BRENDA - Enzyme Database show
show all sequences of 3.1.3.81

Mammalian Mg2+-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity

Dillon, D.A.; Chen, X.; Zeimetz, G.M.; Wu, W.I.; Waggoner, D.W.; Dewald, J.; Brindley, D.N.; Carman, G.M.; J. Biol. Chem. 272, 10361-10366 (1997)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
phosphatidate
slight activation of the DGPP phosphatases activity
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
ceramide 1-phosphate
-
Saccharomyces cerevisiae
lysophosphatidate
-
Saccharomyces cerevisiae
Mn2+
the inhibition of DGPP phosphatase activity by Mn2+ ions follows positive cooperative kinetics
Rattus norvegicus
additional information
no inhibition by N-ethylmaleimide and bromoenol lactone, and by EDTA and EGTA
Rattus norvegicus
phosphatidate
competitive versus diacylglycerol diphosphate
Rattus norvegicus
sphingosine 1-phosphate
-
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the enzyme shows high affinity for diacylglycerol diphosphate, kinetics, overview
Rattus norvegicus
additional information
-
additional information
kinetics
Saccharomyces cerevisiae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
plasma membrane
-
Rattus norvegicus
5886
-
plasma membrane
-
Saccharomyces cerevisiae
5886
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no Mg2+ or other divalent cations required for diacylglycerol diphosphate hydrolase activity
Rattus norvegicus
additional information
no Mg2+ or other divalent cations required
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacylglycerol diphosphate + H2O
Rattus norvegicus
preferred substrate
phosphatidate + phosphate
-
-
?
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
preferred substrate
phosphatidate + phosphate
-
-
?
additional information
Rattus norvegicus
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
?
-
-
-
additional information
Saccharomyces cerevisiae
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Saccharomyces cerevisiae
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
liver
-
Saccharomyces cerevisiae
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylglycerol diphosphate + H2O
preferred substrate
680603
Rattus norvegicus
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
preferred substrate
680603
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 then removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
680603
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
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
680603
Rattus norvegicus
phosphatidate + phosphate
-
-
-
?
additional information
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
680603
Rattus norvegicus
?
-
-
-
-
additional information
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
680603
Saccharomyces cerevisiae
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rattus norvegicus
30
-
assay at
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
6
DGPP phosphatase activity
Rattus norvegicus
5.5
6.5
assay at
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
the inhibition of DGPP phosphatase activity by Mn2+ ions follows positive cooperative kinetics
Rattus norvegicus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
phosphatidate
slight activation of the DGPP phosphatases activity
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ceramide 1-phosphate
-
Saccharomyces cerevisiae
lysophosphatidate
-
Saccharomyces cerevisiae
Mn2+
the inhibition of DGPP phosphatase activity by Mn2+ ions follows positive cooperative kinetics
Rattus norvegicus
additional information
no inhibition by N-ethylmaleimide and bromoenol lactone, and by EDTA and EGTA
Rattus norvegicus
phosphatidate
competitive versus diacylglycerol diphosphate
Rattus norvegicus
sphingosine 1-phosphate
-
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
the inhibition of DGPP phosphatase activity by Mn2+ ions follows positive cooperative kinetics
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
the enzyme shows high affinity for diacylglycerol diphosphate, kinetics, overview
Rattus norvegicus
additional information
-
additional information
kinetics
Saccharomyces cerevisiae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
plasma membrane
-
Rattus norvegicus
5886
-
plasma membrane
-
Saccharomyces cerevisiae
5886
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no Mg2+ or other divalent cations required for diacylglycerol diphosphate hydrolase activity
Rattus norvegicus
additional information
no Mg2+ or other divalent cations required
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacylglycerol diphosphate + H2O
Rattus norvegicus
preferred substrate
phosphatidate + phosphate
-
-
?
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
preferred substrate
phosphatidate + phosphate
-
-
?
additional information
Rattus norvegicus
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
?
-
-
-
additional information
Saccharomyces cerevisiae
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
liver
-
Saccharomyces cerevisiae
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylglycerol diphosphate + H2O
preferred substrate
680603
Rattus norvegicus
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
preferred substrate
680603
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 then removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
680603
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
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
680603
Rattus norvegicus
phosphatidate + phosphate
-
-
-
?
additional information
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
680603
Rattus norvegicus
?
-
-
-
-
additional information
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
680603
Saccharomyces cerevisiae
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rattus norvegicus
30
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
6
DGPP phosphatase activity
Rattus norvegicus
5.5
6.5
assay at
Saccharomyces cerevisiae
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
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
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
14
-
-
1
1
-
-
2
-
3
1
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
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
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
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
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
-
13
-
-
-
-
-
-
-
-
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
-
-
-
-
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
-
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
-
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
1
-
1
2
-
2
-
-
1
-
-
-
1
-
4
1
1
-
-
2
1
-
-
-
4
-
-
3
-
-
-
-
-
-
-
10
4
1
1
-
1
2
-
-
-
1
-
-
1
-
4
1
1
-
-
2
1
-
-
-
-
-
-
-
-
-
680602
Dillon
The Escherichia coli pgpB gene ...
Escherichia coli
J. Biol. Chem.
271
30548-30553
1996
1
-
1
-
1
-
2
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
1
2
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-