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CTP + 1,2-diarachidonoyl phosphatidic acid
diphosphate + CDP-1,2-diarachidonoylglycerol
-
-
-
-
?
CTP + 1,2-diarachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-diarachidonoylglycerol
CTP + 1,2-dicaproyl phosphatidic acid
diphosphate + CDP-1,2-dicaproylglycerol
-
-
-
-
?
CTP + 1,2-dilinoleoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-dilinoleoylglycerol
CTP + 1,2-dioleoyl phosphatidic acid
diphosphate + CDP-dioleoylglycerol
CTP + 1,2-dioleoyl-sn-glycero-3-phosphate
diphosphate + CDP-1,2-dioleoylglycerol
CTP + 1,2-dioleoyl-sn-glycerol 3-phosphate
diphosphate + CDP-1,2-dioleoylglycerol
-
-
-
?
CTP + 1,2-dioleoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-dioleoylglycerol
CTP + 1,2-diolinoleoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-diolinoleoylglycerol
-
-
-
?
CTP + 1,2-dipalmitoyl phosphatidic acid
diphosphate + CDP-dipalmitoylglycerol
CTP + 1,2-distearoyl phosphatidic acid
diphosphate + CDP-1,2-distearoylglycerol
-
-
-
-
?
CTP + 1-arachidonoyl-2-stearoyl phosphatidic acid
diphosphate + CDP-1-arachidonoyl-2-stearoylglycerol
-
-
-
-
?
CTP + 1-oleoyl-2-palmitoyl phosphatidic acid
diphosphate + CDP-1-oleoyl-2-palmitoylglycerol
-
reaction with 1-oleoyl-2-palmitoyl phosphatidic acid at 83.4% of the activity with phosphatidic acid from egg phosphatidylcholine
-
-
?
CTP + 1-oleoyl-2-stearoyl phosphatidic acid
diphosphate + CDP-1-oleoyl-2-stearoylglycerol
-
-
-
-
?
CTP + 1-palmitoyl-2-arachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-arachidonoylglycerol
CTP + 1-palmitoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-oleoylglycerol
CTP + 1-palmitoyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphate
diphosphate + CDP-1-palmitoyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]glycerol
i.e. commercial substrate NBD-PA
-
-
?
CTP + 1-stearoyl-2-arachidonoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoylglycerol
CTP + 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoyl-glycerol
-
-
-
?
CTP + 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoylglycerol
-
-
-
?
CTP + 1-stearoyl-2-docosahexaenoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-docosahexaenoylglycerol
-
-
-
?
CTP + 1-stearoyl-2-linoleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-linoleoyl-glycerol
-
-
-
?
CTP + 1-stearoyl-2-linoleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-linoleoylglycerol
CTP + 1-stearoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-oleoylglycerol
-
-
-
-
?
CTP + 1-stearoyl-2-oleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-oleoylglycerol
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
additional information
?
-
CTP + 1,2-diarachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-diarachidonoylglycerol
-
-
-
?
CTP + 1,2-diarachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-diarachidonoylglycerol
50% of the activity with 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + 1,2-dilinoleoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-dilinoleoylglycerol
-
-
-
?
CTP + 1,2-dilinoleoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-dilinoleoylglycerol
20% of the activity with 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + 1,2-dioleoyl phosphatidic acid
diphosphate + CDP-dioleoylglycerol
-
-
-
?
CTP + 1,2-dioleoyl phosphatidic acid
diphosphate + CDP-dioleoylglycerol
-
reaction with 1-oleoyl-2-palmitoyl-phosphatidic acid at 87.5% of the activity with phosphatidic acid from egg phosphatidylcholine
-
-
?
CTP + 1,2-dioleoyl phosphatidic acid
diphosphate + CDP-dioleoylglycerol
-
-
-
-
?
CTP + 1,2-dioleoyl-sn-glycero-3-phosphate
diphosphate + CDP-1,2-dioleoylglycerol
-
-
-
?
CTP + 1,2-dioleoyl-sn-glycero-3-phosphate
diphosphate + CDP-1,2-dioleoylglycerol
-
-
-
?
CTP + 1,2-dioleoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-dioleoylglycerol
-
-
-
?
CTP + 1,2-dioleoyl-sn-phosphatidic acid
diphosphate + CDP-1,2-dioleoylglycerol
less than 5% of the activity with 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + 1,2-dipalmitoyl phosphatidic acid
diphosphate + CDP-dipalmitoylglycerol
best substrate
-
-
?
CTP + 1,2-dipalmitoyl phosphatidic acid
diphosphate + CDP-dipalmitoylglycerol
-
-
-
-
?
CTP + 1,2-dipalmitoyl phosphatidic acid
diphosphate + CDP-dipalmitoylglycerol
-
reaction with 1-oleoyl-2-palmitoyl phosphatidic acid at 4.6% of the activity with phosphatidic acid from egg phosphatidylcholine
-
-
?
CTP + 1,2-dipalmitoyl phosphatidic acid
diphosphate + CDP-dipalmitoylglycerol
-
-
-
-
?
CTP + 1-palmitoyl-2-arachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-arachidonoylglycerol
-
-
-
?
CTP + 1-palmitoyl-2-arachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-arachidonoylglycerol
65% of the activity with 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + 1-palmitoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-oleoylglycerol
best substrate
-
-
?
CTP + 1-palmitoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-oleoylglycerol
-
reaction with 1-oleoyl-2-palmitoyl phosphatidic acid at 99.7% of the activity with phosphatidic acid from egg phosphatidylcholine
-
-
?
CTP + 1-palmitoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-oleoylglycerol
-
-
-
-
?
