BRENDA - Enzyme Database show
show all sequences of 3.1.3.81

Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae

Wu, W.I.; Liu, Y.; Riedel, B.; Wissing, J.B.; Fischl, A.S.; Carman, G.M.; J. Biol. Chem. 271, 1868-1876 (1996)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
phosphatidylethanolamine
-
Saccharomyces cerevisiae
phosphatidylinositol
-
Saccharomyces cerevisiae
Triton X-100
addition of Triton X-100 stimulates DGPP phosphatase activity to a maximum at a concentration of 2 mM
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
4-chloromercuriphenylsulfonic acid
41% inhibition at 1 mM
Saccharomyces cerevisiae
ADP
24% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
Saccharomyces cerevisiae
Ca2+
-
Saccharomyces cerevisiae
diacylglycerol
slight inhibition
Saccharomyces cerevisiae
diphosphate
48% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
Saccharomyces cerevisiae
Mg2+
-
Saccharomyces cerevisiae
Mn2+
-
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
NaF
94% inhibition at 10 mM
Saccharomyces cerevisiae
NEM
10% inhibition at 5 mM
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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%
Saccharomyces cerevisiae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
associated
Saccharomyces cerevisiae
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
x * 34000, SDS-PAGE
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
preferred substrate
phosphatidate + phosphate
-
-
?
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae MATa ade5
preferred substrate
phosphatidate + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae MATa ade5
-
-
-
Purification (Commentary)
Commentary
Organism
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
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
150
-
purified enzyme
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
680601
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
680601
Saccharomyces cerevisiae
phosphatidate + phosphate
product identification by TLC
-
-
?
diacylglycerol diphosphate + H2O
preferred substrate
680601
Saccharomyces cerevisiae MATa ade5
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
680601
Saccharomyces cerevisiae MATa ade5
phosphatidate + phosphate
product identification by TLC
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 34000, SDS-PAGE
Saccharomyces cerevisiae
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
40.9
-
diacylglycerol diphosphate
pH 6.5, 30°C
Saccharomyces cerevisiae
96.67
-
diacylglycerol diphosphate
pH 6.5, 30°C
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8.5
-
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
-
Saccharomyces cerevisiae
0.058
-
Mn2+
pH 6.5, 30°C
Saccharomyces cerevisiae
0.56
-
Ca2+
pH 6.5, 30°C
Saccharomyces cerevisiae
17
-
Mg2+
pH 6.5, 30°C
Saccharomyces cerevisiae
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
phosphatidylethanolamine
-
Saccharomyces cerevisiae
phosphatidylinositol
-
Saccharomyces cerevisiae
Triton X-100
addition of Triton X-100 stimulates DGPP phosphatase activity to a maximum at a concentration of 2 mM
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-chloromercuriphenylsulfonic acid
41% inhibition at 1 mM
Saccharomyces cerevisiae
ADP
24% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
Saccharomyces cerevisiae
Ca2+
-
Saccharomyces cerevisiae
diacylglycerol
slight inhibition
Saccharomyces cerevisiae
diphosphate
48% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
Saccharomyces cerevisiae
Mg2+
-
Saccharomyces cerevisiae
Mn2+
-
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
NaF
94% inhibition at 10 mM
Saccharomyces cerevisiae
NEM
10% inhibition at 5 mM
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
-
Saccharomyces cerevisiae
0.058
-
Mn2+
pH 6.5, 30°C
Saccharomyces cerevisiae
0.56
-
Ca2+
pH 6.5, 30°C
Saccharomyces cerevisiae
17
-
Mg2+
pH 6.5, 30°C
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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%
Saccharomyces cerevisiae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
associated
Saccharomyces cerevisiae
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
x * 34000, 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
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
preferred substrate
phosphatidate + phosphate
-
-
?
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae MATa ade5
preferred substrate
phosphatidate + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
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
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
150
-
purified enzyme
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
680601
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
680601
Saccharomyces cerevisiae
phosphatidate + phosphate
product identification by TLC
-
-
?
diacylglycerol diphosphate + H2O
preferred substrate
680601
Saccharomyces cerevisiae MATa ade5
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
680601
Saccharomyces cerevisiae MATa ade5
phosphatidate + phosphate
product identification by TLC
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 34000, SDS-PAGE
Saccharomyces cerevisiae
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
40.9
-
diacylglycerol diphosphate
pH 6.5, 30°C
Saccharomyces cerevisiae
96.67
-
diacylglycerol diphosphate
pH 6.5, 30°C
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8.5
-
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
-
-
-
-
-
-
-
-
-