Manually annotated by BRENDA team
additional information
-
tissue expression patterns of lipin isozymes, overview, lipin-1 is responsible for PAP1 activity in adipose tissue and skeletal muscle
Manually annotated by BRENDA team
additional information
-
expression of isozymes PAPalpha and PAPbeta in several cowpea organs
Manually annotated by BRENDA team
additional information
-
tissue-dependent regulation of PAP1, overview
Manually annotated by BRENDA team
additional information
-
atrial tissue
Manually annotated by BRENDA team
additional information
-
triceps muscle
Manually annotated by BRENDA team
additional information
-
visceral adipose tissue
Manually annotated by BRENDA team
additional information
-
isoform lipin-1gamma is not detected in skeletal muscle, liver and small intestine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated with envelope membranes
Manually annotated by BRENDA team
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
the homolog of cyanobacterial LPP, isozyme LPPepsilon1, is localized to chloroplasts and contains a plastidic transit peptide
Manually annotated by BRENDA team
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
the homolog of cyanobacterial LPP, isozyme LPPepsilon2, is localized to chloroplasts and contains a plastidic transit peptide
Manually annotated by BRENDA team
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
the homolog of cyanobacterial LPP, isozyme LPPgamma, is localized to chloroplasts and contains a plastidic transit peptide
Manually annotated by BRENDA team
-
isozye PAPalpha contains an N-terminal transit peptide
Manually annotated by BRENDA team
-
majority of lipin 2
Manually annotated by BRENDA team
-
translocates onto the cytosolic side of intracellular membranes
Manually annotated by BRENDA team
-
multiple forms: PT, D150, D250 and E
Manually annotated by BRENDA team
-
cytosolic and particulate enzyme form
Manually annotated by BRENDA team
-
the largest portion of the activity is localized in the soluble fraction
Manually annotated by BRENDA team
-
Mg2+-dependent enzyme form is mainly located in cytosol and microsomes
Manually annotated by BRENDA team
-
20% of the activity
Manually annotated by BRENDA team
Q91ZP3
the less phosphorylated enzyme forms are located in the cytosol
Manually annotated by BRENDA team
-
lipin-1 and lipin-2 are soluble proteins that can also be localized to the nucleus or associate with endoplasmic reticulum membranes
Manually annotated by BRENDA team
-
the phosphorylated forms of lipins 1 and 2 in HeLa cells and adipocytes are enriched in the cytosolic fraction, whereas the dephosphorylated forms are enriched in the membrane fraction
Manually annotated by BRENDA team
-
wild-type and lipin-2 are present at similar levels in cytosolic and membrane fractions in the absence of oleate
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
wild-type and lipin-2 are present at similar levels in cytosolic and membrane fractions in the absence of oleate
-
Manually annotated by BRENDA team
-
the enzyme binds to the cytosolic side of the membranes, overview
Manually annotated by BRENDA team
-
lipin-1 and lipin-2 are soluble proteins that can also be localized to the nucleus or associate with endoplasmic reticulum membranes
Manually annotated by BRENDA team
-
the enzyme active site exposed to the cytosolic side of the membrane
Manually annotated by BRENDA team
-
early stage, wild-type and mutant
Manually annotated by BRENDA team
-
CHAPS-resistant complexes containing LPP1
Manually annotated by BRENDA team
-
the cationic and the anionic enzyme form are integral membrane proteins
-
Manually annotated by BRENDA team
Acholeplasma laidlawii A
-
-
-
-
Manually annotated by BRENDA team
-
associated with
Manually annotated by BRENDA team
-
lipin-1gamma partially translocates from subcellular membranes to lipid droplets upon fatty acid loading
-
Manually annotated by BRENDA team
-
only 3% of the total activity
Manually annotated by BRENDA team
-
integral membrane protein
Manually annotated by BRENDA team
-
cell surface membrane, PAP-2b acts at the outer leaflet of cell surface bilayers
Manually annotated by BRENDA team
-
two membrane-associated forms, 45000 Da and 104000 Da, of the Mg2+-dependent phosphatidate phosphatase
Manually annotated by BRENDA team
-
isozyme PAP1, PAP2s are integral membrane proteins
Manually annotated by BRENDA team
-