CTP + 1-stearoyl-2-arachidonoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoylglycerol
-
-
-
-
?
CTP + 1-stearoyl-2-arachidonoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoylglycerol
-
-
-
?
CTP + 1-stearoyl-2-linoleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-linoleoylglycerol
-
-
-
?
CTP + 1-stearoyl-2-linoleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-linoleoylglycerol
20% of the activity with 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + 1-stearoyl-2-oleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-oleoylglycerol
-
-
-
?
CTP + 1-stearoyl-2-oleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-oleoylglycerol
20% of the activity with 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in phospholipid synthesis
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in phospholipid synthesis
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
isozyme CDS1 shows no particular substrate specificity, displaying similar activities for almost all substrates tested
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
isozyme CDS2 is selective for the acyl chains at the sn-1 and sn-2 positions, the most preferred species being 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in the de novo biosynthesis of cardiolipin
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
involved in the synthesis of phospholipids and of phosphatidylinositol 4,5-diphosphate, which plays an important role in phosphoinositide-mediated signallng pathways
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in the de novo biosynthesis of cardiolipin
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
NBD-phosphatidate
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
r
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
r
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
phosphatidic acid from egg lecithin and 1-stearoyl 2-arachidonoyl phosphatidic acid are preferred substrates for the microsomal enzyme
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Drosophila sp. (in: flies)
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Drosophila sp. (in: flies)
-
the enzyme is required for the regeneration of the signalling molecule phosphatidylinositol-4,5-diphosphate from phosphatidic acid. A photoreceptor cell-specific isoform is a key regulator of phototransduction, a G-protein-coupled signalling cascade mediated by phospholipase C
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Drosophila sp. (in: flies)
-
the enzyme plays a regulatory role in phototransduction by ensuring an adequate supply of phosphatidylinositol-4,5-diphosphate
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
r
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme is specific for long-chain phosphatidic acid. 1-Acyl-sn-glycero-3-phosphate is not a substrate and phosphatidic acids with acyl chains shorter than 16 carbons are poor substrates
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
high activity with phosphatidic acid from egg phosphatidylcholine
-
-
r
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
strong preference for phosphatidic acid with 16-carbon and 18-carbon length fatty acids and at least one unsaturated fatty acid
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
equilibrium constant is 0.22
-
-
r
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme is involved in the regulation of phospholipid metabolism
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the activity is essential for all phospholipid biosynthesis in Escherichia coli
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme produces key intermediates in phospholipid biosynthesis
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
didecanoyl phosphatidic acid is the most active of the synthetic phosphatidic acids tested, lysophosphatidic acid is a poor substrate
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
the level of CDP-diacylglycerol synthetase 1 is not a critical determinant of cellular phosphatidylinositol content. This argues against a determining role of the activity in the regulation of phosphatidylinositol biosynthesis
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Micrococcus cerificans
-
highly specific for CTP
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Micrococcus cerificans
-
enzyme is involved in synthesis of CDP-diglyceride, which plays a primary role in bacterial biosyntheses of essential phosphoglycerides
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
the enzyme catalyzes the synthesis of CDPdiacylglycerol, an obligatory intermediate compound in the biosynthesis of the major anionic and zwitterionic phospholipids
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
enzyme plays a central role in phospholipid biosynthesis
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
r
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
equilibrium constant is 0.001. Reverse reaction is favored in vitro
-
-
r
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme is involved in the regulation of phospholipid metabolism
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
activity with phosphatidate obtained from egg lecithin which has a variety of mixed fatty acid in ester linkage. The phosphatidate has two oleoyl fatty acids is only 20% as effective as the phospatidate prepared from egg lecithin
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
-
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
-
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
-
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
reaction at the same rate as CTP
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
-
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
Micrococcus cerificans
-
50% of the activity with CTP
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
-
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
-
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
-
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
-
-
-
r
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
-
-
-
r
additional information
?
-
decreasing activity in the order 1,2-dioleoyl phosphatidic acid, 1-palmitoyl-2-oleoyl phosphatidic acid, 1,2-dipalmitoyl phosphatidic acid
-
-
?
additional information
?
-
decreasing activity in the order 1,2-dioleoyl phosphatidic acid, 1-palmitoyl-2-oleoyl phosphatidic acid, 1,2-dipalmitoyl phosphatidic acid
-
-
?
additional information
?
-
decreasing activity in the order 1,2-dioleoyl phosphatidic acid, 1-palmitoyl-2-oleoyl phosphatidic acid, 1,2-dipalmitoyl phosphatidic acid
-
-
?
additional information
?
-
-
decreasing activity in the order 1,2-dioleoyl phosphatidic acid, 1-palmitoyl-2-oleoyl phosphatidic acid, 1,2-dipalmitoyl phosphatidic acid
-
-
?
additional information
?
-
the extraplastidial isoforms are most active with the 18:1/18:1 species of phosphatidates and their activities decreases in the order of 16:0/18:1 phosphatidate to 16:0/16:0 phosphatidate
-
-
?
additional information
?
-
the extraplastidial isoforms are most active with the 18:1/18:1 species of phosphatidates and their activities decreases in the order of 16:0/18:1 phosphatidate to 16:0/16:0 phosphatidate
-
-
?
additional information
?
-
the extraplastidial isoforms are most active with the 18:1/18:1 species of phosphatidates and their activities decreases in the order of 16:0/18:1 phosphatidate to 16:0/16:0 phosphatidate
-
-
?
additional information
?
-
-
the extraplastidial isoforms are most active with the 18:1/18:1 species of phosphatidates and their activities decreases in the order of 16:0/18:1 phosphatidate to 16:0/16:0 phosphatidate
-
-
?
additional information
?
