BRENDA - Enzyme Database

Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli

Carman, G.M.; Biochim. Biophys. Acta 1348, 45-55 (1997)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.3.4
cardiolipin
activation, antagonized by sphinganine
Saccharomyces cerevisiae
3.1.3.4
CDP-diacylglycerol
-
Saccharomyces cerevisiae
3.1.3.4
additional information
no effect on the enzyme forms by choline
Saccharomyces cerevisiae
3.1.3.4
phosphatidylinositol
activation, antagonized by sphinganine
Saccharomyces cerevisiae
3.1.3.4
Triton X-100
the 45-kDa and 104-kDa enzyme forms are dependent on Triton X-100 for activity
Saccharomyces cerevisiae
Cloned(Commentary)
EC Number
Commentary
Organism
3.1.3.81
gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis
Saccharomyces cerevisiae
Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.81
additional information
a gene pgpB mutant shows defect in phosphatidic acid phosphatase activity and also exhibits defects in lysophosphatidic acid phosphatase and phosphatidylglycerophosphate phosphatase activities
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.4
additional information
no effect on the enzyme forms by choline
Saccharomyces cerevisiae
3.1.3.4
N-ethylmaleimide
inhibition of the 45-kDa and 104-kDa enzyme forms
Saccharomyces cerevisiae
3.1.3.4
NEM
-
Saccharomyces cerevisiae
3.1.3.4
Phenylglyoxal
inhibition of the 45-kDa and 104-kDa enzyme forms
Saccharomyces cerevisiae
3.1.3.4
propranolol
inhibition of the 45-kDa and 104-kDa enzyme forms
Saccharomyces cerevisiae
3.1.3.4
Zwitterionic phospholipids
slight inhibition
Saccharomyces cerevisiae
3.1.3.81
diphosphate
-
Saccharomyces cerevisiae
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Escherichia coli
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Mus musculus
3.1.3.81
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
Saccharomyces cerevisiae
3.1.3.81
NaF
-
Saccharomyces cerevisiae
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.3.4
additional information
-
additional information
kinetic analysis, PA phosphatase activity on phosphatidate is cooperative
Saccharomyces cerevisiae
3.1.3.81
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
Escherichia coli
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
cytosol
75-kDA enzyme form
Saccharomyces cerevisiae
5829
-
3.1.3.4
membrane
-
Saccharomyces cerevisiae
16020
-
3.1.3.4
microsome
45-kDA enzyme form and 104-kDA enzyme form
Saccharomyces cerevisiae
-
-
3.1.3.4
mitochondrion
45-kDA enzyme form
Saccharomyces cerevisiae
5739
-
3.1.3.81
microsome
DPP1 is an integral membrane protein with six transmembrane helices, tightly associated with microsomal membranes
Saccharomyces cerevisiae
-
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
required; required for activity by all enzyme forms
Saccharomyces cerevisiae
3.1.3.81
Mn2+
potent inhibition
Escherichia coli
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Escherichia coli
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Mus musculus
3.1.3.81
additional information
the enzyme activity is independent of a divalent cation requirement, the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Saccharomyces cerevisiae
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.3.4
45000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.4
75000
-
cytosolic enzyme form, gel filtration
Saccharomyces cerevisiae
3.1.3.4
91000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.4
104000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.81
34000
-
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.3.4
additional information
Saccharomyces cerevisiae
the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
?
-
-
-
3.1.3.4
phosphatidate + H2O
Saccharomyces cerevisiae
biochemical regulation of PA phosphatases involving phospholipids, nucleotides ATP and CTP and the cAMP-dependent protein kinase A, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction, overview, PA phosphatase activity is regulated by biochemical and genetic mechanisms in a reciprocal manner with the regulation of the phospholipid biosynthetic enzyme phosphatidylserin synthase, overview
1,2-diacyl-sn-glycerol + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Escherichia coli
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
phosphatidate + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
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
phosphatidate + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Mus musculus
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
phosphatidate + phosphate
-
-
?
3.1.3.81
additional information
Saccharomyces cerevisiae
biochemical isozyme regulation mechanism, overview
?
