BRENDA - Enzyme Database
show all sequences of 2.7.8.B14

Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen

Vacaru, A.M.; van den Dikkenberg, J.; Ternes, P.; Holthuis, J.C.; J. Biol. Chem. 288, 11520-11530 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
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
Commentary
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
Commentary
Organism
Structure
Mn2+
the enzyme activity is strictly dependent on the presence of Mn2+ ions
Drosophila melanogaster
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a ceramide + a phosphatidylethanolamine
Drosophila melanogaster
-
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Drosophila melanogaster
O77475
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a ceramide + a phosphatidylethanolamine
-
738578
Drosophila melanogaster
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
-
?
a ceramide + a phosphatidylethanolamine
assay substrate is C6-NBD-ceramide
738578
Drosophila melanogaster
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
27
-
assay at
Drosophila melanogaster
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Drosophila melanogaster
Cloned(Commentary) (protein specific)
Commentary
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 (protein specific)
Localization
Commentary
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 (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
the enzyme activity is strictly dependent on the presence of Mn2+ ions
Drosophila melanogaster
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a ceramide + a phosphatidylethanolamine
Drosophila melanogaster
-
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a ceramide + a phosphatidylethanolamine
-
738578
Drosophila melanogaster
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
-
?
a ceramide + a phosphatidylethanolamine
assay substrate is C6-NBD-ceramide
738578
Drosophila melanogaster
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
27
-
assay at
Drosophila melanogaster
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Drosophila melanogaster
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 2.7.8.B14
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738578
Vacaru
Ceramide phosphoethanolamine b ...
Drosophila melanogaster
J. Biol. Chem.
288
11520-11530
2013
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