-
CDS2 shows substrate specificity at both the sn-1 and sn-2 acyl chain positions. The most preferred substrate is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
additional information
?
-
CDS2 shows substrate specificity at both the sn-1 and sn-2 acyl chain positions. The most preferred substrate is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
additional information
?
-
-
CDS2 shows substrate specificity at both the sn-1 and sn-2 acyl chain positions. The most preferred substrate is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
additional information
?
-
isoform CDS1 appears to have no substrate preference for 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid, with variations of the sn-1 and sn-2 acyl chains resulting in no significant changes in preference
-
-
?
additional information
?
-
isoform CDS1 appears to have no substrate preference for 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid, with variations of the sn-1 and sn-2 acyl chains resulting in no significant changes in preference
-
-
?
additional information
?
-
-
isoform CDS1 appears to have no substrate preference for 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid, with variations of the sn-1 and sn-2 acyl chains resulting in no significant changes in preference
-
-
?
additional information
?
-
mixed micelle-based enzymatic activity with recombinant enzyme. Substrate specificity of CDS1, overview
-
-
?
additional information
?
-
mixed micelle-based enzymatic activity with recombinant enzyme. Substrate specificity of CDS1, overview
-
-
?
additional information
?
-
-
mixed micelle-based enzymatic activity with recombinant enzyme. Substrate specificity of CDS1, overview
-
-
?
additional information
?
-
mixed micelle-based enzymatic activity with recombinant enzyme. Substrate specificity of CDS2, overview
-
-
?
additional information
?
-
mixed micelle-based enzymatic activity with recombinant enzyme. Substrate specificity of CDS2, overview
-
-
?
additional information
?
-
-
mixed micelle-based enzymatic activity with recombinant enzyme. Substrate specificity of CDS2, overview
-
-
?
additional information
?
-
the enzyme does not bind phosphatidylserine, phosphatidylethanolamine, or phosphatidylcholine
-
-
-
additional information
?
-
-
the enzyme does not bind phosphatidylserine, phosphatidylethanolamine, or phosphatidylcholine
-
-
-
additional information
?
-
the enzyme does not bind phosphatidylserine, phosphatidylethanolamine, or phosphatidylcholine
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CTP + 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoyl-glycerol
-
-
-
?
CTP + 1-stearoyl-2-linoleoyl-sn-phosphatidic acid
diphosphate + CDP-1-stearoyl-2-linoleoyl-glycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in phospholipid synthesis
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in phospholipid synthesis
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
isozyme CDS1 shows no particular substrate specificity, displaying similar activities for almost all substrates tested
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
isozyme CDS2 is selective for the acyl chains at the sn-1 and sn-2 positions, the most preferred species being 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in the de novo biosynthesis of cardiolipin
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
involved in the synthesis of phospholipids and of phosphatidylinositol 4,5-diphosphate, which plays an important role in phosphoinositide-mediated signallng pathways
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
involved in the de novo biosynthesis of cardiolipin
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
r
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
r
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Drosophila sp. (in: flies)
-
the enzyme is required for the regeneration of the signalling molecule phosphatidylinositol-4,5-diphosphate from phosphatidic acid. A photoreceptor cell-specific isoform is a key regulator of phototransduction, a G-protein-coupled signalling cascade mediated by phospholipase C
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Drosophila sp. (in: flies)
-
the enzyme plays a regulatory role in phototransduction by ensuring an adequate supply of phosphatidylinositol-4,5-diphosphate
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme is involved in the regulation of phospholipid metabolism
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the activity is essential for all phospholipid biosynthesis in Escherichia coli
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme produces key intermediates in phospholipid biosynthesis
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
the level of CDP-diacylglycerol synthetase 1 is not a critical determinant of cellular phosphatidylinositol content. This argues against a determining role of the activity in the regulation of phosphatidylinositol biosynthesis
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
Micrococcus cerificans
-
enzyme is involved in synthesis of CDP-diglyceride, which plays a primary role in bacterial biosyntheses of essential phosphoglycerides
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
the enzyme catalyzes the synthesis of CDPdiacylglycerol, an obligatory intermediate compound in the biosynthesis of the major anionic and zwitterionic phospholipids
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
enzyme plays a central role in phospholipid biosynthesis
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme is involved in the regulation of phospholipid metabolism
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
-
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
-
-
?
