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Literature summary extracted from
- Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli (1997), Biochim. Biophys. Acta, 1348, 45-55.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.4 | cardiolipin | activation, antagonized by sphinganine | Saccharomyces cerevisiae |  |
| 3.1.3.4 | CDP-diacylglycerol | - |
Saccharomyces cerevisiae | |
| 3.1.3.4 | additional information | no effect on the enzyme forms by choline | Saccharomyces cerevisiae | |
| 3.1.3.4 | phosphatidylinositol | activation, antagonized by sphinganine | Saccharomyces cerevisiae | |
| 3.1.3.4 | Triton X-100 | the 45-kDa and 104-kDa enzyme forms are dependent on Triton X-100 for activity | Saccharomyces cerevisiae | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.1.75 | gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis | Saccharomyces cerevisiae |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.6.1.75 | additional information | a gene pgpB mutant shows defect in phosphatidic acid phosphatase activity and also exhibits defects in lysophosphatidic acid phosphatase and phosphatidylglycerophosphate phosphatase activities | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.4 | ATP | complex inhibition of the 104-kDa enzyme form, inhibition of the 45-kDa enzyme form, inhibition by nucleotides involves the chelation of Mg2+ ions | Saccharomyces cerevisiae | |
| 3.1.3.4 | CTP | complex inhibition of the 104-kDa enzyme form, inhibition of the 45-kDa enzyme form, inhibition by nucleotides involves the chelation of Mg2+ ions | Saccharomyces cerevisiae | |
| 3.1.3.4 | additional information | no effect on the enzyme forms by choline | Saccharomyces cerevisiae | |
| 3.1.3.4 | N-ethylmaleimide | inhibition of the 45-kDa and 104-kDa enzyme forms | Saccharomyces cerevisiae | |
| 3.1.3.4 | NEM | - |
Saccharomyces cerevisiae | |
| 3.1.3.4 | Phenylglyoxal | inhibition of the 45-kDa and 104-kDa enzyme forms | Saccharomyces cerevisiae | |
| 3.1.3.4 | propranolol | inhibition of the 45-kDa and 104-kDa enzyme forms | Saccharomyces cerevisiae | |
| 3.1.3.4 | Zwitterionic phospholipids | slight inhibition | Saccharomyces cerevisiae | |
| 3.6.1.75 | diphosphate | - |
Saccharomyces cerevisiae | |
| 3.6.1.75 | additional information | the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive | Escherichia coli | |
| 3.6.1.75 | additional information | the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive | Mus musculus | |
| 3.6.1.75 | additional information | the enzyme is insensitive to NEM and other sulfhydryl reagents | Saccharomyces cerevisiae | |
| 3.6.1.75 | NaF | - |
Saccharomyces cerevisiae | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.4 | additional information | - |
additional information | kinetic analysis, PA phosphatase activity on phosphatidate is cooperative | Saccharomyces cerevisiae | |
| 3.6.1.75 | additional information | - |
additional information | DGPP phosphatase exhibits typical saturation kinetics with respect to diacylglycerol diphosphate with a the Km value 3-fold greater than its cellular concentration | Escherichia coli |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.3.4 | cytosol | 75-kDA enzyme form | Saccharomyces cerevisiae | 5829 | - |
| 3.1.3.4 | membrane | - |
Saccharomyces cerevisiae | 16020 | - |
| 3.1.3.4 | microsome | 45-kDA enzyme form and 104-kDA enzyme form | Saccharomyces cerevisiae | - |
- |
| 3.1.3.4 | mitochondrion | 45-kDA enzyme form | Saccharomyces cerevisiae | 5739 | - |
| 3.6.1.75 | microsome | DPP1 is an integral membrane protein with six transmembrane helices, tightly associated with microsomal membranes | Saccharomyces cerevisiae | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.4 | Mg2+ | required | Saccharomyces cerevisiae | |
| 3.1.3.4 | Mg2+ | required for activity by all enzyme forms | Saccharomyces cerevisiae | |
