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Information on EC 3.6.1.75 - diacylglycerol diphosphate phosphatase
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3.6.1.75 diacylglycerol diphosphate phosphataseIUBMB Comments
The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response . The phosphatase activity of the bifunctional enzyme is Mg2+-independent and N-ethylmaleimide-insensitive and is distinct from the Mg2+-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase) .The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase .
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
pyrophosphate phosphatase, dpp1-encoded diacylglycerol pyrophosphate phosphatase, diacylglycerol diphosphate phosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DGPP phosphatase
DGPP phosphohydrolase
diacylglycerol pyrophosphate phosphatase
DPP1
DPPL1
DPPL2
EC 3.1.3.81
-
-
formerly
-
PAP2
pyrophosphate phosphatase
-
-
-
-
additional information
DGPP phosphatase
-
-
-
-
DGPP phosphatase
-
-
DGPP phosphohydrolase
-
-
-
-
diacylglycerol pyrophosphate phosphatase
-
-
DPP1
-
-
-
-
DPPL1
-
-
-
-
DPPL2
-
-
-
-
PAP2
-
-
-
-
additional information
-
cf. EC 3.1.3.4, the enzyme is a member of the lipid phosphate phosphatase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate
-
-
-
-
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate
the bifunctional enzyme also catalyzes the phosphohydrolysis of phosphatidic acid to diacylglycerol, but is distinct from the phosphatidate phosphatase, EC 3.1.3.4, being Mg2+-independent and insensitive to N-ethylmaleimide, catalytic site structure within the transverse plane of the vacuole membrane, overview
-
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate
the conserved residues Arg125, His169, and His223 within domains 1, 2, and 3, respectively, play important roles in the DGPP phosphatase and phosphatidic acid phosphatase reactions catalyzed by the enzyme
-
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate
the bifunctional enzyme also catalyzes the phosphohydrolysis of phosphatidic acid to diacylglycerol, but is distinct from the phosphatidate phosphatase, EC 3.1.3.4, being Mg2+-independent and insensitive to N-ethylmaleimide, catalytic site structure within the transverse plane of the vacuole membrane, overview
-
-
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PATHWAY SOURCE
PATHWAYS
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-
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SYSTEMATIC NAME
IUBMB Comments
1,2-diacyl-sn-glycerol 3-phosphate phosphohydrolase
The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response [6]. The phosphatase activity of the bifunctional enzyme is Mg2+-independent and N-ethylmaleimide-insensitive and is distinct from the Mg2+-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase) [5].The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
preferred substrate of isozyme DPPL1
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
preferred substrate of isozyme DPPL2
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
diacylglycerol diphosphate metabolism, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
9.3fold preferred substrate compared to phosphatidic acid, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional enzyme catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional PAP2 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
product identification by TLC
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4, genetic regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional Dpp1p catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the substrate and product of the DGPP phosphatase reaction play roles in lipid signaling and in cell metabolism
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
preferred substrate, the bifunctional enzyme catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the enzyme removes the beta phosphate from DGPP to form phosphatidate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
product identification by TLC
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
additional information
?
-
-
no activity with ADP, 4-nitrophenylphosphate, and diphosphate
-
-
?
additional information
?
-
PAP2 is involved in lipid signaling pathways
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
additional information
?
-
biochemical isozyme regulation mechanism, overview
-
-
?
additional information
?
-
-
DGPP phosphatase plays a role in the regulation of phospholipid metabolism by inositol, as well as regulating the cellular levels of phosphatidylinositol, regulation of DGPP phosphatase by inositol and growth phase, overview
-
-
?
additional information
?
-
-
DPP1 is a zinc-regulated gene, and it contains a putative zinc-responsive element, UASZRE, in its promoter, regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
additional information
?
-
-
the phosphatidate phosphatase activity of the DGPP phosphatase enzyme is distinct from the conventional phosphatidate phosphatase enzymes, EC 3.1.3.4, that are presumably responsible for the synthesis of glycerophospholipids and triacylglycerols in Saccharomyces cerevisiae, the DPP1-encoded DGPP phosphatase is regulated by the stress conditions of zinc depletion, stationary phase, and by inositol supplementation, regulation mechanisms, overview
-
-
?
additional information
?