-
-
-
3.1.3.81
additional information
Mus musculus
PAP2 is involved in lipid signaling pathways
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.3.4
Escherichia coli
-
-
-
3.1.3.4
Saccharomyces cerevisiae
-
-
-
3.1.3.81
Escherichia coli
-
gene pgpB
-
3.1.3.81
Mus musculus
Q61469
-
-
3.1.3.81
Saccharomyces cerevisiae
Q05521
DPP1; gene DPP1, isozyme DGPP phosphatase 1
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.4
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
Saccharomyces cerevisiae
Purification (Commentary)
EC Number
Commentary
Organism
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.81
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
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
dicaproyl phosphatidate + H2O
best substrate of the 104-kDa enzyme form
134878
Saccharomyces cerevisiae
1,2-dicaproyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
dioleoyl phosphatidate + H2O
-
134878
Saccharomyces cerevisiae
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
dipalmitoyl phosphatidate + H2O
-
134878
Saccharomyces cerevisiae
1,2-dipalmitoyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
additional information
the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
134878
Saccharomyces cerevisiae
?
-
-
-
-
3.1.3.4
phosphatidate + H2O
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
134878
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
134878
Escherichia coli
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
134878
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Escherichia coli
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Mus musculus
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Escherichia coli
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
3.1.3.81
additional information
biochemical isozyme regulation mechanism, overview
134878
Saccharomyces cerevisiae
?
-
-
-
-
3.1.3.81
additional information
PAP2 is involved in lipid signaling pathways
134878
Mus musculus
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
3.1.3.4
?
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.81
?
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.81
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Escherichia coli
3.1.3.81
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Mus musculus
3.1.3.81
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Saccharomyces cerevisiae
Temperature Stability [C]
EC Number
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
3.1.3.4
30
-
inhibition of the 45-kDa and 104-kDa enzyme forms, unstable above
Saccharomyces cerevisiae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.3.4
6
7
45-kDa enzyme form
Saccharomyces cerevisiae
3.1.3.4
7
8
75-kDa enzyme form
Saccharomyces cerevisiae
3.1.3.4
7
-
104-kDa enzyme form
Saccharomyces cerevisiae
3.1.3.81
6.5
-
-
Escherichia coli
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.3.4
cardiolipin
activation, antagonized by sphinganine
Saccharomyces cerevisiae
3.1.3.4
CDP-diacylglycerol
-
Saccharomyces cerevisiae
3.1.3.4
additional information
no effect on the enzyme forms by choline
Saccharomyces cerevisiae
3.1.3.4
phosphatidylinositol
activation, antagonized by sphinganine
Saccharomyces cerevisiae
3.1.3.4
Triton X-100
the 45-kDa and 104-kDa enzyme forms are dependent on Triton X-100 for activity
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.81
gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.3.81
additional information
a gene pgpB mutant shows defect in phosphatidic acid phosphatase activity and also exhibits defects in lysophosphatidic acid phosphatase and phosphatidylglycerophosphate phosphatase activities
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.4
additional information
no effect on the enzyme forms by choline
Saccharomyces cerevisiae
3.1.3.4
N-ethylmaleimide
inhibition of the 45-kDa and 104-kDa enzyme forms
Saccharomyces cerevisiae
3.1.3.4
NEM
-
Saccharomyces cerevisiae
3.1.3.4
Phenylglyoxal
inhibition of the 45-kDa and 104-kDa enzyme forms
Saccharomyces cerevisiae
3.1.3.4
propranolol
inhibition of the 45-kDa and 104-kDa enzyme forms
Saccharomyces cerevisiae
3.1.3.4
Zwitterionic phospholipids
slight inhibition
Saccharomyces cerevisiae
3.1.3.81
diphosphate
-
Saccharomyces cerevisiae
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Escherichia coli
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Mus musculus
3.1.3.81
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
Saccharomyces cerevisiae
3.1.3.81
NaF
-
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.3.4
additional information
-
additional information
kinetic analysis, PA phosphatase activity on phosphatidate is cooperative
Saccharomyces cerevisiae
3.1.3.81
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
Escherichia coli
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.3.4
cytosol
75-kDA enzyme form
Saccharomyces cerevisiae
5829
-
3.1.3.4
membrane
-
Saccharomyces cerevisiae
16020
-
3.1.3.4
microsome
45-kDA enzyme form and 104-kDA enzyme form