lipid phosphate phosphatase enzymes possess a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
Manually annotated by BRENDA team
-
LPP1 and LPP3 are distributed in distinct lipid rafts that may provide unique microenvironments defining their non-redundant physiological functions. LPP1 is associated with rafts, which are segregated from those harboring LPP3, in a Triton-100-sensitive but CHAPS-resistant manner
Manually annotated by BRENDA team
Q91ZP3
the more phosphorylated enzyme forms are associated to membranes
Manually annotated by BRENDA team
-
bound to microsomal and plasma membranes
Manually annotated by BRENDA team
A5HKK6
six-transmembrane topology
Manually annotated by BRENDA team
-
the phosphorylated forms of lipins 1 and 2 in HeLa cells and adipocytes are enriched in the cytosolic fraction, whereas the dephosphorylated forms are enriched in the membrane fraction
Manually annotated by BRENDA team
-
LPPs are integral membrane proteins with six transmembrane domains
Manually annotated by BRENDA team
-
wild-type and lipin-2 are present at similar levels in cytosolic and membrane fractions in the absence of oleate, and it translocates to the membrane fraction with increasing levels of oleate
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
the active site of the enzyme is on the outer surface of plasma membranes, or the lumenal surface of internal membranes
Manually annotated by BRENDA team
Geobacillus toebii T-85
-
six-transmembrane topology
-
Manually annotated by BRENDA team
Streptomyces coelicolor ATCC BAA-471
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
wild-type and lipin-2 are present at similar levels in cytosolic and membrane fractions in the absence of oleate, and it translocates to the membrane fraction with increasing levels of oleate
-
Manually annotated by BRENDA team
-
Mg2+-dependent enzyme form is mainly located in cytosol and microsomes. The Mg2+-independent enzyme is mainly located in plasma membrane, mitochondria and microsomes
-
Manually annotated by BRENDA team
-
45-kDA enzyme form and 104-kDA enzyme form
-
Manually annotated by BRENDA team
-
the Mg2+-independent enzyme is mainly located in plasma membrane, mitochondria and microsomes
Manually annotated by BRENDA team
-
the transcriptional coactivator function of lipin1beta necessarily requires localization in the nucleus
Manually annotated by BRENDA team
Saccharomyces cerevisiae W303-1A
-
-
-
Manually annotated by BRENDA team
-
the Mg2+-independent enzyme is mainly located in plasma membrane, mitochondria and microsomes
Manually annotated by BRENDA team
-
associated with disk membrane, photoreceptor membrane of bovine retina
Manually annotated by BRENDA team
-
active site located on the outer surface
Manually annotated by BRENDA team
-
isozyme LPP-1, containing the apical sorting signal FDKTRL, is mainly located at the apical surface membrane, while isozyme LPP-3 is located at the basolateral membrane being targeted by the dityrosine motif in the second cytoplasmic portion
Manually annotated by BRENDA team
-
outside surface, ecto-enzyme
Manually annotated by BRENDA team
-
the enzymes act on the cytoplasmic and the cell surface side of the membrane
Manually annotated by BRENDA team
-
the enzymes act on the cytoplasmic and the cell surface side of the membrane, isozyme LPP1 is located at the apical membrane, isozyme LPP3 is located at the basolateral membrane
Manually annotated by BRENDA team
-
the isozyme LPP-1 is partly expressed in the plama membrane with its C-terminal end located on the cell surface
Manually annotated by BRENDA team
Q8TBJ4
LPR1 is predominantly distributed uniformly along shafts of protrusions, with an occasional enrichment at their tips. LPR1 may be an integral membrane protein link between the actin core and the surrounding lipid layer of a nascent filopodium. LPP3 does not show these types of membrane protrusions
Manually annotated by BRENDA team
-
wild-type and mutant
Manually annotated by BRENDA team
Acholeplasma laidlawii A
-
-
-
Manually annotated by BRENDA team
-
PAH1 and PAH2
-
Manually annotated by BRENDA team
-
associated, the enzyme contains six putative transmembrane domains, the catalytic site is oriented to the cytosolic face of the vacuole membrane
Manually annotated by BRENDA team
Saccharomyces cerevisiae W303-1A
-
associated, the enzyme contains six putative transmembrane domains, the catalytic site is oriented to the cytosolic face of the vacuole membrane
-
Manually annotated by BRENDA team
