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 |
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 |
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 |
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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.6.1.75 | vacuolar membrane | associated | Saccharomyces cerevisiae | 5774 | - |
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 |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.6.1.75 | 34000 | - |
x * 34000, SDS-PAGE | Saccharomyces cerevisiae |
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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.4 | Saccharomyces cerevisiae | - |
gene LPP1 | - |
3.6.1.75 | Saccharomyces cerevisiae | - |
gene DPP1 | - |
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 |
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 |
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 | ? | - |
? |
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 |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.6.1.75 | 5 | 6 | - |
Saccharomyces cerevisiae |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.6.1.75 | additional information | - |
additional information | - |
Saccharomyces cerevisiae |