Saccharomyces cerevisiae
-
-
3.1.3.4
mitochondrion
45-kDA enzyme form
Saccharomyces cerevisiae
5739
-
3.1.3.81
microsome
DPP1 is an integral membrane protein with six transmembrane helices, tightly associated with microsomal membranes
Saccharomyces cerevisiae
-
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.3.4
Mg2+
required; required for activity by all enzyme forms
Saccharomyces cerevisiae
3.1.3.81
Mn2+
potent inhibition
Escherichia coli
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Escherichia coli
3.1.3.81
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Mus musculus
3.1.3.81
additional information
the enzyme activity is independent of a divalent cation requirement, the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.3.4
45000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.4
75000
-
cytosolic enzyme form, gel filtration
Saccharomyces cerevisiae
3.1.3.4
91000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.4
104000
-
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.81
34000
-
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.3.4
additional information
Saccharomyces cerevisiae
the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
?
-
-
-
3.1.3.4
phosphatidate + H2O
Saccharomyces cerevisiae
biochemical regulation of PA phosphatases involving phospholipids, nucleotides ATP and CTP and the cAMP-dependent protein kinase A, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction, overview, PA phosphatase activity is regulated by biochemical and genetic mechanisms in a reciprocal manner with the regulation of the phospholipid biosynthetic enzyme phosphatidylserin synthase, overview
1,2-diacyl-sn-glycerol + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Escherichia coli
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
phosphatidate + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
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
phosphatidate + phosphate
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
Mus musculus
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
phosphatidate + phosphate
-
-
?
3.1.3.81
additional information
Saccharomyces cerevisiae
biochemical isozyme regulation mechanism, overview
?
-
-
-
3.1.3.81
additional information
Mus musculus
PAP2 is involved in lipid signaling pathways
?
-
-
-
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.4
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
Saccharomyces cerevisiae
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.4
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
Saccharomyces cerevisiae
3.1.3.81
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
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
dicaproyl phosphatidate + H2O
best substrate of the 104-kDa enzyme form
134878
Saccharomyces cerevisiae
1,2-dicaproyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
dioleoyl phosphatidate + H2O
-
134878
Saccharomyces cerevisiae
1,2-dioleoyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
dipalmitoyl phosphatidate + H2O
-
134878
Saccharomyces cerevisiae
1,2-dipalmitoyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
additional information
the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol
134878
Saccharomyces cerevisiae
?
-
-
-
-
3.1.3.4
phosphatidate + H2O
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
134878
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
134878
Escherichia coli
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
134878
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Escherichia coli
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Mus musculus
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Escherichia coli
phosphatidate + phosphate
-
-
-
?
3.1.3.81
diacylglycerol diphosphate + H2O
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
134878
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
3.1.3.81
additional information
biochemical isozyme regulation mechanism, overview
134878
Saccharomyces cerevisiae
?
-
-
-
-
3.1.3.81
additional information
PAP2 is involved in lipid signaling pathways
134878
Mus musculus
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.1.3.4
?
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.81
?
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
3.1.3.81
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Escherichia coli
3.1.3.81
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Mus musculus
3.1.3.81
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Saccharomyces cerevisiae
Temperature Stability [C] (protein specific)
EC Number
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
3.1.3.4
30
-
inhibition of the 45-kDa and 104-kDa enzyme forms, unstable above
Saccharomyces cerevisiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.3.4
6
7
45-kDa enzyme form
Saccharomyces cerevisiae
3.1.3.4
7
8
75-kDa enzyme form
Saccharomyces cerevisiae
3.1.3.4
7
-
104-kDa enzyme form
Saccharomyces cerevisiae
3.1.3.81
6.5
-
-
Escherichia coli