| 3.6.1.75 | Mn2+ | potent inhibition | Escherichia coli | |
| 3.6.1.75 | additional information | the enzyme activity is independent of a divalent cation requirement, the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent | Saccharomyces cerevisiae | |
| 3.6.1.75 | additional information | the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent | Escherichia coli | |
| 3.6.1.75 | additional information | the phosphatidic acid phosphatase activity of the DGPP phosphatase is Mg2+-independent | Mus musculus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.4 | 45000 | - |
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE | Saccharomyces cerevisiae |
| 3.1.3.4 | 75000 | - |
cytosolic enzyme form, gel filtration | Saccharomyces cerevisiae |
| 3.1.3.4 | 91000 | - |
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE | Saccharomyces cerevisiae |
| 3.1.3.4 | 104000 | - |
x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE | Saccharomyces cerevisiae |
| 3.6.1.75 | 34000 | - |
x * 34000, DGPP phosphatase 1, SDS-PAGE | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.4 | additional information | Saccharomyces cerevisiae | the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol | ? | - |
? | |
| 3.1.3.4 | phosphatidate + H2O | Saccharomyces cerevisiae | biochemical regulation of PA phosphatases involving phospholipids, nucleotides ATP and CTP and the cAMP-dependent protein kinase A, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction, overview, PA phosphatase activity is regulated by biochemical and genetic mechanisms in a reciprocal manner with the regulation of the phospholipid biosynthetic enzyme phosphatidylserin synthase, overview | 1,2-diacyl-sn-glycerol + phosphate | - |
? | |
| 3.6.1.75 | 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 | - |
? | |
| 3.6.1.75 | diacylglycerol diphosphate + H2O | Saccharomyces cerevisiae | 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 | - |
? | |
| 3.6.1.75 | diacylglycerol diphosphate + H2O | Mus musculus | 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 | - |
? | |
| 3.6.1.75 | additional information | Saccharomyces cerevisiae | biochemical isozyme regulation mechanism, overview | ? | - |
? | |
| 3.6.1.75 | additional information | Mus musculus | PAP2 is involved in lipid signaling pathways | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.4 | Escherichia coli | - |
- |
- |
| 3.1.3.4 | Saccharomyces cerevisiae | - |
- |
- |
| 3.6.1.75 | Escherichia coli | - |
gene pgpB | - |
| 3.6.1.75 | Mus musculus | Q61469 | - |
- |
| 3.6.1.75 | Saccharomyces cerevisiae | Q05521 | DPP1; gene DPP1, isozyme DGPP phosphatase 1 | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.3.4 | phosphoprotein | the 45-kDa PA phosphatase is phosphorylated by protein kinase A, while the purified 104-kDa PA phosphatase is not a substrate, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction | Saccharomyces cerevisiae |
| 3.1.3.4 | proteolytic modification | the 91-kDa enzyme is a proteolysis product of a 104-kDa enzyme form, the 104-kDa PA phosphatase is not a precursor of the 45-kDa enzyme form | Saccharomyces cerevisiae |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.3.4 | 45-kDA, 91-kDA, and 104-kDa enzyme forms to homogeneity from membranes by sodium cholate solubilization of total membranes and subsequent anion exchange, affinity and hydroxylapatite chromatography followed by another step of anion exchange chromatgrphy and gel filtration, cytosolic enzyme form to homogeneity by ammonium sulfate and polyethylene glycol fractionation, steps followed by anion exchange chromatography, gel filtration, and adsorption chromatography | Saccharomyces cerevisiae |
| 3.1.3.4 | partial | Saccharomyces cerevisiae |
| 3.6.1.75 | 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 | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.4 | dicaproyl phosphatidate + H2O | best substrate of the 104-kDa enzyme form | Saccharomyces cerevisiae | 1,2-dicaproyl-sn-glycerol + phosphate | - |