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
-
-
-
r
diphosphate + CDP-diacylglycerol
CTP + phosphatidate
-
-
-
r
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evolution
both CDP-diacylglycerol synthases Tam41 and Cds1 are highly conserved proteins, yet their origins seem to be different. The N-terminal portion of Tam41 possesses the NTase (Nucleotide Transferase) fold, which is consistent with the CDP-DAG synthase function of Tam41. In contrast, Cds1 exhibits the CDP-DAG synthase i.e. NTase activity, yet it does not contain the NTase fold. Cds1 and Tam41 have developed their own commitment to lipid biosynthetic pathways operating in two evolutionary distinct organelles, the endoplasmic reticulum and mitochondria, during evolution of eukaryotic cells
evolution
Cds1 is an evolutionarily conserved protein
evolution
Cds1 is an evolutionarily conserved protein
evolution
isoforms of CDS are located in plastids, mitochondria and the endomembrane system of plants and are encoded by five genes in Arabidopsis. Two genes have previously been shown to code for the plastidial isoforms which are indispensable for the biosynthesis of plastidial phosphatidylglycerol, and thus biogenesis and function of thylakoid membranes. the extraplastidial CDS isoforms, encoded by CDS1 and CDS2 which are constitutively expressed contrary to CDS3. These closely related CDS genes code for membrane proteins located in the endoplasmic reticulum and possess very similar enzymatic properties
evolution
Trypanosoma cruzi and Leishmaniasp. have both a eukaryotic and prokaryotic version, but Trypanosoma brucei has likely lost its prokaryotic homologue in the recent past
evolution
-
Cds1 is an evolutionarily conserved protein
-
evolution
-
Cds1 is an evolutionarily conserved protein
-
evolution
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
Trypanosoma cruzi and Leishmaniasp. have both a eukaryotic and prokaryotic version, but Trypanosoma brucei has likely lost its prokaryotic homologue in the recent past
-
malfunction
biochemical phenotype of the TbCDS conditional knockout, overvie. Lipid extracts from TbCDS CKO have a similar distribution of molecular species to that of wild-type cells across the phospholipid classes to that of wild-type cells, but an increase in diacylglycerols and triacylglycerols i detected. The decrease in CDS activity causes a marked reduction in phosphatidylinositol levels, the disproportional reduction implies the C36:1 species turns over faster than the C40:4 species. Incorporation of [3H]inositol into phosphatidylinositol and phosphatidylinositol phosphate seems relatively unaffected in the TbCDS CKO, but the mutant shows a significant reduction in flux through the GPI pathway
malfunction
cycling bbl1 mutant cells deficient in the function of the endoplasmic reticlum-resident CDP-DG synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the endoplasmic reticlum membranes. These unusual structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion. Interfering with the CDP-DG route of phosphatidic acid utilization rewires cellular metabolism to adopt a triacylglycerol-rich lifestyle reliant on the Kennedy pathway. The bbl1 mutant enzyme is catalytically deficient, penotype, overview
malfunction
cycling cells deficient in the function of the endoplasmic reticlum-resident CDP-DG synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the endoplasmic reticlum membranes. These unusual structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion. Interfering with the CDP-DG route of phosphatidic acid utilization rewires cellular metabolism to adopt a triacylglycerol-rich lifestyle reliant on the Kennedy pathway
malfunction
knocking down CDS1 results in the formation of giant or supersized lipid droplets in cultured cells. Depleting CDS1 almost completely blocked the differentiation of 3T3-L1 preadipocytes. The levels of many phosphatidate species are significantly increased upon knocking down CDS1, the amount of phosphatidate in the endoplasmic reticulum is dramatically increased upon knocking down CDS1, overview. The changes in phosphatidate level and localization may underlie the formation of giant lipid droplets as well as the block in adipogenesis in CDS-deficient cells
malfunction
knocking down CDS1 results in the formation of giant or supersized lipid droplets in cultured cells. Depleting CDS2 in 3T3-L1 preadipocytes has a moderate inhibitory effect on adipocyte differentiation. Only a small number of phosphatidate species are increased upon depleting CDS2, the amount of phosphatidate in the endoplasmic reticulum is dramatically increased upon knocking down CDS2, overview. The changes in phosphatidate level and localization may underlie the formation of giant lipid droplets as well as the block in adipogenesis in CDS-deficient cells
malfunction
knocking down CDS1 results in the formation of giant or supersized lipid droplets in cultured cells. The levels of many phosphatidate species are significantly increased upon knocking down CDS1, the amount of phosphatidate in the endoplasmic reticulum is dramatically increased upon knocking down CDS1, overview. The changes in phosphatidate level and localization may underlie the formation of giant lipid droplets as well as the block in adipogenesis in CDS-deficient cells
malfunction
knocking down CDS2 results in the formation of giant or supersized lipid droplets in cultured cells. Only a small number of phosphatidate species are increased upon depleting CDS2, the amount of phosphatidate in the endoplasmic reticulum is dramatically increased upon knocking down CDS2, overview. The changes in phosphatidate level and localization may underlie the formation of giant lipid droplets as well as the block in adipogenesis in CDS-deficient cells
malfunction
knockout mutant DELTAtam41 cells show severe growth defects on fermentable or non-fermentable media at high temperature, steady-state levels of cytochrome c1 of complex III and cytochrome oxidase subunit IV (Cox4) of complex IV are decreased in the mutant cells. Overexpression of Art5 (a arrestin-related trafficking adaptor family member) restores the temperature-sensitive growth defects of DELTAtam41 cells completely on fermentable media but only partly on non-fermentable media, which renders the cell growth dependent on mitochondrial respiration. Overexpression of both Cds1 and Art5 rescues growth defects of pgs1DELTAtam41DELTA cells. The growth defects of DELTAtam41 at elevated temperature are suppressed by the simultaneous deletion of the ITR1 gene
malfunction
