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diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
additional information
?
-
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
preferred substrate of isozyme DPPL1
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
preferred substrate of isozyme DPPL2
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
diacylglycerol diphosphate metabolism, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
9.3fold preferred substrate compared to phosphatidic acid, 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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional enzyme 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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional PAP2 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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
product identification by TLC
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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, genetic regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional Dpp1p 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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the substrate and product of the DGPP phosphatase reaction play roles in lipid signaling and in cell metabolism
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
preferred substrate, the bifunctional enzyme 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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate, the enzyme removes the beta phosphate from DGPP to form phosphatidate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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
product identification by TLC
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
additional information
?
-
-
no activity with ADP, 4-nitrophenylphosphate, and diphosphate
-
-
?
additional information
?
-
PAP2 is involved in lipid signaling pathways
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
additional information
?
-
biochemical isozyme regulation mechanism, overview
-
-
?
additional information
?
-
-
DGPP phosphatase plays a role in the regulation of phospholipid metabolism by inositol, as well as regulating the cellular levels of phosphatidylinositol, regulation of DGPP phosphatase by inositol and growth phase, overview
-
-
?
additional information
?
-
-
DPP1 is a zinc-regulated gene, and it contains a putative zinc-responsive element, UASZRE, in its promoter, regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
DGPP stimulates the activity of pure phosphatidylserine synthase by a mechanism that increases the affinity of the enzyme for its substrate CDP-diacylglycerol
-
-
?
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diacylglycerol diphosphate + H2O
phosphatidate + phosphate
additional information
?
-
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
diacylglycerol diphosphate metabolism, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
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, genetic regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional Dpp1p 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
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the substrate and product of the DGPP phosphatase reaction play roles in lipid signaling and in cell metabolism
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
preferred substrate
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
the bifunctional DPP1 catalyzes the removal of the beta-phosphate from diacylglycerol diphosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol, which is the reaction of EC 3.1.3.4, zinc-mediated regulation, overview
-
-
?
diacylglycerol diphosphate + H2O
phosphatidate + phosphate
-
-
-
-
?
additional information
?
-
PAP2 is involved in lipid signaling pathways
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
additional information
?
-
biochemical isozyme regulation mechanism, overview
-
-
?
additional information
?
-
-
DGPP phosphatase plays a role in the regulation of phospholipid metabolism by inositol, as well as regulating the cellular levels of phosphatidylinositol, regulation of DGPP phosphatase by inositol and growth phase, overview
-
-
?
additional information
?
-
-
DPP1 is a zinc-regulated gene, and it contains a putative zinc-responsive element, UASZRE, in its promoter, regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of the cellular levels of diacylglycerol diphosphate, phosphatidate, and diacylglycerol
-
-
?
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
-
-
?
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4-chloromercuriphenylsulfonic acid
-
41% inhibition at 1 mM
ADP
-
24% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
phosphatidate
-
competitive versus diacylglycerol diphosphate
sphingosine
-
inhibition of both isozymes, overview
sphingosine 1-phosphate
-
-
Ca2+
-
inhibition of both isozymes, overview
CDP-diacylglycerol
-
-
CDP-diacylglycerol
-
mixed inhibition mechanism
diacylglycerol
-
slight inhibition
diacylglycerol
-
DPP1-encoded PAP2 enzyme is inhibited by CDP-DAG
diphosphate
-
diphosphate
-
48% inhibition at a 10fold excess of inhibitor to substrate diacylglycerol diphosphate
Mg2+
-
inhibition of both isozymes, overview
Mn2+
-
inhibition of both isozymes, overview
Mn2+
-
complete inhibition at about 0.075 mM MnCl2
Mn2+
-
the inhibition of DGPP phosphatase activity by Mn2+ ions follows positive cooperative kinetics
NaF
-
inhibition of both isozymes, overview
NaF
-
94% inhibition at 10 mM
NEM
inhibition of isozyme DPPL1; inhibition of isozyme DPPL2
NEM
-
10% inhibition at 5 mM
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
Zn2+
-