additional information
-
cytosolic and particulate enzyme form
-
Manually annotated by BRENDA team
additional information
-
post-Golgi localization
-
Manually annotated by BRENDA team
additional information
-
the majority of the activity is localized in particulate fraction
-
Manually annotated by BRENDA team
additional information
-
isozyme PAP1 is located in all subcellular compartments, alterations in isozymes content in different subcellular compartments during aging, comparison of subcellular distribution in adult and aged rat cerebellum, overview
-
Manually annotated by BRENDA team
additional information
-
the enzyme also hydrolyses extracellularly located substrates
-
Manually annotated by BRENDA team
additional information
-
the enzymes act intra- and extracellularly
-
Manually annotated by BRENDA team
additional information
-
the enzymes act intra- and extracellularly
-
Manually annotated by BRENDA team
additional information
-
the enzymes act intra- and extracellularly
-
Manually annotated by BRENDA team
additional information
-
the enzymes act intra- and extracellularly, the subcellular localization influences the physiological role of the isozymes
-
Manually annotated by BRENDA team
additional information
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
isozyme LPPbeta contains no plastidic transit peptide
-
Manually annotated by BRENDA team
additional information
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
isozyme LPPdelta contains no plastidic transit peptide
-
Manually annotated by BRENDA team
additional information
-
LLP2 is not localized in Golgi apparatus, mitochondria, nucleus, or nuclear membrane, not localized to the Golgi apparatus, mitochondria, nucleus, or nuclear membrane
-
Manually annotated by BRENDA team
additional information
-
the NLS sequences govern nuclear localization of lipin-1alpha and determine its membrane association and physiological function
-
Manually annotated by BRENDA team
additional information
-
20% of transfected 3T3-L1 adipocyte cells contain lipin-1alpha exclusively in the nucleus, in more than 50% of cells lipin-1alpha is present in similar amounts in the cytoplasm and the nucleus. 14-3-3 proteins promote cytoplasmic localization of lipin-1alpha
-
Manually annotated by BRENDA team
additional information
-
in confluent endothelial cells, a fraction of p120-catenin associates and colocalizes with LPP3 at the plasma membrane, via the C-terminal cytoplasmic domain, thereby limiting the ability of LPP3 to stimulate beta-catenin/lymphoid enhancer binding factor 1 signaling
-
Manually annotated by BRENDA team
additional information
-
in embryonic cortical neurons, lipin-1beta shows exclusively cytoplasmic localization. In SH-SY5Y clones, ectopic lipin-1a exhibits both nuclear and cytosolic localization, with a higher concentration in the nucleus, whereas lipin-1alpha is concentrated in the cytoplasm in HEK-93A cells. Sumoylation facilitates the nuclear localization and transcriptional coactivator behavior of lipin-1alpha in embryonic cortical neurons
-
Manually annotated by BRENDA team
additional information
-
LPP1 and LPP3 are present in caveolae, localised to distinct lipid rafts
-
Manually annotated by BRENDA team
additional information
-
Myc-gpLPP1-FLAG-LPP2, FLAG-gpLPP1-Myc-LPP3 and Myc-LPP2-FLAG-LPP3 are co-localized at the plasma membrane and in a perinuclear region of HEK-293 cells
-
Manually annotated by BRENDA team
additional information
-
Myc-LPP1-FLAG-hLPP2 and FLAG-LPP1-Myc-hLPP3 are co-localized at the plasma membrane and in a perinuclear region of HEK-293 cells
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
Q91ZP3
NH2-terminal region, including the conserved NLIP domain present, immunoprecipitation
680814
35000
Q8TBJ4
LPR1, Western blot analysis
681013
37000
-
gel filtration
134895
38000
Q8TBJ4
LPR1, Western blot analysis
681013
45000
Q91ZP3
conserved CLIP domain present, immunoprecipitation
680814
53000 - 83000
-
-
666926
60000
-
immunoprecipitation, band only visible at mRNA overexpression levels of 100fold or more
680744
75000
-
gel filtration
134866
75000
-
cytosolic enzyme form, gel filtration
134878
101000
-
PAH1 and PAH2, calculated from sequence
710418
140000
-
Western blotting
709417
218000
-
gel filtration
134886
265000
-
native PAGE
134896
290000 - 300000
-
gel filtration
134896
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q9EWX3, Q9K3P6
x * 27000, SDS-PAGE
?