loss of CdsA function causes significant accumulation of neutral lipids in many tissues along with reduced cell/organ size. These phenotypes can be traced back to reduced phosphatidylinositol levels and, subsequently, low insulin pathway activity. Overexpressing CdsA rescues the fat storage and cell growth phenotypes of insulin pathway mutants. A diacylglycerol-to-phosphatidylethanolamine route mediated by the choline/ethanolamine phosphotransferase Bbc may contribute to the growth of fat cells in silenced CdsA RNAi. CdsA RNAi affects phosphatidylinositol metabolism and insulin pathway activity, strong salivary gland fat storage phenotype of CdsA RNAi. CdsA mutations affect salivary gland fat storage and cell size. But loss of function of CdsA does not affect fat cell lipid storage and growth
malfunction
the seedling lethal phenotype of the cds1cds2 double mutant shows that plant cells require at least one catalytically active microsomal CDS isoform for cell division and expansion. According to the altered glycerolipid composition of the double mutant in comparison with wild-type seedlings, it is likely that the drastic decrease in the level of phosphatidylinositol and the increase in phosphatidic acid cause defects in cell division and expansion. The cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
malfunction
enzyme knockdown results in decreased mitochondrial CDP diacylglycerol synthase activity, decreased cardiolipin levels and a decrease in oxygen consumption
malfunction
enzyme knockout causes abnormal heart development, specifically a defect in heart valve formation
malfunction
enzyme mutants show a defective growth due to impaired replication
malfunction
enzyme mutants show defects in spermatid individualization and enlargement of mitochondria and the axonemal sheath of the spermatids
malfunction
-
enzyme mutations cause resistance to daptomycin
malfunction
-
enzyme mutations cause resistance to daptomycin
malfunction
isoform CDS2 deficiency, but not isoform CDS1 deficiency, promotes the lipid droplet association of diacylglycerol-O-acyltransferase 2 and glycerol-3-phosphateacyltransferase 4 and impairs initial lipid droplet maturation
malfunction
-
cycling cells deficient in the function of the endoplasmic reticlum-resident CDP-DG synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the endoplasmic reticlum membranes. These unusual structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion. Interfering with the CDP-DG route of phosphatidic acid utilization rewires cellular metabolism to adopt a triacylglycerol-rich lifestyle reliant on the Kennedy pathway
-
malfunction
-
cycling bbl1 mutant cells deficient in the function of the endoplasmic reticlum-resident CDP-DG synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the endoplasmic reticlum membranes. These unusual structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion. Interfering with the CDP-DG route of phosphatidic acid utilization rewires cellular metabolism to adopt a triacylglycerol-rich lifestyle reliant on the Kennedy pathway. The bbl1 mutant enzyme is catalytically deficient, penotype, overview
-
malfunction
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
biochemical phenotype of the TbCDS conditional knockout, overvie. Lipid extracts from TbCDS CKO have a similar distribution of molecular species to that of wild-type cells across the phospholipid classes to that of wild-type cells, but an increase in diacylglycerols and triacylglycerols i detected. The decrease in CDS activity causes a marked reduction in phosphatidylinositol levels, the disproportional reduction implies the C36:1 species turns over faster than the C40:4 species. Incorporation of [3H]inositol into phosphatidylinositol and phosphatidylinositol phosphate seems relatively unaffected in the TbCDS CKO, but the mutant shows a significant reduction in flux through the GPI pathway
-
metabolism
CDP-diacylglycerol synthase Cds1 resides in the endoplasmic reticulum but not in mitochondria, while CDP-diacylglycerol synthase Tam41, a highly conserved mitochondrial maintenance protein, directly catalyzes the formation of CDP-DAG from phosphatidate in the mitochondrial inner membrane
metabolism
cytidine diphosphate diacylglycerol (CDP-DAG) is a central lipid intermediate for several pathways in both prokaryotes and eukaryotes, being produced by CDP-DAG synthase
metabolism
the two isoforms of human CDS, CDS1 and CDS2, show different acyl chain specificities for its lipid substrate. CDS1 and CDS2 can create different CDP-DAG pools that may serve to enrich different phospholipid species with specific acyl chains
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
metabolism
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
cytidine diphosphate diacylglycerol (CDP-DAG) is a central lipid intermediate for several pathways in both prokaryotes and eukaryotes, being produced by CDP-DAG synthase
-
physiological function
enzyme can substitute for the corresponding enzyme in Plasmodium knowlesi. Both the C-terminal cytidylyltransferase domain and the N-terminal extension are essential to Plasmodium spp.
physiological function
Arabidopsis mutants lacking either one or both CDS1 and CDS2 genes clearly show that these two genes have redundant functions. As reflected in the seedling lethal phenotype of the cds1cds2 double mutant, plant cells require at least one catalytically active microsomal CDS isoform for cell division and expansion
physiological function
CDS gene expression is essential in the bloodstream form of the parasite. A CDS conditional knockout shows morphological changes including a cell-cycle arrest due in part to kinetoplast segregation defects. The conditional knockout shows drastically altered lipid metabolism where reducing levels of phosphatidylinositol detrimentally impact on glycoylphosphatidylinositol biosynthesis. Expression of Trypanosoma brucei CDS gene complements a non-viable yeast CDS null strain
physiological function
cycling cells deficient in the function of the ER-resident CDP-diacylglycerol synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the ER membranes. These structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion
physiological function
inositol depletion by overexpressing an arrestin-related protein Art5 partially restores the defects of cell growth and cardiolipin synthesis in the absence of Tam41
physiological function
