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Literature summary for 3.1.3.4 extracted from

  • Carman, G.M.
    Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli (1997), Biochim. Biophys. Acta, 1348, 45-55.
    View publication on PubMed

Activating Compound

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

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 [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

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

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae
Mg2+ required for activity by all enzyme forms Saccharomyces cerevisiae

Molecular Weight [Da]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

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 (Commentary)

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 and Products (Substrate)

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

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

Synonyms Comment Organism
PA phosphatase
-
Saccharomyces cerevisiae

Temperature Stability [°C]

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

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