Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cardiolipin | activation, antagonized by sphinganine | Saccharomyces cerevisiae | |
CDP-diacylglycerol | - |
Saccharomyces cerevisiae | |
additional information | no effect on the enzyme forms by choline | Saccharomyces cerevisiae | |
phosphatidylinositol | activation, antagonized by sphinganine | Saccharomyces cerevisiae | |
Triton X-100 | the 45-kDa and 104-kDa enzyme forms are dependent on Triton X-100 for activity | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 | |
additional information | no effect on the enzyme forms by choline | Saccharomyces cerevisiae | |
N-ethylmaleimide | inhibition of the 45-kDa and 104-kDa enzyme forms | Saccharomyces cerevisiae | |
NEM | - |
Saccharomyces cerevisiae | |
Phenylglyoxal | inhibition of the 45-kDa and 104-kDa enzyme forms | Saccharomyces cerevisiae | |
propranolol | inhibition of the 45-kDa and 104-kDa enzyme forms | Saccharomyces cerevisiae | |
Zwitterionic phospholipids | slight inhibition | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic analysis, PA phosphatase activity on phosphatidate is cooperative | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | 75-kDA enzyme form | Saccharomyces cerevisiae | 5829 | - |
membrane | - |
Saccharomyces cerevisiae | 16020 | - |
microsome | 45-kDA enzyme form and 104-kDA enzyme form | Saccharomyces cerevisiae | - |
- |
mitochondrion | 45-kDA enzyme form | Saccharomyces cerevisiae | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae | |
Mg2+ | required for activity by all enzyme forms | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
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 |
75000 | - |
cytosolic enzyme form, gel filtration | Saccharomyces cerevisiae |
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 |
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 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol | ? | - |
? | |
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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 |
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 (Comment) | Organism |
---|---|
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 |
partial | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dicaproyl phosphatidate + H2O | best substrate of the 104-kDa enzyme form | Saccharomyces cerevisiae | 1,2-dicaproyl-sn-glycerol + phosphate | - |
? | |
dioleoyl phosphatidate + H2O | - |
Saccharomyces cerevisiae | 1,2-dioleoyl-sn-glycerol + phosphate | - |
? | |
dipalmitoyl phosphatidate + H2O | - |
Saccharomyces cerevisiae | 1,2-dipalmitoyl-sn-glycerol + phosphate | - |
? | |
additional information | the enzyme plays a major role in the synthesis of phospholipid and triacylglycerol | Saccharomyces cerevisiae | ? | - |
? | |
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 | - |
? | |
phosphatidic acid + H2O | - |
Escherichia coli | 1,2-diacyl-sn-glycerol + phosphate | - |
? | |
phosphatidic acid + H2O | - |
Saccharomyces cerevisiae | 1,2-diacyl-sn-glycerol + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | 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 |
Synonyms | Comment | Organism |
---|---|---|
PA phosphatase | - |
Saccharomyces cerevisiae |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
inhibition of the 45-kDa and 104-kDa enzyme forms, unstable above | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 7 | 45-kDa enzyme form | Saccharomyces cerevisiae |
7 | 8 | 75-kDa enzyme form | Saccharomyces cerevisiae |
7 | - |
104-kDa enzyme form | Saccharomyces cerevisiae |