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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.1 gene bbc, 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
2.7.8.2 gene CG7149, 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
2.7.8.B14 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

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.8.1 endoplasmic reticulum exclusive Drosophila melanogaster 5783
-
2.7.8.2 Golgi apparatus
-
 Drosophila melanogaster 5794
-
2.7.8.B14 Golgi membrane the enzyme resides in the Golgi complex with its active site facing the lumen Drosophila melanogaster 139
-
2.7.8.B14 plasma membrane at high expression level Drosophila melanogaster 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.B14 Mn2+ the enzyme activity is strictly dependent on the presence of Mn2+ ions Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.1 CDP-ethanolamine + 1,2-diacyl-sn-glycerol Drosophila melanogaster
-
 CMP + a phosphatidylethanolamine
-
 r
2.7.8.2 CDP-choline + 1,2-diacyl-sn-glycerol Drosophila melanogaster
-
 CMP + a phosphatidylcholine
-
 r
2.7.8.2 CDP-ethanolamine + 1,2-diacyl-sn-glycerol Drosophila melanogaster
-
 CMP + a phosphatidylethanolamine
-
 r
2.7.8.2 additional information Drosophila melanogaster the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1 ?
-
 ?
2.7.8.B14 a ceramide + a phosphatidylethanolamine Drosophila melanogaster
-
 a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.1 Drosophila melanogaster A1Z9E0
-
-
2.7.8.2 Drosophila melanogaster Q8T0S3
-
-
2.7.8.B14 Drosophila melanogaster O77475
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.1 CDP-ethanolamine + 1,2-diacyl-sn-glycerol
-
 Drosophila melanogaster CMP + a phosphatidylethanolamine
-
 r
2.7.8.2 CDP-choline + 1,2-diacyl-sn-glycerol
-
 Drosophila melanogaster CMP + a phosphatidylcholine
-
 r
2.7.8.2 CDP-ethanolamine + 1,2-diacyl-sn-glycerol
-
 Drosophila melanogaster CMP + a phosphatidylethanolamine
-
 r
2.7.8.2 additional information the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1 Drosophila melanogaster ?
-
 ?
2.7.8.B14 a ceramide + a phosphatidylethanolamine
-
 Drosophila melanogaster a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
 ?
2.7.8.B14 a ceramide + a phosphatidylethanolamine assay substrate is C6-NBD-ceramide Drosophila melanogaster a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.8.1 Bb in a boxcar, isoform B UniProt Drosophila melanogaster
2.7.8.1 bbc
-
 Drosophila melanogaster
2.7.8.1 CEPT
-
 Drosophila melanogaster
2.7.8.1 CG6016 locus name Drosophila melanogaster
2.7.8.1 dCCS2
-
 Drosophila melanogaster
2.7.8.1 ethanolamine phosphotransferase
-
 Drosophila melanogaster
2.7.8.2 CEPT
-
 Drosophila melanogaster
2.7.8.2 CG7149
-
 Drosophila melanogaster
2.7.8.2 CG7149, isoform A UniProt Drosophila melanogaster
2.7.8.2 dCCS3
-
 Drosophila melanogaster
2.7.8.2 diacylglycerol cholinephosphotransferase
-
 Drosophila melanogaster
2.7.8.B14 CCS
-
 Drosophila melanogaster
2.7.8.B14 CDP-Eth:ceramide ethanolamine phosphotransferase
-
 Drosophila melanogaster
2.7.8.B14 CDP-ethanolamine:ceramide ethanolamine phosphotransferase
-
 Drosophila melanogaster
2.7.8.B14 ceramide ethanolamine phosphotransferase
-
 Drosophila melanogaster
2.7.8.B14 CG4585
-
 Drosophila melanogaster
2.7.8.B14 CPE synthase
-
 Drosophila melanogaster
2.7.8.B14 cpeS
-
 Drosophila melanogaster
2.7.8.B14 dCCS4
-
 Drosophila melanogaster
2.7.8.B14 monofunctional CPE synthase
-
 Drosophila melanogaster
2.7.8.B14 PE:ceramide ethanolamine phosphotransferase
-
 Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.8.B14 27
-
 assay at Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.8.B14 7
-
 assay at Drosophila melanogaster

General Information

EC Number General Information Comment Organism
2.7.8.1 evolution the enzyme belongs to the CEPT subfamily Drosophila melanogaster
2.7.8.2 evolution the enzyme belongs to the CEPT subfamily Drosophila melanogaster
2.7.8.B14 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
2.7.8.B14 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
2.7.8.B14 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
2.7.8.B14 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