BRENDA - Enzyme Database
show all sequences of 3.1.3.81

Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae

Han, G.S.; Johnston, C.N.; Carman, G.M.; J. Biol. Chem. 279, 5338-5345 (2004)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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
Saccharomyces cerevisiae
Cloned(Commentary)
Cloned (Commentary)
Organism
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
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
Zn2+
zinc depletion increases the enzyme activity in vivo, stress condition of zinc depletion induces DPP1 expression
Saccharomyces cerevisiae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
vacuolar membrane
associated, the enzyme contains six putative transmembrane domains, the catalytic site is oriented to the cytosolic face of the vacuole membrane
Saccharomyces cerevisiae
5774
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae
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
phosphatidate + phosphate
-
-
?
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae W303-1A
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
phosphatidate + phosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Saccharomyces cerevisiae
-
gene DPP1
-
Saccharomyces cerevisiae W303-1A
-
gene DPP1
-
Purification (Commentary)
Purification (Commentary)
Organism
preparation of vacuoles
Saccharomyces cerevisiae
Reaction
Reaction
Commentary
Organism
Reaction ID
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
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.4
-
recombinant vacuole membranes of intact vacuoles from overexpressing transgenic mutant DTY1
Saccharomyces cerevisiae
7
-
recombinant vacuole membranes of Triton X-100-ruptured vacuoles from overexpressing transgenic mutant DTY1
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
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
680628
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
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
680628
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
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
680628
Saccharomyces cerevisiae W303-1A
phosphatidate + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the enzyme has six putative transmembrane domains and a hydrophilic region that contains a phosphatase motif required for its catalytic activity, membrane topology, overview
Saccharomyces cerevisiae
Synonyms
Synonyms
Commentary
Organism
DGPP phosphatase
-
Saccharomyces cerevisiae
diacylglycerol pyrophosphate phosphatase
-
Saccharomyces cerevisiae
DPP1
-
Saccharomyces cerevisiae
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
assay at
Saccharomyces cerevisiae
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
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
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Zn2+
zinc depletion increases the enzyme activity in vivo, stress condition of zinc depletion induces DPP1 expression
Saccharomyces cerevisiae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
vacuolar membrane
associated, the enzyme contains six putative transmembrane domains, the catalytic site is oriented to the cytosolic face of the vacuole membrane
Saccharomyces cerevisiae
5774
-
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
Saccharomyces cerevisiae
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
phosphatidate + phosphate
-
-
?
diacylglycerol diphosphate + H2O
Saccharomyces cerevisiae W303-1A
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
phosphatidate + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
preparation of vacuoles
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.4
-
recombinant vacuole membranes of intact vacuoles from overexpressing transgenic mutant DTY1
Saccharomyces cerevisiae
7
-
recombinant vacuole membranes of Triton X-100-ruptured vacuoles from overexpressing transgenic mutant DTY1
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
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
680628
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
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
680628
Saccharomyces cerevisiae
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
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
680628
Saccharomyces cerevisiae W303-1A
phosphatidate + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme has six putative transmembrane domains and a hydrophilic region that contains a phosphatase motif required for its catalytic activity, membrane topology, overview
Saccharomyces cerevisiae
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
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
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
1
-
1
2
-
2
-
-
1
-
-
-
1
-
4
1
2
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
-
2
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
1
2
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-