isoforms CDS1 and CDS2 could create different CDP-diacylglycerol pools that may serve to enrich different phospholipid species with specific acyl chains. CDS1 shows no particular substrate specificity, displaying similar activities for almost all substrates tested, and shows no acyl chain-dependent inhibition. Both isoforms CDS1 and CDS2 are inhibited by their anionic phospholipid end products
physiological function
isoforms CDS1 and CDS2 could create different CDP-diacylglycerol pools that may serve to enrich different phospholipid species with specific acyl chains. CDS2 is selective for the acyl chains at the sn-1 and sn-2 positions, the most preferred species being 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid. Inhibition of CDS2 by phosphatidylinositol is also acyl chain-dependent, with the strongest inhibition seen with the 1-stearoyl-2-arachidonoyl species. Both isoforms CDS1 and CDS2 are inhibited by their anionic phospholipid end products
physiological function
knocking down either isoform CDS1 or isoform CDS2 results in the formation of giant or supersized lipid droplets in cultured cells. Depleting CDS1 almost completely blocks the differentiation of 3T3-L1 preadipocytes. The levels of many phosphatidic acid species are significantly increased upon knocking down CDS1. The amount of phosphatidic acid in the endoplasmic reticulum is dramatically increased upon knocking down CDS1 or CDS2
physiological function
knocking down either isoform CDS1 or isoform CDS2 results in the formation of giant or supersized lipid droplets in cultured cells. Depleting CDS2 has a moderate inhibitory effect on adipocyte differentiation. Only a small number of phosphatidic acid species are increased upon depleting CDS2. The amount of phosphatidic acid in the endoplasmic reticulum is dramatically increased upon knocking down CDS1 or CDS2
physiological function
loss of CdsA function causes significant accumulation of neutral lipids in many tissues along with reduced cell/organ size. These phenotypes can be traced back to reduced phosphatidylinositol levels and, subsequently, low insulin pathway activity. Overexpressing CdsA rescues the fat storage and cell growth phenotypes of insulin pathway mutants. CdsA regulates salivary gland fat storage and cell size
physiological function
CDP-DG synthase is responsible for a rate-limiting step in the production of phospholipids. It catalyzes condensation of phosphatidate and cytidine triphosphate, releasing the CDP-diacylglycerol and diphosphate products
physiological function
CDP-DG synthase is responsible for a rate-limiting step in the production of phospholipids. It catalyzes condensation of phosphatidate and cytidine triphosphate, releasing the CDP-diacylglycerol and diphosphate products
physiological function
CDP-diacylglycerol synthases (CDS) are critical enzymes that catalyze the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid
physiological function
CDP-diacylglycerol synthases regulate the growth of lipid droplets and adipocyte development, role of CDP-diacylglycerol in lipid storage in mammals. The expansion of lipid droplets and the differentiation of preadipocytes are two important aspects of mammalian lipid storage, CDS1 and CDS2 are important regulators of lipid storage
physiological function
CDP-diacylglycerol synthases regulate the growth of lipid droplets and adipocyte development, role of CDP-diacylglycerol in lipid storage in mammals. The expansion of lipid droplets and the differentiation of preadipocytes are two important aspects of mammalian lipid storage, CDS1 and CDS2 are important regulators of lipid storage
physiological function
cytidine diphosphate diacylglycerol synthase (CDS) catalyzes the activation of phosphatidic acid to CDP-diacylglycerol, a central intermediate in glycerolipid biosynthesis in prokaryotic and eukaryotic organisms. CDP-diacylglycerol is the precursor to phosphatidylinositol, phosphatidylglycerol, and cardiolipin of eukaryotic phospholipids that are essential for various cellular functions
physiological function
TbCDS is essential for formation of glycosylphosphatidylinositol intermediates. The enzyme is required for synthesis of CDP-DAG for the synthesis of the bulk of phosphatidylinositol in the cell, it produces CDP-DAG required for the endoplasmic reticulum localized phosphatidylinositol synthase to make phosphatidylinositol for GPI anchors
physiological function
the CDP-diacylglycerol synthase Tam41 is required for cardiolipin biosynthesis in mitochondria
physiological function
the enzyme diverts phosphatidic acid from triacylglycerol synthesis to phosphatidylinositol synthesis and coordinates cell growth and fat storage. Enzyme CdsA coordinates cell/tissue growth and lipid storage through the insulin pathway. The enzyme is important for the phototransduction pathway. CdsA regulates salivary gland fat storage and cell size
physiological function
-
the enzyme is essential for embryogenesis, phototransduction, metamorphosis, and spermatogenesis
physiological function
the enzyme participates in regulating heart valve formation through mediating PINK1-dependent mitophagy
physiological function
-
CDP-DG synthase is responsible for a rate-limiting step in the production of phospholipids. It catalyzes condensation of phosphatidate and cytidine triphosphate, releasing the CDP-diacylglycerol and diphosphate products
-
physiological function
-
CDP-DG synthase is responsible for a rate-limiting step in the production of phospholipids. It catalyzes condensation of phosphatidate and cytidine triphosphate, releasing the CDP-diacylglycerol and diphosphate products
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
CDS gene expression is essential in the bloodstream form of the parasite. A CDS conditional knockout shows morphological changes including a cell-cycle arrest due in part to kinetoplast segregation defects. The conditional knockout shows drastically altered lipid metabolism where reducing levels of phosphatidylinositol detrimentally impact on glycoylphosphatidylinositol biosynthesis. Expression of Trypanosoma brucei CDS gene complements a non-viable yeast CDS null strain
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
TbCDS is essential for formation of glycosylphosphatidylinositol intermediates. The enzyme is required for synthesis of CDP-DAG for the synthesis of the bulk of phosphatidylinositol in the cell, it produces CDP-DAG required for the endoplasmic reticulum localized phosphatidylinositol synthase to make phosphatidylinositol for GPI anchors
-
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C102Y
mutation is the molecular basis for the inositol excretion phenotype
D220A
site-directed mutagenesis of TAM41, catalytically inactive mutant