the DGPP phosphatase activity is inhibited by zinc by a mechanism that involves formation of DGPP-zinc complexes, overview
Zn2+
-
zinc depletion increases the enzyme activity in vivo, stress condition of zinc depletion induces DPP1 expression
Zn2+
-
DPP1-encoded PAP2 activity is inhibited by Zn2+ ions in a mechanism that involves the formation of DGPP-Zn2+ complexes
additional information
-
no inhibition by EDTA and NEM of both isozymes
-
additional information
-
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
-
additional information
-
the enzyme is insensitive to NEM and other sulfhydryl reagents
-
additional information
the phosphatidic acid phosphatase activity of the DGPP phosphatase is NEM-insensitive
-
additional information
-
no inhibition by N-ethylmaleimide and bromoenol lactone, and by EDTA and EGTA
-
additional information
the enzyme is insensitive to NEM and other sulfhydryl reagents
-
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
-
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
-
additional information
-
no or poor inhibition by phospholipids, overview
-
additional information
-
Dpp1p, DPP1-encoded PAP2 activity, is NEM-insensitive
-
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H169A
-
site-directed mutagenesis of the phosphatase sequence motif residue, the mutant shows 9% of wild-type enzyme DGPP phosphatase activity and no phosphatidic acid phosphatase activity
H169A
-
site-directed mutagenesis, the mutant enzyme shows 9% of wild-type enzyme activity
H223A
-
site-directed mutagenesis of the phosphatase sequence motif residue, the mutant shows 0.03% of wild-type enzyme DGPP phosphatase activity and no phosphatidic acid phosphatase activity
H223A
-
site-directed mutagenesis, the mutant enzyme shows 0.03% of wild-type enzyme activity
R125A
-
site-directed mutagenesis of the phosphatase sequence motif residue, the mutant shows 0.05% of wild-type enzyme DGPP phosphatase activity and no phosphatidic acid phosphatase activity
R125A
-
site-directed mutagenesis, the mutant enzyme shows 0.05% of wild-type enzyme activity
additional information
-
a gene pgpB mutant shows defect in phosphatidic acid phosphatase activity and also exhibits defects in lysophosphatidic acid phosphatase and phosphatidylglycerophosphate phosphatase activities
additional information
-
mutant strain CF20 is defective in gene pgpB and in phosphatidic acid phosphatase, lysophosphatidic acid phosphatase, and phosphatidylglycerophosphate phosphatase activities, while the overexpressing strain JM103 shows an enhancement of these activities, overview
additional information
-
construction of a dpp1D mutant by deletion of the chromosomal copy of theDPP1 gene, the dpp1D mutant is viable and does not exhibit any obvious growth defects, the mutant is devoid of DGPP phosphatase activity and accumulates DGPP 4-fold compared to wild-type levels, phenotype, overview
additional information
-
construction of a mutant by deletions from the 5' end of the promoter indicated sequences responsible for enzyme expression, mutations in the three URSPDS elements within the DPP1 promoter abolish Gis1p-DNA interactions in vitro and abolish the regulation of DPP1 in vivo
additional information
-
dpp1DELTA mutants do not exhibit any dramatic phenotypes under a variety of growth conditions including fluctuations in zinc supplementation
additional information
-
the regulation pattern of DGPP phosphatase in mutants defective in plasma membrane, Zrt1p and Zrt2p, and vacuolar membrane, Zrt3p, zinc transporters indicates that the enzyme expression is sensitive to the cytoplasmic levels of zinc
additional information
-
construction of a dpp1D mutant by deletion of the chromosomal copy of theDPP1 gene, the dpp1D mutant is viable and does not exhibit any obvious growth defects, the mutant is devoid of DGPP phosphatase activity and accumulates DGPP 4-fold compared to wild-type levels, phenotype, overview
-
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DPP1 is a zinc-regulated gene, and it contains a putative zinc-responsive element, UASZRE, in its promoter, regulation mechanism, overview
-
expression from a plasmid vector bearing the PDPP1-lacZ reporter gene, expression analysis in presence or absence of inositol
-
expression of isozyme DPPL1 in Spodoptera frugiperda Sf9 cells
expression of isozyme DPPL2 in Spodoptera frugiperda Sf9 cells
gene DPP1, DNA and amino acid sequence determination and analysis, overexpression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method, subcloning in Escherichia coli strain DH5alpha
-
gene DPP1, expression of wild-type and phosphatase sequence motif mutant enzymes in an enzyme-deficient mutant yeast strain, subcloning in Escherichia coli strain DH5alpha and XL-1 bLue
-
gene DPP1, functional overexpression of HA-tagged enzyme in the DPP1-deficient mutant Saccharomyces cerevisiae strain DTY1 in vacuole membranes, the transcription factor Zap1p binds the DPP1 promoter and induces the expression of DGPP phosphatase
-
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
-
gene DPP1, location on chromosome IV, DNA and amino acid sequence determination and analysis
gene DPP1, subcloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), promoter structure determination and analysis, identification of three binding sites, URSPDS, for transcription factor Gis1p in the DPP1 promoter, direct interaction between Gis1p and DPP1 promoter elements, analysis of genetic regulation, overview
-
gene pgpB, overexpression in strain JM103 leads to 370fold increased Mg2+-independent phosphatidic acid phosphatase activity and to 310fold increased DGPP phosphatase activity
-
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Carman, G.M.
Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli
Biochim. Biophys. Acta
1348
45-55
1997
Escherichia coli, Saccharomyces cerevisiae (Q05521), Mus musculus (Q61469)
brenda
Toke, D.A.; McClintick, M.L.; Carman, G.M.
Mutagenesis of the phosphatase sequence motif in diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae
Biochemistry
38
14606-14613
1999
Saccharomyces cerevisiae
brenda
Oshiro, J.; Han, G.S.; Carman, G.M.
Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1635
1-9
2003
Saccharomyces cerevisiae
brenda
Takeuchi, M.; Harigai, M.; Momohara, S.; Ball, E.; Abe, J.; Furuichi, K.; Kamatani, N.
Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase
Gene
399
174-180
2007
Homo sapiens (Q5VZY2), Homo sapiens (Q8NEB5)
brenda
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
J. Biol. Chem.
271
1868-1876
1996
Saccharomyces cerevisiae, Saccharomyces cerevisiae MATa ade5
brenda
Dillon, D.A.; Wu, W.I.; Riedel, B.; Wissing, J.B.; Dowhan, W.; Carman, G.M.
The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity
J. Biol. Chem.
271
30548-30553
1996
Escherichia coli
brenda
Dillon, D.A.; Chen, X.; Zeimetz, G.M.; Wu, W.I.; Waggoner, D.W.; Dewald, J.; Brindley, D.N.; Carman, G.M.
Mammalian Mg2+-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity
J. Biol. Chem.
272
10361-10366
1997
Saccharomyces cerevisiae, Rattus norvegicus
brenda
Toke, D.A.; Bennett, W.L.; Dillon, D.A.; Wu, W.I.; Chen, X.; Ostrander, D.B.; Oshiro, J.; Cremesti, A.; Voelker, D.R.; Fischl, A.S.; Carman, G.M.
Isolation and characterization of the Saccharomyces cerevisiae DPP1 gene encoding diacylglycerol pyrophosphate phosphatase
J. Biol. Chem.
273
3278-3284
1998
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
brenda
Oshiro, J.; Rangaswamy, S.; Chen, X.; Han, G.S.; Quinn, J.E.; Carman, G.M.
Regulation of the DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol and growth phase. Inhibition of DGPP phosphatase activity by CDP-diacylglyceron and activation of phosphatidylserine synthase activity by DGPP
J. Biol. Chem.
275
40887-40896
2000
Saccharomyces cerevisiae
brenda
Han, G.S.; Johnston, C.N.; Chen, X.; Athenstaedt, K.; Daum, G.; Carman, G.M.
Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc
J. Biol. Chem.
276
10126-10133
2001
Saccharomyces cerevisiae
brenda
Oshiro, J.; Han, G.S.; Iwanyshyn, W.M.; Conover, K.; Carman, G.M.
Regulation of the yeast DPP1-encoded diacylglycerol pyrophosphate phosphatase by transcription factor Gis1p
J. Biol. Chem.
278
31495-31503
2003
Saccharomyces cerevisiae
brenda
Han, G.S.; Johnston, C.N.; Carman, G.M.
Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae
J. Biol. Chem.
279
5338-5345
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
brenda
Riedel, B.; Morr, M.; Wu, W.I.; Carman, G.M.; Wissing, J.B.
Metabolism of diacylglycerol pyrophosphate by suspension cultured Catharanthus roseus cells. Identification and characterization of diacylglycerol pyrophosphate phosphatase in plants
Plant Sci.
128
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