-
-
DGPP phosphatase utilizes several lipid phosphate substrates in vitro, including lysoPA, sphingoid base phosphates, isoprenoid phosphates, and phosphatidylglycerophosphate, the enzyme contains a three-domain lipid phosphatase motif required for catalytic activity
-
-
?
additional information
?
-
-
DGPP stimulates the activity of pure phosphatidylserine synthase by a mechanism that increases the affinity of the enzyme for its substrate CDP-diacylglycerol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
diacylglycerol diphosphate metabolism, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4, genetic regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional Dpp1p catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it also removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the substrate and product of the DGPP phosphatase reaction play roles in lipid signaling and in cell metabolism
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
additional information
?
-
PAP2 is involved in lipid signaling pathways
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
additional information
?
-
biochemical isozyme regulation mechanism, overview
-
-
?
additional information
?
-
-
DGPP phosphatase plays a role in the regulation of phospholipid metabolism by inositol, as well as regulating the cellular levels of phosphatidylinositol, regulation of DGPP phosphatase by inositol and growth phase, overview
-
-
?
additional information
?
-
-
DPP1 is a zinc-regulated gene, and it contains a putative zinc-responsive element, UASZRE, in its promoter, regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
additional information
?
-
-
the phosphatidate phosphatase activity of the DGPP phosphatase enzyme is distinct from the conventional phosphatidate phosphatase enzymes, EC 3.1.3.4, that are presumably responsible for the synthesis of glycerophospholipids and triacylglycerols in Saccharomyces cerevisiae, the DPP1-encoded DGPP phosphatase is regulated by the stress conditions of zinc depletion, stationary phase, and by inositol supplementation, regulation mechanisms, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no divalent metal ion requirement of both isozymes
additional information
-
the enzyme activity is independent of a divalent cation requirement, the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
additional information
-
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
additional information
-
no Mg2+ or other divalent cations required for diacylglycerol diphosphate hydrolase activity
additional information
the enzyme activity is independent of a divalent cation requirement, the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
additional information
-
the enzyme is Mg2+-independent and shows no divalent cation requirement for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
24% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
diphosphate
-
48% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
Mn2+
-
the inhibition of DGPP phosphatase activity by Mn2+ ions follows positive cooperative kinetics
Zn2+
-
the regulation of DPP1 expression in zinc-limited cells is dependent on the transcription factor Zap1p and binding to a cis-acting element, UASZRE, a zinc-responsive element, DPP1 expression is sensitive to the cytoplasmic levels of zinc, overview
Zn2+
-
the DGPP phosphatase activity is inhibited by zinc by a mechanism that involves formation of DGPP-zinc complexes, overview
Zn2+
-
zinc depletion increases the enzyme activity in vivo, stress condition of zinc depletion induces DPP1 expression
Zn2+
-
DPP1-encoded PAP2 activity is inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
additional information
-
no inhibition by EDTA and NEM of both isozymes
-
additional information
-
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
-
additional information
-
the enzyme is insensitive to NEM and other sulfhydryl reagents
-
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
-
additional information
-
no inhibition by N-ethylmaleimide and bromoenol lactone, and by EDTA and EGTA
-
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
-
additional information
-
no inhibition by NEM, phenylglyoxal, and sulfhydryl reagents, repression of DPP1 expression is mediated by the transcription factor Gis1p, which binds to three post-diauxic shift elements in the promoter
-
additional information
-
poor inhibition by ATP and AMP, the enzyme is inhibited by divalent cations, but is relatively insensitive to thioreactive agents, no inhibition by phospholipids or phosphatidic acid versus diacylglycerol diphosphate as substrate, no inhibition by EDTA, glycerol 3-phosphate, and inositol 1-phosphate
-
additional information
-
no or poor inhibition by phospholipids, overview
-
additional information
-
Dpp1p, DPP1-encoded PAP2 activity, is NEM-insensitive
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
-
addition of Triton X-100 stimulates DGPP phosphatase activity to a maximum at a concentration of 2 mM
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
-
inositol induces the enzyme in both exponential and stationary phase cells
-
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.041
diacylglycerol diphosphate
pH 6.5, 37°C, recombinant isozyme DPPL2
0.104
diacylglycerol diphosphate
pH 6.5, 37°C, recombinant isozyme DPPL1
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
DGPP phosphatase exhibits typical saturation kinetics with respect to diacylglycerol diphosphate with a the Km value 3-fold greater than its cellular concentration
-
additional information
additional information
-
