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Literature summary for 2.7.8.B14 extracted from

  • Vacaru, A.M.; van den Dikkenberg, J.; Ternes, P.; Holthuis, J.C.
    Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen (2013), J. Biol. Chem., 288, 11520-11530.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.8.B14

Cloned(Commentary)

Cloned (Comment) Organism
gene CG4585, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression from vector mammalian expression vector pcDNA3.1/V5-His-TOPO in HeLa cells and in Drosophila S2 cells Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi membrane the enzyme resides in the Golgi complex with its active site facing the lumen Drosophila melanogaster 139
-
plasma membrane at high expression level Drosophila melanogaster 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the enzyme activity is strictly dependent on the presence of Mn2+ ions Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a ceramide + a phosphatidylethanolamine Drosophila melanogaster
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 a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
 ?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster O77475
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a ceramide + a phosphatidylethanolamine
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 Drosophila melanogaster a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
 ?
a ceramide + a phosphatidylethanolamine assay substrate is C6-NBD-ceramide Drosophila melanogaster a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
 ?

Synonyms

Synonyms Comment Organism
CCS
-
 Drosophila melanogaster
CDP-Eth:ceramide ethanolamine phosphotransferase
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 Drosophila melanogaster
CDP-ethanolamine:ceramide ethanolamine phosphotransferase
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 Drosophila melanogaster
ceramide ethanolamine phosphotransferase
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 Drosophila melanogaster
CG4585
-
 Drosophila melanogaster
CPE synthase
-
 Drosophila melanogaster
cpeS
-
 Drosophila melanogaster
dCCS4
-
 Drosophila melanogaster
monofunctional CPE synthase
-
 Drosophila melanogaster
PE:ceramide ethanolamine phosphotransferase
-
 Drosophila melanogaster

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
27
-
 assay at Drosophila melanogaster

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Drosophila melanogaster

General Information

General Information Comment Organism
evolution insect-specific CPE synthase belongs to a novel branch of CDP-alcohol phosphotransferases with unique membrane topology. CPE synthase constitutes a new branch within the CDP-alcohol phosphotransferase superfamily with homologues in Arthropoda (insects, spiders, mites, scorpions), Cnidaria (Hydra, sea anemones), and Mollusca (oysters) but not in most other animal phyla. The enzyme resides in the Golgi complex with its active site facing the lumen, contrary to the membrane topology of other CDPalcohol phosphotransferases Drosophila melanogaster
malfunction depletion of dCCS4 caused a major (about 60%) reduction in CPES activity. When incubated with CDP-[14C]Eth in the presence of Mn2+ ions, lysates of dCCS4-depleted cells synthesize only a minor (about 25%) fraction of the radiolabeled CPE formed in lysates of control (dsGFP-treated) cells. In addition, loss of dCCS4 causes a substantial drop in de novo synthesis of CPE, accompanied by a defect in cell growth Drosophila melanogaster
metabolism ceramide phosphoethanolamine (CPE) is the principal membrane sphingolipid. The corresponding CPE synthase shares mechanistic features with enzymes mediating phospholipid biosynthesis via the Kennedy pathway, e.g. EC 2.7.8.2. Drosophila lacks the phosphocholine-containing sphingomyelin (SM) found in mammalian membranes and instead synthesizes ceramide phosphoethanolamine (CPE). SMS2, EC 2.7.8.27, is a bifunctional enzyme that produces both SM and CPE, SMS2 likely accounts for the plasma membrane-resident CPE synthase activity Drosophila melanogaster
physiological function CDP-ethanolamine:ceramide ethanolamine phosphotransferase is the enzyme responsible for bulk production of ceramide phosphoethanolamine (CPE) in Drosophila. The smaller crosssectional area of the phosphoethanolamine headgroup in CPE allows a closer contact between these molecules in comparison with SM, promoting membrane viscosity. Contrary to sphingomyelin, CPE does not interact favorably with cholesterol and fails to form sterol-rich domains in model bilayers. The addition of CDP-Eth to lysates of HeLa cells expressing dCCS4 caused a dramatic increase in NBD-CPE formation. Drosophila S2 cells require dCCS4 for CDP-Eth-dependent CPE production and growth Drosophila melanogaster