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Synonyms
cdp-diacylglycerol synthase, cdp-dg, phosphatidate cytidylyltransferase, tam41, cdp-dag synthase, tamm41, ctp:phosphatidate cytidylyltransferase, cdp-diglyceride synthetase, cdp-dg synthase, tbcds,
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CDP diacylglycerol synthase
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CDP-DG synthetase
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CDP-diacylglyceride synthetase
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CDP-diacylglycerol synthase
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CDP-diglyceride pyrophosphorylase
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CDP-diglyceride synthetase
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CDPdiglyceride pyrophosphorylase
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CTP-diacylglycerol synthetase
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CTP:1,2-diacylglycerophosphate-cytidyl transferase
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CTP:phosphatidate cytidylyltransferase
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cytidine diphosphoglyceride pyrophosphorylase
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cytidylyltransferase, phosphatidate
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phosphatidate cytidyltransferase
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phosphatidic acid cytidylyltransferase
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CTP + 1,2-dioleoyl-sn-glycerol 3-phosphate
diphosphate + CDP-1,2-dioleoylglycerol
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CTP + 1-stearoyl-2-arachidonoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoylglycerol
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
the enzyme prefers 1-stearoyl-2-arachidonoyl phosphatidic acid as substrate. Little or no activity is detected towards phosphatidic acids containing saturated fatty acyl groups in both the sn-1 and sn-2 positions
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CTP + 1,2-diarachidonoyl phosphatidic acid
diphosphate + CDP-1,2-diarachidonoylglycerol
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CTP + 1,2-dicaproyl phosphatidic acid
diphosphate + CDP-1,2-dicaproylglycerol
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CTP + 1,2-dioleoyl phosphatidic acid
diphosphate + CDP-dioleoylglycerol
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CTP + 1,2-dipalmitoyl phosphatidic acid
diphosphate + CDP-dipalmitoylglycerol
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CTP + 1,2-distearoyl phosphatidic acid
diphosphate + CDP-1,2-distearoylglycerol
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CTP + 1-arachidonoyl-2-stearoyl phosphatidic acid
diphosphate + CDP-1-arachidonoyl-2-stearoylglycerol
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CTP + 1-oleoyl-2-stearoyl phosphatidic acid
diphosphate + CDP-1-oleoyl-2-stearoylglycerol
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CTP + 1-palmitoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-oleoylglycerol
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CTP + 1-stearoyl-2-arachidonoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoylglycerol
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CTP + 1-stearoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-oleoylglycerol
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CTP + phosphatidate
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
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CTP + phosphatidate
diphosphate + CDP-diacylglycerol
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CTP + phosphatidate
diphosphate + CDP-diacylglycerol
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involved in the de novo biosynthesis of cardiolipin
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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reaction with 1,2-dioleoylphosphatidic acid. Varying the fatty acid composition in the phosphatidic acids added exogenously gives the following order of decreasing activity: 1-stearoyl-2-oleoylphosphatidic acid, 1-oleoyl-2-stearoylphosphatidic acid, 1,2-dioleoylphosphatidic acid, 1-palmitoyl-2-oleoylphosphatidic acid, 1-stearoyl-2-arachidonoylphosphatidic acid, 1-arachidonoyl-2-stearoylphosphatidic acid, 1,2-diarachidonoylphosphatidic acid, 1,2-dicaproylphosphatidic acid, 1,2-dipalmitoylphosphatidic acid, 1,2-distearoylphosphatidic acid
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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the enzyme shows a linear increase in activity with membrane-bound phosphatidate concentrations up to at least 100 nmol phosphatidate per mg of microsomal protein. The enzyme has a large reserve capacity and suggests that the enzyme is operating intracellularly, i.e. at phosphatidate concentrations of 5-10 mM/mg endoplasmic reticulum protein, far below the maximal capacity. The ratio of phosphatidate conversion into CDP diglyceride and 1,2-diglyceride seems to be constant for a large range of membrane-bounmd phosphatidate concentrations. The membrane-bound enzyme cannot utilize phosphatidate substrate present in heat denatured membranes, but is active on phosphatidate incorporated into membranes of phospholipid vesicles