-
x * 25000, SDS-PAGE
?
Q9EWX3, Q9K3P6
x * 40000, SDS-PAGE
?
-
x * 38000-40000, SDS-PAGE
?
-
x * 32158, isoenzyme PAP-2a, calculation from nucleotide sequence
?
-
x * 51000, cationic enzyme form, SDS-PAGE
?
-
x * 35119, isoenzyme PAP-2b, calculation from nucleotide sequence
?
-
x * 38000, enzyme form PAP2B, SDS-PAGE
?
-
x * 45000-52000, SDS-PAGE
?
-
x * 83000, SDS-PAGE under reducing and nonreducing conditions
?
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
x * 23371, isozyme LPPdelta, sequence calculation
?
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
x * 25736, isozyme LPPgamma, sequence calculation
?
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
x * 30578, isozyme LPPepsilon1, sequence calculation
?
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
x * 31512, isozyme LPPepsilon2, sequence calculation
?
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
?
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
x * 46151, isozyme LPPdelta, sequence calculation
?
-
x * 31000-36000, recombinant Myc-tagged and/or FLAG-tagged LPP1 or LLP3, SDS-PAGE
?
-
x * 32400, recombinant PA-PSP, SDS-PAGE
?
-
x * 31000 + x * 34500 + x * 35000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP1
?
-
x * 32000 + x * 34000, Western blot analysis, LPP3. X * 33000 , Western blot analysis, LPP2
?
-
x * 33000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP2. x * 32000 + x * 34000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP3
?
Acholeplasma laidlawii A
-
x * 25000, SDS-PAGE
-
?
Streptomyces coelicolor ATCC BAA-471
-
x * 40000, SDS-PAGE, x * 27000, SDS-PAGE
-
dimer
-
dimerization is not essential for catalytic activity, the enzyme also forms higher complexes, which is not required for activity in vitro or in vivo, but does confer structural stability
dimer
-
Wunen forms homodimers
dimer
-
catalytic activity is required for dimerisation
hexamer
-
-
monomer
-
1 * 95000, about, PAH1, sequence calculation, 1 * 124000, PAH1, SDS-PAGE
additional information
-
the LPPs contain three conserved active site domains and six conserved transmembrane domains
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
-
LPP1 monomers might exist in equilibrium with oligomeric LPP1, the LPP1 monomer is inactive, endogenous LPP2 and LPP3 form a complex
additional information
-
PAP1 activity is conferred by the DxDxT motif of the C-Lip domain contained in all lipin family members
additional information
-
the isozymes PAPalpha and PAPbeta contain the six transmembrane regions and the consensus sequences corresponding to the catalytic domain of the phosphatase family
additional information
Saccharomyces cerevisiae W303-1A
-
the enzyme has six putative transmembrane domains and a hydrophilic region that contains a phosphatase motif required for its catalytic activity, membrane topology, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
-
glycoprotein
-
N-glycosylation
glycoprotein
-
the two Mg2+-independent isoenzymes, PAP-2a and PAP-2b are glycoproteins
glycoprotein
-
N-glycosylation
glycoprotein
-
the glycosylation is not required for catalytic activity, no glycosylation of PRG-1
phosphoprotein
-
reversible phosphorylation might play a role in enzyme regulation
phosphoprotein
-
mitotic phosphorylation of lipin 1 inhibits its phosphatidic acid phosphatase activity
phosphoprotein
-
phosphorylation play an important role in modulation of enzyme activity, phosphorylation of lipin-1 influences its subcellular localization, dephosphorylation of lipin-1 in response to oleic acid and epinephrine
phosphoprotein
-
insulin-stimulated phosphorylation sites in lipin-1 are at Ser106, Ser634, and Ser720
sumoylation
-
isoforms lipin-1alpha and lipin-1beta undergo sumoylation on two consensus sumoylation sites
glycoprotein
-
N-glycosylation
glycoprotein
-
glycosylation is not required for activity
glycoprotein
-
the glycosylation is not required for catalytic activity, no glycosylation of PRG-1
phosphoprotein
-
reversible phosphorylation might play a role in enzyme regulation
phosphoprotein
Q91ZP3
identification of fifteen phosphorylation sites by mass spectrometric analysis
phosphoprotein
-
mitotic phosphorylation of lipin 2 inhibits its phosphatidic acid phosphatase activity
phosphoprotein
-
phosphorylation plays an important role in modulation of enzyme activity, phosphorylation of lipin-1 and lipin-2 is associated with reduced PAP1 activity druing mitosis, phosphorylation of lipin-1, mainly at Ser106, influences its subcellular localization, dephosphorylation of lipin-1 in response to oleic acid and epinephrine
phosphoprotein
-
serine 106 residue of lipin-1 and lipin-2 is a major site of phosphorylation
phosphoprotein
-
insulin-stimulated phosphorylation sites in lipin-1 are at Ser106, Ser634, and Ser720
sumoylation
-
isoforms lipin-1alpha and lipin-1beta undergo sumoylation on two consensus sumoylation sites
glycoprotein
-
the anionic and the cationic enzyme form are glycoproteins
glycoprotein
-
N-glycosylation
glycoprotein
-
the glycosylation is not required for catalytic activity, no glycosylation of PRG-1
phosphoprotein
-
