Information on EC 3.1.3.81 - diacylglycerol diphosphate phosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.3.81
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RECOMMENDED NAME
GeneOntology No.
diacylglycerol diphosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phosphatidate metabolism, as a signaling molecule
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Glycerolipid metabolism
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Glycerophospholipid metabolism
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
1,2-diacyl-sn-glycerol 3-phosphate phosphohydrolase
The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response [6]. The phosphatase activity of the bifunctional enzyme is Mg2+-independent and N-ethylmaleimide-insensitive and is distinct from the Mg2+-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase) [5].The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase [4].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
microsomal and soluble isozymes
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-
Manually annotated by BRENDA team
gene pgpB
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
show the reaction diagram
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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potent inhibition
NaCl
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monovalent metal ions stimulate the enzyme activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuriphenylsulfonic acid
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41% inhibition at 1 mM
ADP
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24% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
CDP-diacylglycerol
ceramide 1-phosphate
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diacylglycerol
diphosphate
lysophosphatidate
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phosphatidate
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competitive versus diacylglycerol diphosphate
sphingosine
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inhibition of both isozymes, overview
sphingosine 1-phosphate
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additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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35% stimulation at 2 mM
phosphatidate
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slight activation of the DGPP phosphatases activity
phosphatidylethanolamine
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phosphatidylinositol
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Triton X-100
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addition of Triton X-100 stimulates DGPP phosphatase activity to a maximum at a concentration of 2 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041 - 0.104
diacylglycerol diphosphate
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40.9 - 96.67
diacylglycerol diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.56
Ca2+
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pH 6.5, 30°C
17
Mg2+
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pH 6.5, 30°C
0.058
Mn2+
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pH 6.5, 30°C
additional information
additional information
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
CDP
Saccharomyces cerevisiae
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0.034
Mn2+
Escherichia coli
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pH 6.5, 30°C
0.09
Zn2+
Saccharomyces cerevisiae
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pH 5.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001
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mutant H223A, DGPP phosphatase activity
0.00014
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mutant R125A, DGPP phosphatase activity
0.0269
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mutant H169A, DGPP phosphatase activity
0.0472
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wild-type enzyme, phosphatidic acid phosphatase activity
0.29
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wild-type enzyme, DGPP phosphatase activity
1.4
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recombinant vacuole membranes of intact vacuoles from overexpressing transgenic mutant DTY1
7
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recombinant vacuole membranes of Triton X-100-ruptured vacuoles from overexpressing transgenic mutant DTY1
150
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
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soluble isozyme
4.5
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microsomal isozyme
5.5 - 6.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at; assay at
40
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both isozymes
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
synovium containing, specific expression of isozyme DPPL2
Manually annotated by BRENDA team
isozyme DPPL2
Manually annotated by BRENDA team
specific expression of DPPL2, expression in endothelial cell lines, overview
Manually annotated by BRENDA team
isozyme DPPL2
Manually annotated by BRENDA team
specific expression of isozyme DPPL2
Manually annotated by BRENDA team
specific expression of isozyme DPPL2
Manually annotated by BRENDA team
isozyme DPPL2
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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soluble isozyme, 80% of total activity
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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x * 31000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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10 min, 90% remaing DGPP phosphatase activity of mutant H169A, loss of 20-25% activity of wild-type enzyme and mutants R125A and H223A
50
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10 min, inactivation of mutants R125A and H223A, 80% remaining DGPP phosphatase activity of wild-type enzyme and mutant H169A
65
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10 min, wild-type enzyme and mutant H169A, 75% remaining DGPP phosphatase activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
preparation of vacuoles
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DPP1 is a zinc-regulated gene, and it contains a putative zinc-responsive element, UASZRE, in its promoter, regulation mechanism, overview
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expression from a plasmid vector bearing the PDPP1-lacZ reporter gene, expression analysis in presence or absence of inositol
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expression of isozyme DPPL1 in Spodoptera frugiperda Sf9 cells; expression of isozyme DPPL2 in Spodoptera frugiperda Sf9 cells
gene DPP1, DNA and amino acid sequence determination and analysis, overexpression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method, subcloning in Escherichia coli strain DH5alpha
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gene DPP1, expression of wild-type and phosphatase sequence motif mutant enzymes in an enzyme-deficient mutant yeast strain, subcloning in Escherichia coli strain DH5alpha and XL-1 bLue
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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
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gene DPP1, genetic regulation, induction by zinc depletion is mediated by the transcription factor Zap1p, which binds to a zinc-responsive element in the DPP1 promoter, repression of DPP1 expression is mediated by the transcription factor Gis1p, which binds to three post-diauxic shift elements in the promoter, overview
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gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis
gene DPP1, subcloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), promoter structure determination and analysis, identification of three binding sites, URSPDS, for transcription factor Gis1p in the DPP1 promoter, direct interaction between Gis1p and DPP1 promoter elements, analysis of genetic regulation, overview
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gene pgpB, overexpression in strain JM103 leads to 370fold increased Mg2+-independent phosphatidic acid phosphatase activity and to 310fold increased DGPP phosphatase activity
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information