BRENDA - Enzyme Database
show all sequences of 3.1.3.81

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:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis
Saccharomyces cerevisiae
Engineering
Protein Variants
Commentary
Organism
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
Inhibitors
Commentary
Organism
Structure
diphosphate
-
Saccharomyces cerevisiae
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Escherichia coli
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Mus musculus
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
Saccharomyces cerevisiae
NaF
-
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
DPP1 is an integral membrane protein with six transmembrane helices, tightly associated with microsomal membranes
Saccharomyces cerevisiae
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
potent inhibition
Escherichia coli
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Escherichia coli
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Mus musculus
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]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
-
-
?
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
-
-
?
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
-
-
?
additional information
Saccharomyces cerevisiae
biochemical isozyme regulation mechanism, overview
?
-
-
-
additional information
Mus musculus
PAP2 is involved in lipid signaling pathways
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
gene pgpB
-
Mus musculus
Q61469
-
-
Saccharomyces cerevisiae
Q05521
DPP1; gene DPP1, isozyme DGPP phosphatase 1
-
Purification (Commentary)
Purification (Commentary)
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
additional information
biochemical isozyme regulation mechanism, overview
134878
Saccharomyces cerevisiae
?
-
-
-
-
additional information
PAP2 is involved in lipid signaling pathways
134878
Mus musculus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Escherichia coli
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Mus musculus
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Saccharomyces cerevisiae
Synonyms
Synonyms
Commentary
Organism
DGPP phosphatase
-
Saccharomyces cerevisiae
DGPP phosphatase
-
Escherichia coli
diacylglycerol pyrophosphate phosphatase
-
Saccharomyces cerevisiae
diacylglycerol pyrophosphate phosphatase
-
Escherichia coli
PAP2
-
Mus musculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis
Saccharomyces cerevisiae
Engineering (protein specific)
Protein Variants
Commentary
Organism
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)
Inhibitors
Commentary
Organism
Structure
diphosphate
-
Saccharomyces cerevisiae
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Escherichia coli
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
Mus musculus
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
Saccharomyces cerevisiae
NaF
-
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
DPP1 is an integral membrane protein with six transmembrane helices, tightly associated with microsomal membranes
Saccharomyces cerevisiae
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
potent inhibition
Escherichia coli
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Escherichia coli
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Mus musculus
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)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
-
-
?
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
-
-
?
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
-
-
?
additional information
Saccharomyces cerevisiae
biochemical isozyme regulation mechanism, overview
?
-
-
-
additional information
Mus musculus
PAP2 is involved in lipid signaling pathways
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
additional information
biochemical isozyme regulation mechanism, overview
134878
Saccharomyces cerevisiae
?
-
-
-
-
additional information
PAP2 is involved in lipid signaling pathways
134878
Mus musculus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 34000, DGPP phosphatase 1, SDS-PAGE
Saccharomyces cerevisiae
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Escherichia coli
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Mus musculus
More
the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Escherichia coli
Other publictions for EC 3.1.3.81
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
679998
Takeuchi
Cloning and characterization o ...
Homo sapiens
Gene
399
174-180
2007
-
-
1
-
-
-
1
2
-
1
-
-
-
2
-
-
-
-
-
16
-
-
2
-
8
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
2
-
2
-
-
-
-
-
-
-
17
-
-
2
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
682952
Carman
Roles of phosphatidate phospha ...
Saccharomyces cerevisiae
Trends Biochem. Sci.
31
694-699
2006
-
-
-
-
-
-
3
-
3
1
-
1
-
1
-
-
-
-
-
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
3
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680628
Han
Vacuole membrane topography of ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
J. Biol. Chem.
279
5338-5345
2004
1
-
1
-
-
-
1
-
3
-
-
2
-
18
-
-
1
1
-
-
2
-
3
1
3
1
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
3
-
-
2
-
-
-
1
-
-
2
-
3
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
678372
Oshiro
Diacylglycerol pyrophosphate p ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1635
1-9
2003
1
-
1
-
4
-
7
-
1
1
1
2
-
1
-
-
1
1
-
-
-
-
3
2
3
-
-
-
-
1
-
-
-
1
-
-
1
-
1
-
-
4
-
-
7
1
-
1
1
1
2
-
-
-
1
-
-
-
-
3
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
680624
Oshiro
Regulation of the yeast DPP1-e ...
Saccharomyces cerevisiae
J. Biol. Chem.
278
31495-31503
2003
-
-
1
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680613
Han
Regulation of the Saccharomyce ...
Saccharomyces cerevisiae
J. Biol. Chem.
276
10126-10133
2001
-
-
1
-
1
-
1
-
1
-
1
1
-
2
-
-
-
-
-
-
-
-
1
1
2
1
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
1
-
1
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
680612
Oshiro
Regulation of the DPP1-encoded ...
Saccharomyces cerevisiae
J. Biol. Chem.
275
40887-40896
2000
1
-
1
-
-
-
3
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
2
1
3
1
-
-
-
1
-
-
-
1
-
1
1
-
1
-
-
-
-
1
3
1
-
-
-
1
1
-
-
-
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
678120
Toke
Mutagenesis of the phosphatase ...
Saccharomyces cerevisiae
Biochemistry
38
14606-14613
1999
-
-
1
-
3
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
5
-
2
1
2
1
-
3
-
1
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
5
-
2
1
1
-
3
-
1
-
-
-
-
-
-
-
-
-
680606
Toke
Isolation and characterization ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
J. Biol. Chem.
273
3278-3284
1998
-
-
1
-
1
-
-
-
1
1
1
2
-
17
-
-
-
-
-
-
-
-
2
2
2
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
2
-
-
-
-
-
-
-
-
2
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
134878
Carman
Phosphatidate phosphatases and ...
Escherichia coli, Mus musculus, Saccharomyces cerevisiae
Biochim. Biophys. Acta
1348
45-55
1997
-
-
1
-
1
-
5
1
1
4
1
5
-
3
-
-
1
-
-
-
-
-
7
4
5
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
5
-
1
1
4
1
5
-
-
-
1
-
-
-
-
7
4
-
-
-
-
1
-
-
-
-
-
-
-
-
-
680603
Dillon
Mammalian Mg2+-independent pho ...
Rattus norvegicus, Saccharomyces cerevisiae
J. Biol. Chem.
272
10361-10366
1997
1
-
-
-
-
-
6
2
2
2
-
4
-
2
-
-
-
-
-
2
-
-
6
-
6
2
-
-
-
2
-
-
-
1
-
-
1
-
-
-
-
-
-
-
6
1
2
2
2
-
4
-
-
-
-
-
2
-
-
6
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
682447
Riedel
-
Metabolism of diacylglycerol p ...
Catharanthus roseus
Plant Sci.
128
1-10
1997
-
-
-
-
-
-
6
-
2
2
-
1
-
1
-
-
-
-
-
4
-
-
3
-
2
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
2
2
-
1
-
-
-
-
-
4
-
-
3
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
680601
Wu
Purification and characterizat ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MATa ade5
J. Biol. Chem.
271
1868-1876
1996
3
-
-
-
-
-
10
1
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10
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680602
Dillon
The Escherichia coli pgpB gene ...
Escherichia coli
J. Biol. Chem.
271
30548-30553
1996
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