reversible phosphorylation might play a role in enzyme regulation
phosphoprotein
-
phosphorylation plays an important role in modulation of enzyme activity, phosphorylation of lipin-1 influences its subcellular localization, dephosphorylation of lipin-1 in response to oleic acid and epinephrine
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
-
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
-
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
inhibition of the 45-kDa and 104-kDa enzyme forms, unstable above
134878
30
-
45000 Da enzyme form, unstable above
134892
50
-
45000 Da enzyme form, complete inactivation after 20 min
134892
55
-
10 min, over 80% of the Mg2+-dependent activity is lost durring incubation of cytosol and microsomal fractions, the Mg2+-independent enzyme is stable
134867
55
-
20 min, 70% loss of activity with membrane-bound phosphatidic acid, 24% loss of activity with aqueously dispersed phosphatidic acid
134872
55
-
activity of PAP-2 is not seriously affected after 20 min
651209
60
A5HKK6
30 min, 50% remaining activity
691384
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, activity in cytosolic fraction is stable for at least two months
-
-80C, stable for at least 1 month
-
-80C, 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
chloroplast preparation from native and transgenic plants; chloroplast preparation from native and transgenic plants; chloroplast preparation from native and transgenic plants
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
Ni-NTA column chromatography
-
recombinant His6-tagged PAP2L2 18.4fold from Escherichia coli by solubilization using 0.3% v/v Triton X-100, and nickel affinity chromatography
A5HKK6
recombinant His-tagged lipin from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant LPP3 from Drosophila melanogaster cells S2 by immunoaffinity
-
recombinant LPP1 from Drosophila melanogaster cells S2 by immunoaffinity
-
V5-tagged proteins immunopurified
-
a cationic and an anionic enzyme form
-
from liver
-
two forms of PAP2: PAP2A and PAP2B
-
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; partial
-
45000 Da enzyme form and 104000 Da enzyme form
-
preparation of vacuoles
-
PtA fusion affinity purification
-
recombinant His-tagged wild-type and mutant isozyme PAH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-DE3(pLysS) cells
-
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
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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
Q0WUC2, Q6NLA5, Q6NQL6, Q9SUW4
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
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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
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gene laza, genetic structure and organiszation, expression analysis and pathway regulation, overview
-
genomic library screening, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His6-tagged PAP2L2 in Escherichia coli
A5HKK6
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
-
expressed either as untagged proteins or as Flag- or EGFP-tagged enzymes in HUVEC cells or in HEK-293 cells
-
expressed in HEK293 cells as a green fluorescent fusion protein
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expressed in P-388D1 cells
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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 isozyme DPPL1 in Spodoptera frugiperda Sf9 cells; expression of isozyme DPPL2 in Spodoptera frugiperda Sf9 cells
Q5VZY2, Q8NEB5
expression of lipin-1 in HeLa M cells
-
expression of myc-tagged wild-type human and mouse LPP-1 isozyme or Myc-tagged human and mouse LPP-1 mutant R217K in primary bronchial epithelial cells
-
expression of PAP2a in Saos-2 cells, promoter determination and anaylsis, expression in HEK-293T cells, expression regulation anaylsis, overview
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expression of presqualene diphosphate phosphatase in COS-7 cells, co-expression with CTP:phosphocholine cytidylyltransferase-alpha
-
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
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functional overexpression of GFP-tagged LPPs in rat2 fibroblasts, the transformed cells show reduced proliferation, overview; rat2 fibroblasts transduced and overexpressed with LPP2, LPP2-GFP and mutant LPP2(R214K)-GFP
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gene LPIN2 is located on chromosome 18p11
-
LPIN1 reporter plasmid transiently transfected into Hep-G2 cells
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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
Q8TBJ4
LPP1, LPP2 and LPP3
-
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
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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
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overexpression of LPP-3 in HEK293 cells and in Xenopus laevis dorsal blastomeres of embryos causing a mild ventralizing effect
Q6T4P5, Q7Z2D5, Q8TBJ4, Q96GM1
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
