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Literature summary extracted from

  • Wu, W.I.; Liu, Y.; Riedel, B.; Wissing, J.B.; Fischl, A.S.; Carman, G.M.
    Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae (1996), J. Biol. Chem., 271, 1868-1876.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.1.75 phosphatidylethanolamine
-
 Saccharomyces cerevisiae
3.6.1.75 phosphatidylinositol
-
 Saccharomyces cerevisiae
3.6.1.75 Triton X-100 addition of Triton X-100 stimulates DGPP phosphatase activity to a maximum at a concentration of 2 mM Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.75 4-chloromercuriphenylsulfonic acid 41% inhibition at 1 mM Saccharomyces cerevisiae
3.6.1.75 ADP 24% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate Saccharomyces cerevisiae
3.6.1.75 Ca2+
-
 Saccharomyces cerevisiae
3.6.1.75 diacylglycerol slight inhibition Saccharomyces cerevisiae
3.6.1.75 diphosphate 48% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate Saccharomyces cerevisiae
3.6.1.75 Mg2+
-
 Saccharomyces cerevisiae
3.6.1.75 Mn2+
-
 Saccharomyces cerevisiae
3.6.1.75 additional information poor inhibition by ATP and AMP, the enzyme is inhibited by divalent cations, but is relatively insensitive to thioreactive agents, no inhibition by phospholipids or phosphatidic acid versus diacylglycerol diphosphate as substrate, no inhibition by EDTA, glycerol 3-phosphate, and inositol 1-phosphate Saccharomyces cerevisiae
3.6.1.75 NaF 94% inhibition at 10 mM Saccharomyces cerevisiae
3.6.1.75 NEM 10% inhibition at 5 mM Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.75 additional information
-
 additional information kinetics, the DGPP phosphatase exhibits typical saturation kinetics with respect to DGPP, the Km value for diacylglycerol diphosphate is 3fold greater than its cellular concentration of 0.18 mol% Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.75 membrane associated Saccharomyces cerevisiae 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.75 34000
-
 x * 34000, SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.75 diacylglycerol diphosphate + H2O Saccharomyces cerevisiae preferred substrate phosphatidate + phosphate
-
 ?
3.6.1.75 diacylglycerol diphosphate + H2O Saccharomyces cerevisiae MATa ade5 preferred substrate phosphatidate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.75 Saccharomyces cerevisiae
-
-
-
3.6.1.75 Saccharomyces cerevisiae MATa ade5
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.75 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 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.75 150
-
 purified enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.75 diacylglycerol diphosphate + H2O preferred substrate 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 Saccharomyces cerevisiae phosphatidate + phosphate product identification by TLC ?
3.6.1.75 diacylglycerol diphosphate + H2O preferred substrate Saccharomyces cerevisiae MATa ade5 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 MATa ade5 phosphatidate + phosphate product identification by TLC ?

Subunits

EC Number Subunits Comment Organism
3.6.1.75 ? x * 34000, SDS-PAGE Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.6.1.75 DGPP phosphatase
-
 Saccharomyces cerevisiae
3.6.1.75 diacylglycerol pyrophosphate phosphatase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.75 30
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6.1.75 40.9
-
 diacylglycerol diphosphate pH 6.5, 30°C Saccharomyces cerevisiae
3.6.1.75 96.67
-
 diacylglycerol diphosphate pH 6.5, 30°C Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.75 6 8.5
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.6.1.75 additional information
-
 additional information
-
 Saccharomyces cerevisiae
3.6.1.75 0.058
-
 Mn2+ pH 6.5, 30°C Saccharomyces cerevisiae
3.6.1.75 0.56
-
 Ca2+ pH 6.5, 30°C Saccharomyces cerevisiae
3.6.1.75 17
-
 Mg2+ pH 6.5, 30°C Saccharomyces cerevisiae