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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mammalian enzymes show similar efficacy for CTP and dCTP, however CTP is the preferred substrate in vivo, since dCDP-diacylglycerol is not detectable in mammalian tissues. In Escherichia coli equivalent amounts of CDP-diacylglycerol and dCDP-diacylglycerol are detected. Arabinofuranosylcytosine is also found to be incorporated into lipid in mammalian cells, suggesting that it is a substrate for the enzyme
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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enzyme plays a central role in phospholipid biosynthesis
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dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
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dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
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mammalian enzymes show similar efficacy for CTP and dCTP, however CTP is the preferred substrate in vivo, since dCDP-diacylglycerol is not detectable in mammalian tissues. In Escherichia coli equivalent amounts of CDP-diacylglycerol and dCDP-diacylglycerol are detected. Arabinofuranosylcytosine is also found to be incorporated into lipid in mammalian cells, suggesting that it is a substrate for the enzyme
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CTP + phosphatidate
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
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mammalian enzymes show similar efficacy for CTP and dCTP, however CTP is the preferred substrate in vivo, since dCDP-diacylglycerol is not detectable in mammalian tissues. In Escherichia coli equivalent amounts of CDP-diacylglycerol and dCDP-diacylglycerol are detected. Arabinofuranosylcytosine is also found to be incorporated into lipid in mammalian cells, suggesting that it is a substrate for the enzyme
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CTP + phosphatidate
diphosphate + CDP-diacylglycerol
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CTP + phosphatidate
diphosphate + CDP-diacylglycerol
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involved in the de novo biosynthesis of cardiolipin
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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mammalian enzymes show similar efficacy for CTP and dCTP, however CTP is the preferred substrate in vivo, since dCDP-diacylglycerol is not detectable in mammalian tissues. In Escherichia coli equivalent amounts of CDP-diacylglycerol and dCDP-diacylglycerol are detected. Arabinofuranosylcytosine is also found to be incorporated into lipid in mammalian cells, suggesting that it is a substrate for the enzyme
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CTP + phosphatidate
diphosphate + CDPdiacylglycerol
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enzyme plays a central role in phospholipid biosynthesis
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?
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Mok, A.Y.P.; McDougall, G.E.; McMurray, W.C.
CDP-diacylglycerol synthesis in rat liver mitochondria
FEBS Lett.
312
236-240
1992
Rattus norvegicus
brenda
Liteplo, R.G.; Sribney, M.
The stimulation of rat liver microsomal CTP: phosphatidate cytidylyltransferase activity by guanosine triphosphate
Biochim. Biophys. Acta
619
660-668
1980
Rattus norvegicus
brenda
Sribney, M.; Dove, J.L.; Lyman, E.M.
Studies on the synthesis of CDP-diacylglycerol: stimulation by GTP and inhibition by ATP and fluoride
Biochim. Biophys. Acta
79
749-755
1977
Rattus norvegicus
brenda
Bishop, H.H.; Strickland, K.P.
Studies on the formation by rat brain preparations of CDP-diglyceride from CTP and phosphatidic acids of varying fatty acid compositions
Can. J. Biochem.
54
249-260
1976
Rattus norvegicus
brenda
Sturton, R.G.; Brindley, D.N.
Factors controlling the activities of phosphatidate phosphohydrolase and phosphatidate cytidylyltransferase. The effects of chlorpromazine, demethylimipramine, cinchocaine, norfenfluramine, mepyramine and magnesium ions
Biochem. J.
162
25-32
1977
Rattus norvegicus
brenda
Van Heusden, G.P.H.; Van den Bosch, H.
The influence of exogenous and of membrane-bound phosphatidate concentration on the activity of CTP: phosphatidate cytidylyltransferase and phosphatidate phosphohydrolase
Eur. J. Biochem.
84
405-412
1978
Rattus norvegicus
brenda
Heacock, A.M.; Agranoff, B.W.
CDP-diacylglycerol synthase from mammalian tissues
Biochim. Biophys. Acta
1348
166-172
1997
Cavia porcellus, Drosophila sp. (in: flies), Escherichia coli, Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Monaco, M.E.; Feldman, M.
Extraction and stabilization of mammalian CDP-diacylglycerol synthase activity
Biochem. Biophys. Res. Commun.
239
166-170
1997
Rattus norvegicus
brenda
Saito, S.; Goto, K.; Tonosaki, A.; Kondo, H.
Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain
J. Biol. Chem.
272
9503-9509
1997
Rattus norvegicus (O35052)
brenda
Jiang, Y.J.; Lu, B.; Xu, F.Y.; Gartshore, J.; Taylor, W.A.; Halayko, A.J.; Gonzalez, F.J.; Takasaki, J.; Choy, P.C.; Hatch, G.M.
Stimulation of cardiac cardiolipin biosynthesis by PPARalpha activation
J. Lipid Res.
45
244-252
2004
Mus musculus, Rattus norvegicus
brenda
Blunsom, N.J.; Gomez-Espinosa, E.; Ashlin, T.G.; Cockcroft, S.
Mitochondrial CDP-diacylglycerol synthase activity is due to the peripheral protein, TAMM41 and not due to the integral membrane protein, CDP-diacylglycerol synthase 1
Biochim. Biophys. Acta Mol. Cell Biol. Lipids
1863
284-298
2018
Rattus norvegicus (D3ZKT0)
brenda