kinetics, the DGPP phosphatase exhibits typical saturation kinetics with respect to DGPP, the Km value for diacylglycerol diphosphate is 3fold greater than its cellular concentration of 0.18 mol%
-
additional information
additional information
-
the enzyme shows high affinity for diacylglycerol diphosphate, kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the inhibition of DGPP phosphatase activity by Mn2+ ions follows positive cooperative kinetics
-
additional information
additional information
-
value for CDP-diacylglacerol is 5 mol%
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
-
recombinant vacuole membranes of intact vacuoles from overexpressing transgenic mutant DTY1
7
-
recombinant vacuole membranes of Triton X-100-ruptured vacuoles from overexpressing transgenic mutant DTY1
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
synovium containing, specific expression of isozyme DPPL2
brenda
specific expression of DPPL2, expression in endothelial cell lines, overview
brenda
additional information
additional information
DPPL1 is ubiquitously expressed in various tissues and cells, overview
brenda
additional information
DPPL1 is ubiquitously expressed in various tissues and cells, overview
brenda
additional information
DPPL2 mRNA is restricted to several tissues, expression in cancer cell lines, overview
brenda
additional information
DPPL2 mRNA is restricted to several tissues, expression in cancer cell lines, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
ChPAP2 is localized at the plasma membrane and in the lumen of vacuoles
brenda
-
an integral membrane protein with six transmembrane spanning regions
brenda
-
DGPP phosphatase is an integral membrane protein with six transmembrane-spanning domains
brenda
-
DGPP phosphatase is an integral membrane protein with six transmembrane-spanning domains
-
brenda
DPP1 is an integral membrane protein with six transmembrane helices, tightly associated with microsomal membranes
-
brenda
ChPAP2 is localized at the plasma membrane and in the lumen of vacuoles
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associated, the enzyme contains six putative transmembrane domains, the catalytic site is oriented to the cytosolic face of the vacuole membrane
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associated, the enzyme contains six putative transmembrane domains, the catalytic site is oriented to the cytosolic face of the vacuole membrane
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme (ChPAP) may play important roles in promoting Na-ion movement into the cell and maintaining the cytoplasmic ion balance. In addition, the enzyme may catalyze diacylglycerol pyrophosphate to phosphatidate in vacuoles
Show AA Sequence and Transmembrane Helices (1252 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
additional information
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
additional information
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Dpp1p contains three cysteine residues, the DPP1-encoded PAP2 enzyme contains a three-domain lipid phosphatase motif that is localized to the hydrophilic surface of the membrane
additional information
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
additional information
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the enzyme contains a three-domain lipid phosphatase motif required for catalytic activity and six transmembrane-spanning regions distributed over the entire polypeptide sequence, topography of the phosphatase sequence motif of the DPP1-encoded DGPP phosphatase, overview
additional information
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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
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the enzyme has six putative transmembrane domains and contains a phosphatase motif required for its catalytic activity, overview
additional information
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the primary structure of the DGPP phosphatase protein contains a three-domain phosphatase sequence motif, which is important for catalysis, the residues Arg125, His169, and His223 in domains 1, 2, and 3 are involved
additional information
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the enzyme has six putative transmembrane domains and a hydrophilic region that contains a phosphatase motif required for its catalytic activity, membrane topology, overview
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additional information
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the enzyme has six putative transmembrane domains and contains a phosphatase motif required for its catalytic activity, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H169A
H223A
R125A
additional information
H169A
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site-directed mutagenesis of the phosphatase sequence motif residue, the mutant shows 9% of wild-type enzyme DGPP phosphatase activity and no phosphatidic acid phosphatase activity
H169A
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site-directed mutagenesis, the mutant enzyme shows 9% of wild-type enzyme activity
H223A
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site-directed mutagenesis of the phosphatase sequence motif residue, the mutant shows 0.03% of wild-type enzyme DGPP phosphatase activity and no phosphatidic acid phosphatase activity
H223A
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site-directed mutagenesis, the mutant enzyme shows 0.03% of wild-type enzyme activity
R125A
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site-directed mutagenesis of the phosphatase sequence motif residue, the mutant shows 0.05% of wild-type enzyme DGPP phosphatase activity and no phosphatidic acid phosphatase activity