Y130A
site-directed mutagenesis of TAM41, catalytically inactive mutant
F240A
the mutant retains about 47% of wild type activity
K156A
the mutant retains 6.81% of wild type activity
K183A
the mutant enzyme is almost inactive
Q254A
the mutant enzyme is almost inactive
R180A
the mutant enzyme is almost inactive
R245A
the mutant retains 29.89% of wild type activity
Y144A
the mutant enzyme is almost inactive
F240A
-
the mutant retains about 47% of wild type activity
-
K156A
-
the mutant retains 6.81% of wild type activity
-
K183A
-
the mutant enzyme is almost inactive
-
R245A
-
the mutant retains 29.89% of wild type activity
-
Y144A
-
the mutant enzyme is almost inactive
-
C1226T/C1227T/P363S
construction of loss-of-function mutation in CDP-DG synthase in Schizosaccharomyces japonicus bbl1 mutant cells, the mutation triggers abnormal lipid droplet biogenesis and triacylglycerol accumulation. The P363S mutation in the Cds1 enzyme leads to a reduction in its CDP-DG synthase activity and potential shunting of a bulk of cellular phosphatidate into triacylglycerol biosynthesis through the DG pathway. The cds1bbl1 mutation is recessive, since introduction of the wild-type gene as an extra copy fully rescues the phenotype of bbl1 cells. Mutant bbl1 phenotype, overview
C1226T/C1227T/P363S
-
construction of loss-of-function mutation in CDP-DG synthase in Schizosaccharomyces japonicus bbl1 mutant cells, the mutation triggers abnormal lipid droplet biogenesis and triacylglycerol accumulation. The P363S mutation in the Cds1 enzyme leads to a reduction in its CDP-DG synthase activity and potential shunting of a bulk of cellular phosphatidate into triacylglycerol biosynthesis through the DG pathway. The cds1bbl1 mutation is recessive, since introduction of the wild-type gene as an extra copy fully rescues the phenotype of bbl1 cells. Mutant bbl1 phenotype, overview
-
additional information
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS1, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS1, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS1, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
-
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS1, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS2, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS2, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS2, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
-
generation of a T-DNA insertion (in the 5' untranslated region) mutant of CDS2, the cds1cds2 double mutant is seedling lethal, phenotypes, overview. The seedling-lethal phenotype of cds1cds2 double mutants can be rescued by inducing the expression of a functional CDS1 or CDS2 gene
additional information
transient siRNA knockdown of CDS1 in HeLa cells downregulates CDS1 by 81%. In siCDS2 HeLa cells, the mRNA expression of CDS1 is increased by 2.6fold, but in siCDS1 cells, the CDS2 level is unchanged. Knocking down CDS1 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
transient siRNA knockdown of CDS1 in HeLa cells downregulates CDS1 by 81%. In siCDS2 HeLa cells, the mRNA expression of CDS1 is increased by 2.6fold, but in siCDS1 cells, the CDS2 level is unchanged. Knocking down CDS1 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
transient siRNA knockdown of CDS1 in HeLa cells downregulates CDS2 by 90%. In siCDS2 HeLa cells, the mRNA expression of CDS1 is increased by 2.6fold, but in siCDS1 cells, the CDS2 level is unchanged. Knocking down CDS2 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
transient siRNA knockdown of CDS1 in HeLa cells downregulates CDS2 by 90%. In siCDS2 HeLa cells, the mRNA expression of CDS1 is increased by 2.6fold, but in siCDS1 cells, the CDS2 level is unchanged. Knocking down CDS2 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
transient siRNA knockdown of CDS1 in 3T3-L1 cells downregulates CDS1 by 48%. Knocking down CDS1 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
transient siRNA knockdown of CDS1 in 3T3-L1 cells downregulates CDS1 by 48%. Knocking down CDS1 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
transient siRNA knockdown of CDS1 in 3T3-L1 cells downregulates CDS2 by 90%. Knocking down CDS2 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
transient siRNA knockdown of CDS1 in 3T3-L1 cells downregulates CDS2 by 90%. Knocking down CDS2 results in the formation of giant or supersized lipid droplets in cultured cells
additional information
-
the cdsA-inactivated PAL mutant strain lacks phycobilisomes
additional information
generation of a conditional CDS knockout in the bloodstream form parasite, phenotype, overview
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
generation of a conditional CDS knockout in the bloodstream form parasite, phenotype, overview
-
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Inglis-Broadgate, S.L.; Ocaka, L.; Banerjee, R.; Gaasenbeek, M.; Chapple, J.P.; Cheetham, M.E.; Clark, B.J.; Hunt, D.M.; Halford, S.
Isolation and characterization of murine Cds (CDP-diacylglycerol synthase) 1 and 2
Gene
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2005
Mus musculus (P98191), Mus musculus (Q99L43), Mus musculus
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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
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Mus musculus, Rattus norvegicus
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Mercade, A.; Sanchez, A.; Folch, J.M.
Characterization and physical mapping of the porcine CDS1 and CDS2 genes
Anim. Biotechnol.
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Sus scrofa
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Laczko-Dobos, H.; Ughy, B.; Toth, S.Z.; Komenda, J.; Zsiros, O.; Domonkos, I.; Parducz, A.; Bogos, B.; Komura, M.; Itoh, S.; Gombos, Z.
Role of phosphatidylglycerol in the function and assembly of Photosystem II reaction center, studied in a cdsA-inactivated PAL mutant strain of Synechocystis sp. PCC6803 that lacks phycobilisomes
Biochim. Biophys. Acta
1777
1184-1194
2008
Synechocystis sp.
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Shastri, S.; Zeeman, A.M.; Berry, L.; Verburgh, R.J.; Braun-Breton, C.; Thomas, A.W.; Gannoun-Zaki, L.; Kocken, C.H.; Vial, H.J.
Plasmodium CDP-DAG synthase: an atypical gene with an essential N-terminal extension
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40
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Plasmodium falciparum (Q8ILZ6), Plasmodium falciparum
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Waugh, M.G.; Minogue, S.; Clayton, E.L.; Hsuan, J.J.