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overexpression of LPPs in HEK293 cells, expression of LPP3 in Drosophila melanogaster cells S2
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separate overexpression of isozymes LPP1, LPP2, or LPP3 in HEK-293 cells reducing lysophosphatidic acid-stimulated p42/p44 MAPK activation
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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
Q32ZL2
transient and stable overexpression in HEK-293 cells, baculovirus vectors for recombinant expression of LPPs in cultured Sf9 cells
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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
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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
-
expression analysis of lipin-1 and lipin-2, recombinant expression of lipin-2 in Hep-G2 cells using an adenoviral vector
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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
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expression of Myc-tagged and/or FLAG-tagged LPP1, LLP2, and LLP3 in HEK-293 cells, overview
-
expression of myc-tagged wild-type LPP-1 isozyme or Myc-tagged recombinant LPP-1 mutant R217K in human primary bronchial epithelial cells
-
expression of the gene encoding the enzyme under control of chicken beta-actin promoter in mice embryos
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expression of wild-type and mutant enzymes in rat2 fibroblasts
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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
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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
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gene Lpp1, stable overexpression of wild-type and mutant LPP1 enzymes in Rat2 fibroblasts using a retroviral vector and puromycin selection
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genes Lpin1, Lpin2, and Lpin3, expression analysis reveals distinct gene regulation in the hepatocytes
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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
Q91ZP3
HEK293 cells or 3T3-L1 adipocytes transfected with wild-type or mutant lipin-1alpha lacking the serine-rich domain
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lipin-1 adenovirus overexpression
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overexpression in HEK-293 cells
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rat2 fibroblasts transduced and overexpressed with LPP1 and mLPP1-GFP
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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
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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
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wild-type transfected inot human dermal microvascular endothelial cells
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genes Lpin1, Lpin2, and Lpin3, expression analysis reveals distinct gene regulation in the hepatocytes
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overexpression of isozyme LPP1 in Rat2 fibroblasts
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rat2 fibroblasts infected with adenoviral vectors containing LPP1-myc or LPP1(R217K)-myc. Rat2 fibroblasts stably overexpressing LPP1
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rat2 fibroblasts transduced and overexpressed with LPP3-GFP or myc-LPP3
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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
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expression in Escherichia coli
Q0SKM5
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
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gene PAH1, expression in Escherichia coli
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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
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overexpression in Sf-9 insect cells
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overexpression in Spodoptera frugiperda Sf9 cells using the baculovirus expression system, and in Saccharomyces cerevisiae using multicopy plasmids
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subcloning and expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha and BL21(DE3)
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expression in Escherichia coli; expression in Escherichia coli
Q9EWX3, Q9K3P6
full-length of the cDNA of lipin1
B7STY8
genes VuPAPalpha and VuPAPbeta, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of VuPAPalpha in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
homozygous T-DNA-tagged mutants of PAH1 and PAH2 do not express their respective full-length mRNAs
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LPP2 expression is down-regulated by abscisic acid (0.01 mM)
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LPP3 expression is up-regulated by abscisic acid (0.01 mM)
