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Literature summary extracted from

  • Oshiro, J.; Han, G.S.; Carman, G.M.
    Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae (2003), Biochim. Biophys. Acta, 1635, 1-9.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.4 additional information expression of the DPP1 gene, which encodes DGPP phosphatase, is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase, induction by zinc depletion is mediated by the transcription factor Zap1p, which binds to a zinc-responsive element in the DPP1 promoter Saccharomyces cerevisiae
3.6.1.75 additional information expression of the DPP1 gene, which encodes DGPP phosphatase, is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase, induction by zinc depletion is mediated by the transcription factor Zap1p, which binds to a zinc-responsive element in the DPP1 promoter Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.75 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 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.75 H169A site-directed mutagenesis, the mutant enzyme shows 9% of wild-type enzyme activity Saccharomyces cerevisiae
3.6.1.75 H223A site-directed mutagenesis, the mutant enzyme shows 0.03% of wild-type enzyme activity Saccharomyces cerevisiae
3.6.1.75 additional information dpp1DELTA mutants do not exhibit any dramatic phenotypes under a variety of growth conditions including fluctuations in zinc supplementation Saccharomyces cerevisiae
3.6.1.75 R125A site-directed mutagenesis, the mutant enzyme shows 0.05% of wild-type enzyme activity Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.4 4-chlormercuriphenylsulfonic acid
-
Saccharomyces cerevisiae
3.1.3.4 Ca2+
-
Saccharomyces cerevisiae
3.1.3.4 Co2+
-
Saccharomyces cerevisiae
3.1.3.4 diacylglycerol diphosphate conpetitive versus phosphatidate Saccharomyces cerevisiae
3.1.3.4 Mn2+
-
Saccharomyces cerevisiae
3.1.3.4 NEM potent inhibition of LPP1 Saccharomyces cerevisiae
3.1.3.4 Phenylglyoxal
-
Saccharomyces cerevisiae
3.1.3.4 phosphatidate conpetitive versus diacylglycerol diphosphate Saccharomyces cerevisiae
3.1.3.4 Zn2+
-
Saccharomyces cerevisiae
3.6.1.75 CDP-diacylglycerol
-
Saccharomyces cerevisiae
3.6.1.75 Cu2+
-
Saccharomyces cerevisiae
3.6.1.75 diphosphate
-
Saccharomyces cerevisiae
3.6.1.75 Mn2+
-
Saccharomyces cerevisiae
3.6.1.75 additional information no inhibition by NEM, phenylglyoxal, and sulfhydryl reagents, repression of DPP1 expression is mediated by the transcription factor Gis1p, which binds to three post-diauxic shift elements in the promoter Saccharomyces cerevisiae
3.6.1.75 NaF
-
Saccharomyces cerevisiae
3.6.1.75 Zn2+ the regulation of DPP1 expression in zinc-limited cells is dependent on the transcription factor Zap1p and binding to a cis-acting element, UASZRE, a zinc-responsive element, DPP1 expression is sensitive to the cytoplasmic levels of zinc, overview Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.75 vacuolar membrane associated Saccharomyces cerevisiae 5774
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.4 additional information the enzyme is Mg2+-independent and shows no divalent cation requirement for activity Saccharomyces cerevisiae
3.6.1.75 additional information the enzyme is Mg2+-independent and shows no divalent cation requirement for activity Saccharomyces cerevisiae

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.
3.1.3.4 diacylglycerol diphosphate + H2O Saccharomyces cerevisiae
-
phosphatidate + phosphate
-
?
3.1.3.4 phosphatidate + H2O Saccharomyces cerevisiae preferred substrate diacyl-sn-glycerol + 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 additional information Saccharomyces cerevisiae the phosphatidate phosphatase activity of the DGPP phosphatase enzyme is distinct from the conventional phosphatidate phosphatase enzymes, EC 3.1.3.4, that are presumably responsible for the synthesis of glycerophospholipids and triacylglycerols in Saccharomyces cerevisiae, the DPP1-encoded DGPP phosphatase is regulated by the stress conditions of zinc depletion, stationary phase, and by inositol supplementation, regulation mechanisms, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.4 Saccharomyces cerevisiae
-
gene LPP1
-
3.6.1.75 Saccharomyces cerevisiae
-
gene DPP1
-

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.75 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate the conserved residues Arg125, His169, and His223 within domains 1, 2, and 3, respectively, play important roles in the DGPP phosphatase and phosphatidic acid phosphatase reactions catalyzed by the enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.4 diacylglycerol diphosphate + H2O
-
Saccharomyces cerevisiae phosphatidate + phosphate
-
?
3.1.3.4 diacylglycerol diphosphate + H2O the bifunctional LPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it removes the phosphate from phosphatidate to form diacylglycerol Saccharomyces cerevisiae phosphatidate + phosphate
-
?
3.1.3.4 lysophosphatidic acid + H2O
-
Saccharomyces cerevisiae ?
-
?
3.1.3.4 additional information the LPP1-encoded enzyme has broad substrate specificity Saccharomyces cerevisiae ?
-
?
3.1.3.4 phosphatidate + H2O preferred substrate, the bifunctional LPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, reaction of EC 3.1.3.B2, and it removes the phosphate from phosphatidate to form diacylglycerol Saccharomyces cerevisiae 1,2-diacyl-sn-glycerol + phosphate
-
?
3.1.3.4 phosphatidate + H2O preferred substrate Saccharomyces cerevisiae 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 Saccharomyces cerevisiae phosphatidate + phosphate
-
?
3.6.1.75 additional information the phosphatidate phosphatase activity of the DGPP phosphatase enzyme is distinct from the conventional phosphatidate phosphatase enzymes, EC 3.1.3.4, that are presumably responsible for the synthesis of glycerophospholipids and triacylglycerols in Saccharomyces cerevisiae, the DPP1-encoded DGPP phosphatase is regulated by the stress conditions of zinc depletion, stationary phase, and by inositol supplementation, regulation mechanisms, overview Saccharomyces cerevisiae ?
-
?
3.6.1.75 additional information DGPP phosphatase utilizes several lipid phosphate substrates in vitro, including lysoPA, sphingoid base phosphates, isoprenoid phosphates, and phosphatidylglycerophosphate, the enzyme contains a three-domain lipid phosphatase motif required for catalytic activity Saccharomyces cerevisiae ?
-
?

Subunits

EC Number Subunits Comment Organism
3.6.1.75 ? x * 34000, SDS-PAGE Saccharomyces cerevisiae
3.6.1.75 More the enzyme contains a three-domain lipid phosphatase motif required for catalytic activity and six transmembrane-spanning regions distributed over the entire polypeptide sequence, topography of the phosphatase sequence motif of the DPP1-encoded DGPP phosphatase, overview Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.1.3.4 More cf. EC 3.1.3.B2, the enzyme is a member of the lipid phosphate phosphatase superfamily Saccharomyces cerevisiae
3.6.1.75 DGPP phosphatase
-
Saccharomyces cerevisiae
3.6.1.75 diacylglycerol pyrophosphate phosphatase
-
Saccharomyces cerevisiae
3.6.1.75 More cf. EC 3.1.3.4, the enzyme is a member of the lipid phosphate phosphatase superfamily Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.75 5 6
-
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