R125A
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site-directed mutagenesis, the mutant enzyme shows 0.05% of wild-type enzyme activity
additional information
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a gene pgpB mutant shows defect in phosphatidic acid phosphatase activity and also exhibits defects in lysophosphatidic acid phosphatase and phosphatidylglycerophosphate phosphatase activities
additional information
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mutant strain CF20 is defective in gene pgpB and in phosphatidic acid phosphatase, lysophosphatidic acid phosphatase, and phosphatidylglycerophosphate phosphatase activities, while the overexpressing strain JM103 shows an enhancement of these activities, overview
additional information
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construction of a dpp1D mutant by deletion of the chromosomal copy of theDPP1 gene, the dpp1D mutant is viable and does not exhibit any obvious growth defects, the mutant is devoid of DGPP phosphatase activity and accumulates DGPP 4-fold compared to wild-type levels, phenotype, overview
additional information
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construction of a mutant by deletions from the 5' end of the promoter indicated sequences responsible for enzyme expression, mutations in the three URSPDS elements within the DPP1 promoter abolish Gis1p-DNA interactions in vitro and abolish the regulation of DPP1 in vivo
additional information
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dpp1DELTA mutants do not exhibit any dramatic phenotypes under a variety of growth conditions including fluctuations in zinc supplementation
additional information
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the regulation pattern of DGPP phosphatase in mutants defective in plasma membrane, Zrt1p and Zrt2p, and vacuolar membrane, Zrt3p, zinc transporters indicates that the enzyme expression is sensitive to the cytoplasmic levels of zinc
additional information
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construction of a dpp1D mutant by deletion of the chromosomal copy of theDPP1 gene, the dpp1D mutant is viable and does not exhibit any obvious growth defects, the mutant is devoid of DGPP phosphatase activity and accumulates DGPP 4-fold compared to wild-type levels, phenotype, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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10 min, 90% remaing DGPP phosphatase activity of mutant H169A, loss of 20-25% activity of wild-type enzyme and mutants R125A and H223A
50
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10 min, inactivation of mutants R125A and H223A, 80% remaining DGPP phosphatase activity of wild-type enzyme and mutant H169A
65
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10 min, wild-type enzyme and mutant H169A, 75% remaining DGPP phosphatase activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
33333fold to homogeneity by solubilization from membranes with Triton X-100, followed by anion exchange chromatography, affinity and hydroxylapatite chromatography, and again anion exchange chromatography
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native enzyme, tightly associated with microsomal membranes, is purified by solubilization from microsomal membranes with Triton X-100 followed by anion exchange, affinity and hydroxylapatite chromatography, followed by another step of anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DPP1 is a zinc-regulated gene, and it contains a putative zinc-responsive element, UASZRE, in its promoter, regulation mechanism, overview
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expression from a plasmid vector bearing the PDPP1-lacZ reporter gene, expression analysis in presence or absence of inositol
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gene DPP1, DNA and amino acid sequence determination and analysis, overexpression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method, subcloning in Escherichia coli strain DH5alpha
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gene DPP1, expression of wild-type and phosphatase sequence motif mutant enzymes in an enzyme-deficient mutant yeast strain, subcloning in Escherichia coli strain DH5alpha and XL-1 bLue
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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 DPP1, genetic regulation, induction by zinc depletion is mediated by the transcription factor Zap1p, which binds to a zinc-responsive element in the DPP1 promoter, repression of DPP1 expression is mediated by the transcription factor Gis1p, which binds to three post-diauxic shift elements in the promoter, overview
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gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis
gene DPP1, subcloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), promoter structure determination and analysis, identification of three binding sites, URSPDS, for transcription factor Gis1p in the DPP1 promoter, direct interaction between Gis1p and DPP1 promoter elements, analysis of genetic regulation, overview
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gene pgpB, overexpression in strain JM103 leads to 370fold increased Mg2+-independent phosphatidic acid phosphatase activity and to 310fold increased DGPP phosphatase activity
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the relative transcript levels of ChPAP in Chlorella cells are strongly induced by NaCl and sorbitol stresses. The upregulated ChPAP2 expression may enhance drought tolerance
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carman, G.M.
Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli
Biochim. Biophys. Acta
1348
45-55
1997
Escherichia coli, Saccharomyces cerevisiae (Q05521), Mus musculus (Q61469)
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Toke, D.A.; McClintick, M.L.; Carman, G.M.
Mutagenesis of the phosphatase sequence motif in diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae
Biochemistry
38
14606-14613
1999
Saccharomyces cerevisiae
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Oshiro, J.; Han, G.S.; Carman, G.M.
Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1635
1-9
2003
Saccharomyces cerevisiae
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Takeuchi, M.; Harigai, M.; Momohara, S.; Ball, E.; Abe, J.; Furuichi, K.; Kamatani, N.
Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase
Gene
399
174-180
2007
Homo sapiens (Q5VZY2), Homo sapiens (Q8NEB5)
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Wu, W.I.; Liu, Y.; Riedel, B.; Wissing, J.B.; Fischl, A.S.; Carman, G.M.
Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae
J. Biol. Chem.
271
1868-1876
1996
Saccharomyces cerevisiae, Saccharomyces cerevisiae MATa ade5
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Dillon, D.A.; Wu, W.I.; Riedel, B.; Wissing, J.B.; Dowhan, W.; Carman, G.M.
The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity
J. Biol. Chem.
271
30548-30553
1996
Escherichia coli
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Dillon, D.A.; Chen, X.; Zeimetz, G.M.; Wu, W.I.; Waggoner, D.W.; Dewald, J.; Brindley, D.N.; Carman, G.M.
Mammalian Mg2+-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity
J. Biol. Chem.
272
10361-10366
1997
Saccharomyces cerevisiae, Rattus norvegicus
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Toke, D.A.; Bennett, W.L.; Dillon, D.A.; Wu, W.I.; Chen, X.; Ostrander, D.B.; Oshiro, J.; Cremesti, A.; Voelker, D.R.; Fischl, A.S.; Carman, G.M.
Isolation and characterization of the Saccharomyces cerevisiae DPP1 gene encoding diacylglycerol pyrophosphate phosphatase
J. Biol. Chem.
273
3278-3284
1998
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
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Oshiro, J.; Rangaswamy, S.; Chen, X.; Han, G.S.; Quinn, J.E.; Carman, G.M.
Regulation of the DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol and growth phase. Inhibition of DGPP phosphatase activity by CDP-diacylglyceron and activation of phosphatidylserine synthase activity by DGPP
J. Biol. Chem.
275
40887-40896
2000
Saccharomyces cerevisiae
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Han, G.S.; Johnston, C.N.; Chen, X.; Athenstaedt, K.; Daum, G.; Carman, G.M.
Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc
J. Biol. Chem.
276
10126-10133
2001
Saccharomyces cerevisiae
brenda
Oshiro, J.; Han, G.S.; Iwanyshyn, W.M.; Conover, K.; Carman, G.M.
Regulation of the yeast DPP1-encoded diacylglycerol pyrophosphate phosphatase by transcription factor Gis1p
J. Biol. Chem.
278
31495-31503
2003
Saccharomyces cerevisiae
brenda
Han, G.S.; Johnston, C.N.; Carman, G.M.
Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae
J. Biol. Chem.
279
5338-5345
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
brenda
Riedel, B.; Morr, M.; Wu, W.I.; Carman, G.M.; Wissing, J.B.
Metabolism of diacylglycerol pyrophosphate by suspension cultured Catharanthus roseus cells. Identification and characterization of diacylglycerol pyrophosphate phosphatase in plants
Plant Sci.
128
1-10
1997
Catharanthus roseus
-
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Carman, G.M.; Han, G.S.
Roles of phosphatidate phosphatase enzymes in lipid metabolism
Trends Biochem. Sci.
31
694-699
2006
Saccharomyces cerevisiae
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Buhrmann, C.; Brockmueller, A.; Harsha, C.; Kunnumakkara, A.; Kubatka, P.; Aggarwal, B.; Shakibaei, M.
Evidence that tumor microenvironment initiates epithelial-to-mesenchymal transition and calebin A can suppress it in colorectal cancer cells
Front. Pharmacol.
12
738282
2021
Chlorella sp. KQ-2014 (A0A140HDC8)
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