BRENDA - Enzyme Database show
show all sequences of 3.1.3.81

The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity

Dillon, D.A.; Wu, W.I.; Riedel, B.; Wissing, J.B.; Dowhan, W.; Carman, G.M.; J. Biol. Chem. 271, 30548-30553 (1996)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
EDTA
35% stimulation at 2 mM
Escherichia coli
Cloned(Commentary)
Commentary
Organism
gene pgpB, overexpression in strain JM103 leads to 370fold increased Mg2+-independent phosphatidic acid phosphatase activity and to 310fold increased DGPP phosphatase activity
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
additional information
mutant strain CF20 is defective in gene pgpB and in phosphatidic acid phosphatase, lysophosphatidic acid phosphatase, and phosphatidylglycerophosphate phosphatase activities, while the overexpressing strain JM103 shows an enhancement of these activities, overview
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
Mn2+
complete inhibition at about 0.075 mM MnCl2
Escherichia coli
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme activity is independent of a divalent cation requirement, the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
gene pgpB
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
680602
Escherichia coli
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
9.3fold preferred substrate compared to phosphatidic acid, 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
680602
Escherichia coli
phosphatidate + phosphate
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Escherichia coli
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.034
-
pH 6.5, 30°C
Escherichia coli
Mn2+
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
EDTA
35% stimulation at 2 mM
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene pgpB, overexpression in strain JM103 leads to 370fold increased Mg2+-independent phosphatidic acid phosphatase activity and to 310fold increased DGPP phosphatase activity
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
mutant strain CF20 is defective in gene pgpB and in phosphatidic acid phosphatase, lysophosphatidic acid phosphatase, and phosphatidylglycerophosphate phosphatase activities, while the overexpressing strain JM103 shows an enhancement of these activities, overview
Escherichia coli
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.034
-
pH 6.5, 30°C
Escherichia coli
Mn2+
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Mn2+
complete inhibition at about 0.075 mM MnCl2
Escherichia coli
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme activity is independent of a divalent cation requirement, the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
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, 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
680602
Escherichia coli
phosphatidate + phosphate
-
-
-
?
diacylglycerol diphosphate + H2O
9.3fold preferred substrate compared to phosphatidic acid, 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
680602
Escherichia coli
phosphatidate + phosphate
-
-
-
?
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
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
-
-
-
-
-
-
-
-
-