? | |
| 3.1.3.4 | dioleoyl phosphatidate + H2O | - |
Saccharomyces cerevisiae | 1,2-dioleoyl-sn-glycerol + phosphate | - |
? | |
| 3.1.3.4 | dipalmitoyl phosphatidate + H2O | - |
Saccharomyces cerevisiae | 1,2-dipalmitoyl-sn-glycerol + phosphate | - |
? | |
| 3.1.3.4 | additional information | the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol | Saccharomyces cerevisiae | ? | - |
? | |
| 3.1.3.4 | phosphatidate + H2O | biochemical regulation of PA phosphatases involving phospholipids, nucleotides ATP and CTP and the cAMP-dependent protein kinase A, phosphorylation does not affect substrate binding but does alter the catalytic step in the reaction, overview, PA phosphatase activity is regulated by biochemical and genetic mechanisms in a reciprocal manner with the regulation of the phospholipid biosynthetic enzyme phosphatidylserin synthase, overview | Saccharomyces cerevisiae | 1,2-diacyl-sn-glycerol + phosphate | - |
? | |
| 3.1.3.4 | phosphatidic acid + H2O | - |
Escherichia coli | 1,2-diacyl-sn-glycerol + phosphate | - |
? | |
| 3.1.3.4 | phosphatidic acid + H2O | - |
Saccharomyces cerevisiae | 1,2-diacyl-sn-glycerol + phosphate | - |
? | |
| 3.6.1.75 | 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 | Escherichia coli | phosphatidate + phosphate | - |
? | |
| 3.6.1.75 | 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 | Saccharomyces cerevisiae | phosphatidate + phosphate | - |
? | |
| 3.6.1.75 | 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 | Mus musculus | phosphatidate + phosphate | - |
? | |
| 3.6.1.75 | diacylglycerol diphosphate + H2O | preferred substrate, the bifunctional enzyme 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 | Escherichia coli | phosphatidate + phosphate | - |
? | |
| 3.6.1.75 | diacylglycerol diphosphate + H2O | preferred substrate, the bifunctional enzyme 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 | Saccharomyces cerevisiae | phosphatidate + phosphate | - |
? | |
| 3.6.1.75 | additional information | biochemical isozyme regulation mechanism, overview | Saccharomyces cerevisiae | ? | - |
? | |
| 3.6.1.75 | additional information | PAP2 is involved in lipid signaling pathways | Mus musculus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.4 | ? | x * 45000, 45-kDA enzyme form, SDS-PAGE, x * 91000, 91-kDA enzyme form, SDS-PAGE, x * 104000, 104-kDa enzyme form, SDS-PAGE | Saccharomyces cerevisiae |
| 3.6.1.75 | ? | x * 34000, DGPP phosphatase 1, SDS-PAGE | Saccharomyces cerevisiae |
| 3.6.1.75 | More | the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity | Escherichia coli |
| 3.6.1.75 | More | the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity | Saccharomyces cerevisiae |
| 3.6.1.75 | More | the enzyme contains a specific three-domain lipid phosphatase motif required for catalytic activity | Mus musculus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.4 | PA phosphatase | - |
Saccharomyces cerevisiae |
| 3.6.1.75 | DGPP phosphatase | - |
Escherichia coli |
| 3.6.1.75 | DGPP phosphatase | - |
Saccharomyces cerevisiae |
| 3.6.1.75 | diacylglycerol pyrophosphate phosphatase | - |
Escherichia coli |
| 3.6.1.75 | diacylglycerol pyrophosphate phosphatase | - |
Saccharomyces cerevisiae |
| 3.6.1.75 | PAP2 | - |
Mus musculus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.4 | 30 | - |
inhibition of the 45-kDa and 104-kDa enzyme forms, unstable above | Saccharomyces cerevisiae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.4 | 6 | 7 | 45-kDa enzyme form | Saccharomyces cerevisiae |
| 3.1.3.4 | 7 | 8 | 75-kDa enzyme form | Saccharomyces cerevisiae |
| 3.1.3.4 | 7 | - |
104-kDa enzyme form | Saccharomyces cerevisiae |
| 3.6.1.75 | 6.5 | - |
- |
Escherichia coli |
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