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lysophosphatidic acid phosphatase is highly expressed during phosphate starvation, cab leaf virus infection, and abiotic stresses (heat, syringolin, bamacia tabaci)
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downregulation of LPIN-1 by RNAi
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RNAi downregulation of lpin-1
Q9XXT5
Wunens are normally expressed in somatic tissues that germ cells avoid
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atrial lipin-1 and lipin-3 mRNA expression in diabetic patients is 50% and 59% lower as in non-diabetic patients, respectively
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in polycystic ovary syndrome patients, lipin 1beta expression in subcutaneous and visceral adipose tissue depots is lower than in controls. In polycystic ovary syndrome patients, visceral adipose lipin 1beta expression correlates negatively with homeostasis model assessment-insulin resistance, body mass index and waist circumference. Subcutaneous lipin 1beta expression in polycystic ovary syndrome patients correlates negatively with body mass index, waist circumference and plasma triglycerides
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LPIN1 mRNA levels decrease significantly after transfection with LPIN1 siRNA. LPIN1 mRNA levels are reduced to ca. 0.6fold after transfection with SREBP-1 siRNA
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hepatic lipin-1 expression is selectively repressed by insulin
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expression of lipin 1beta in viscera adipose tissue does not correlate with PPARG, LPL, LIPE, adiponectin and SLC2A4 gene expression
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lipin-1 gene expression is regulated in a glucocorticoid receptor-dependent manner
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LPIN1 mRNA does not change in cells transfected with SREBP-2 siRNA. Both the sterol regulatory element and the nuclear factor Y-binding site are important in the regulation of LPIN1 transcription
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epidermal growth factor increases LPP3 mRNA in HeLa cells. Androgen increases LPP1 mRNA in adenocarcinoma cells
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insulin therapy increases both PAP1 activity and lipin mRNA expression in diabetic patients
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lipin1 is induced in the late stages of adipocyte differentiation. During the maturation of adipocytes, the increase of lipin1alpha is less than that of lipin1beta. CCAAT/enhancer-binding protein alpha directly controls the expression of lipin1, overexpression of CCAAT/enhancer-binding protein alpha activates the lipin1 promoter (from nt -1340 to -524) about 6fold over the basal activity in a transient transfection assay
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positive correlation between lipin-1 expression levels in adipose tissue and insulin sensitivity in obese subjects with normal or impaired glucose tolerance and in healthy young men. Lipin-1 expression is induced in adipocytes by insulin-sensitizing drugs such as thiazolidinediones and harmine. Lipin-2 expression in human adipose tissue
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sterol regulatory element-binding protein 1 (SREBP-1) and nuclear factor Y are necessary for the activation of LPIN1 transcription. Induction of the LPIN1 gene by sterol depletion. The region between nucleotides -2428 and -2378 of the LPIN1 promoter contains sequences that mediate the induction of LPIN1 by sterol depletion. LPIN1 mRNA levels are induced 3.3fold in lipoprotein-deficient serum medium relative to those in sterol-containing medium. In statin-containing medium, LPIN1 mRNA increases 7.2fold
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subcutaneous lipin 1beta expression in polycystic ovary syndrome patients correlates positively with high density lipoprotein-cholesterol. Expression of lipin 1beta in subcutaneous adipose tissue correlates positively with PPARG, LPL, LIPE, adiponectin and SLC2A4 gene expression
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total lipin-1 mRNA expression is significantly induced by dexamethasone in human preadipocytes and differentiated adipocytes
-
hepatic lipin-1 expression is selectively stimulated by glucocorticoids. The expression of lipin-1 is markedly up-regulated under stress conditions
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in the 3T3-L1 cell line, lipin-2 protein levels decline dramatically as adipocyte differentiation proceeds to become virtually undetectable in mature adipocytes, when lipin-1 is expressed at high levels
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lipin 1 knockdown by shRNA, decline in lipin 1 expression with increasing obesity in ob/ob mice
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RNAi against lipin 2 markedly reduces PAP-1 activity in hepatocytes from both wild-type and fld mice and suppresses triglyceride synthesis under conditions of high fatty acid availability