CDP-diacylglycerol phospholipid synthesis in detergent-soluble, non-raft, membrane microdomains of the endoplasmic reticulum
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52
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2011
Homo sapiens
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Serricchio, M.; Buetikofer, P.
Phosphatidylglycerophosphate synthase associates with a mitochondrial inner membrane complex and is essential for growth of Trypanosoma brucei
Mol. Microbiol.
87
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Trypanosoma brucei brucei (Q57U32), Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927 (Q57U32)
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DSouza, K.; Kim, Y.J.; Balla, T.; Epand, R.M.
Distinct properties of the two isoforms of CDP-diacylglycerol synthase
Biochemistry
53
7358-7367
2014
Homo sapiens (O95674), Homo sapiens (Q92903), Homo sapiens
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Tamura, Y.; Harada, Y.; Nishikawa, S.; Yamano, K.; Kamiya, M.; Shiota, T.; Kuroda, T.; Kuge, O.; Sesaki, H.; Imai, K.; Tomii, K.; Endo, T.
Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria
Cell Metab.
17
709-718
2013
Saccharomyces cerevisiae (P38221), Saccharomyces cerevisiae (P53230), Saccharomyces cerevisiae
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Qi, Y.; Kapterian, T.S.; Du, X.; Ma, Q.; Fei, W.; Zhang, Y.; Huang, X.; Dawes, I.W.; Yang, H.
CDP-diacylglycerol synthases regulate the growth of lipid droplets and adipocyte development
J. Lipid Res.
57
767-780
2016
Homo sapiens (O95674), Homo sapiens (Q92903), Mus musculus (P98191), Mus musculus (Q99L43)
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He, Y.; Yam, C.; Pomraning, K.; Chin, J.S.; Yew, J.Y.; Freitag, M.; Oliferenko, S.
Increase in cellular triacylglycerol content and emergence of large ER-associated lipid droplets in the absence of CDP-DG synthase function
Mol. Biol. Cell
25
4083-4095
2014
Schizosaccharomyces japonicus, Schizosaccharomyces japonicus (B6JVL2), Schizosaccharomyces pombe (Q9P381), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972 (Q9P381), Schizosaccharomyces japonicus yFS275 (B6JVL2)
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Zhou, Y.; Peisker, H.; Weth, A.; Baumgartner, W.; Doermann, P.; Frentzen, M.
Extraplastidial cytidinediphosphate diacylglycerol synthase activity is required for vegetative development in Arabidopsis thaliana
Plant J.
75
867-879
2013
Arabidopsis thaliana (O04928), Arabidopsis thaliana (O49639), Arabidopsis thaliana (Q1PE48), Arabidopsis thaliana
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Liu, Y.; Wang, W.; Shui, G.; Huang, X.
CDP-diacylglycerol synthetase coordinates cell growth and fat storage through phosphatidylinositol metabolism and the insulin pathway
PLoS Genet.
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Drosophila melanogaster, Drosophila melanogaster (P56079)
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Lilley, A.C.; Major, L.; Young, S.; Stark, M.J.; Smith, T.K.
The essential roles of cytidine diphosphate-diacylglycerol synthase in bloodstream form Trypanosoma brucei
Mol. Microbiol.
92
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Trypanosoma brucei brucei (Q57U32), Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927 (Q57U32)
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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
Blunsom, N.J.; Cockcroft, S.
CDP-diacylglycerol synthases (CDS) gateway to phosphatidylinositol and cardiolipin synthesis
Front. Cell Dev. Biol.
8
63
2020
Aeropyrum pernix, Saccharomyces cerevisiae, Drosophila melanogaster, Schizosaccharomyces pombe, Streptococcus mitis, Streptococcus oralis, Thermotoga maritima, Toxoplasma gondii, Trypanosoma brucei brucei, Eimeria falciformis, Arabidopsis thaliana (O04928), Arabidopsis thaliana (O49639), Arabidopsis thaliana (Q1PE48), Arabidopsis thaliana (Q94A03), Arabidopsis thaliana (Q9M001), Escherichia coli (P0ABG1), Danio rerio (Q3B7H2), Homo sapiens (Q92903), Homo sapiens (Q95674)
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Kong, P.; Ufermann, C.M.; Zimmermann, D.L.M.; Yin, Q.; Suo, X.; Helms, J.B.; Brouwers, J.F.; Gupta, N.
Two phylogenetically and compartmentally distinct CDP-diacylglycerol synthases cooperate for lipid biogenesis in Toxoplasma gondii
J. Biol. Chem.
292
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2017
Toxoplasma gondii (A0A191SG65), Toxoplasma gondii (A0A192XRE2), Toxoplasma gondii
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Xu, Y.; Mak, H.Y.; Lukmantara, I.; Li, Y.E.; Hoehn, K.L.; Huang, X.; Du, X.; Yang, H.
CDP-DAG synthase 1 and 2 regulate lipid droplet growth through distinct mechanisms
J. Biol. Chem.
294
16740-16755
2019
Homo sapiens (O95674), Homo sapiens (Q92903)
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Laurinyecz, B.; Peter, M.; Vedelek, V.; Kovacs, A.L.; Juhasz, G.; Maroy, P.; Vigh, L.; Balogh, G.; Sinka, R.
Reduced expression of CDP-DAG synthase changes lipid composition and leads to male sterility in Drosophila
Open Biology
6
50169
2016
Drosophila melanogaster (P56079)
brenda
Jiao, H.; Yin, Y.; Liu, Z.
Structures of the mitochondrial CDP-DAG synthase Tam41 suggest a potential lipid substrate pathway from membrane to the active site
Structure
27
1258-1269
2019
Schizosaccharomyces pombe (O74339), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972 (O74339)
brenda