BRENDA - Enzyme Database

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)
EC Number
Commentary
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
Commentary
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
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.8.1
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
-
738578
Drosophila melanogaster
CMP + a phosphatidylethanolamine
-
-
-
r
2.7.8.2
CDP-choline + 1,2-diacyl-sn-glycerol
-
738578
Drosophila melanogaster
CMP + a phosphatidylcholine
-
-
-
r
2.7.8.2
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
-
738578
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
738578
Drosophila melanogaster
?
-
-
-
-
2.7.8.B14
a ceramide + a phosphatidylethanolamine
-
738578
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
738578
Drosophila melanogaster
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.7.8.B14
27
-
assay at
Drosophila melanogaster
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.7.8.B14
7
-
assay at
Drosophila melanogaster
Cloned(Commentary) (protein specific)
EC Number
Commentary
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 (protein specific)
EC Number
Localization
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.8.1
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
-
738578
Drosophila melanogaster
CMP + a phosphatidylethanolamine
-
-
-
r
2.7.8.2
CDP-choline + 1,2-diacyl-sn-glycerol
-
738578
Drosophila melanogaster
CMP + a phosphatidylcholine
-
-
-
r
2.7.8.2
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
-
738578
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
738578
Drosophila melanogaster
?
-
-
-
-
2.7.8.B14
a ceramide + a phosphatidylethanolamine
-
738578
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
738578
Drosophila melanogaster
a ceramide phosphoethanolamine + a 1,2-diacyl-sn-glycerol
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.7.8.B14
27
-
assay at
Drosophila melanogaster
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.7.8.B14
7
-
assay at
Drosophila melanogaster
General Information
EC Number
General Information
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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