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hepatic lipin-1 expression is selectively repressed by insulin
-
the expression of lipid phosphate phosphatases is decreased in many tumors
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lipin 2 protein content is increased in fld liver independent of changes in steady-state Lpin2 mRNA levels. Lipin 2 is dynamically regulated in liver but is not a target gene of peroxisome proliferator-activated receptorgamma-coactivator 1alpha
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lipin-1 gene expression is regulated in a glucocorticoid receptor-dependent manner
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both lipin 2 mRNA and protein expression are significantly induced by food deprivation. Lipin 2 knockdown leads to a compensatory increase in Lpin3 mRNA expression, especially in fld hepatocytes
-
hepatic lipin-1 expression levels and VLDL secretion both increase in obese individuals following gastric bypass surgery
-
in the 3T3-L1 cell line, lipin-2 protein levels are highest in preadipocytes
-
lipin-2 is most prominently expressed in liver, where levels are much higher than lipin-1, and also in kidney, lung, gastrointestinal tract, and specific regions of the brain. Fasting induces hepatic lipin-1 by 25fold and lipin-2 by 5fold. Lipin-2 is also expressed in circulating red blood cells and sites of lymphopoiesis, like bone marrow, thymus, and spleen
-
lipin-1A and -B expression levels increase dramatically during differentiation of 3T3-L1 preadipocytes to mature adipocytes. Glucocorticoids are the stimulus for the induction of lipin-1 expression in differentiating adipocytes. Lpin1 glucocorticoid response element binds to the glucocorticoid receptor and leads to transcriptional activation in adipocytes and hepatocytes. The Lpin1 promoter directly binds the glucocorticoid receptor in a hormone-dependent manner. Dexamethasone rapidly induces lipin-1 gene expression in a dose-dependent manner, it acts at the level of lipin-1 gene transcription. In response to 0.001 mM dexamethasone treatment, lipin-1B mRNA levels increase as early as 1 h, and lipin-1A levels after 2 h, whereby lipin-1B levels peak with a 7fold induction at 2 h and lipin-1A levels increase to a maximum of 3fold above baseline and remain elevated near this level throughout 24 h. Adipose tissue lipin-1 expression is increased in conditions associated with increased local glucocorticoid concentrations in vivo
-
hepatic lipin-1 expression is selectively stimulated by glucocorticoids. The expression of lipin-1 is markedly upregulated under stress conditions
-
lipin-2 is most prominently expressed in liver, where levels are much higher than lipin-1, and also in kidney, lung, gastrointestinal tract, and specific regions of the brain. Fasting induces hepatic lipin-1 by 25fold and lipin-2 by 5fold. Lipin-2 is also expressed in circulating red blood cells and sites of lymphopoiesis, like bone marrow, thymus, and spleen
Mus musculus C57BL/6J
-
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PAP1 activity is highly related with cardiac lipin-1 and lipin-3 mRNA expression in Zucker diabetic fatty rats
-
left ventricular lipin-1 and lipin-3 expression is 7- to 27fold higher than respective atrial mRNA expression n Zucker diabetic fatty rats
-
mRNA in rat triceps muscle is increased by approximately 2fold after an acute bout of endurance swimming exercise. Lipin-1 mRNA expression in the triceps muscle, compared with that of the control muscle, significantly increases by 85% and 71% immediately after 3- and 6-h swimming exercise, respectively. Lipin-1 mRNA expression in rat triceps muscle is significantly elevated at 6 h after subcutaneous injections of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) by 82% or clenbuterol by 3fold, which are 5'-AMP-activated protein kinase and beta2-adrenergic receptor activators, respectively
-
wild type cells supplemented with palmitoleic acid exhibit an induction in phosphatidate phosphatase activity
-
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
Saccharomyces cerevisiae W303-1A
-
-
no difference in lipin-alpha mRNA expression between Rongchang pigs with high or low intramuscular fat
B7STY8
the longissimus dorsi muscle of Rongchang obese pigs have a higher level of mRNA expression for lipin1 and its isoforms than PIC lean pigs. Rongchang pigs with higher intramuscular fat content have a higher lipin1 and lipin-beta mRNA expression in longissimus dorsisi muscle than Rongchang pigs with lower intramuscular fat content
B7STY8
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
D712E/D714E
-
catalytically inactive. Mutant binds to serine/threonine protein phosphatase-1 catalytic subunit to the same extent as wild-type
D9A
-
mutant is inactive towards lysophosphatidic acids
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
R127K/H223L
-
negligible LPP1 activity, although each mutant is still able to form oligomers
R214K
-
site-directed mutagenesis, 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
R217K
-
adenoviral construction of an inactive isozyme LPP-1 mutant