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CTP + 2-aminoethylarsonic acid
diphosphate + cytidine-O-PO2-O-AsO2-CH2-CH2-NH3+
-
-
spontaneous hydrolysis to CMP and-O-AsO2--CH2-CH2-NH3+
?
CTP + 2-aminoethylphosphonate
?
-
-
-
-
?
CTP + ethanolamine phosphate
CDP-ethanolamine + diphosphate
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
CTP + phosphocholine
diphosphate + CDP-choline
-
-
-
-
?
CTP + phosphodimethylethanolamine
diphosphate + CDP-dimethylethanolamine
-
-
-
-
?
CTP + phosphomonomethylethanolamine
diphosphate + CDP-methylethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
additional information
?
-
CTP + ethanolamine phosphate
CDP-ethanolamine + diphosphate
-
-
-
-
?
CTP + ethanolamine phosphate
CDP-ethanolamine + diphosphate
-
-
-
?
CTP + ethanolamine phosphate
CDP-ethanolamine + diphosphate
-
-
-
-
?
CTP + ethanolamine phosphate
CDP-ethanolamine + diphosphate
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
rate limiting enzyme in phosphatidylethanolamine biosynthesis. Defects in CTP:phosphorylethanolamine cytidylyltransferase affect embryonic and postembryonic development
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
enzyme activity increases during the dark and then decreases during the light period, while the mRNA level does not alter, providing evidence for posttranslational regulation
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
Pcyt2is necessary for murine development. A single Pcyt2 allele in heterozygotes can maintain phospholipid homeostasis
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
r
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
r
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
rate-regulatory enzyme of phosphatidylethanolamine synthesis via the CDP-ethanolamine pathway
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
catalyzes a central step in phosphatidylethanolamine synthesis
-
r
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
catalyzes a central step in phosphatidylethanolamine synthesis
-
r
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
at physiological ethanolamine concentrations, the supply of CDPethanolamine, via the expression level of CTP:phosphoethanolamine cytidylyltransferase, together with the amount of cellular diacylglycerol available to CTP:phosphoethanolamine cytidylyltransferase are major factors regulating the flux through the CDPethanolamine pathway
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
dCTP + ethanolamine phosphate
diphosphate + dCDP-ethanolamine
-
-
-
-
?
additional information
?
-
-
uses N-methylated derivatives of ethanolamine phosphate less efficiently and does not react with phosphocholine
-
-
?
additional information
?
-
catalytic reaction of ECT obeys Michaelis-Menten kinetics with respect to both CTP and phosphoethanolamine
-
-
?
additional information
?
-
-
catalytic reaction of ECT obeys Michaelis-Menten kinetics with respect to both CTP and phosphoethanolamine
-
-
?
additional information
?
-
-
Pcyt2 is the main regulatory enzyme in the CDP-ethanolamine pathwa
-
-
?
additional information
?
-
uses N-methylated derivatives of ethanolamine phosphate less efficiently and does not react with phosphocholine
-
-
?
additional information
?
-
-
uses N-methylated derivatives of ethanolamine phosphate less efficiently and does not react with phosphocholine
-
-
?
additional information
?
-
-
the enzyme shows high substrate specificity for ethanolamine phosphate
-
-
?
additional information
?
-
-
uses N-methylated derivatives of ethanolamine phosphate less efficiently and does not react with phosphocholine
-
-
?
additional information
?
-
-
the enzyme shows high substrate specificity for ethanolamine phosphate
-
-
?
additional information
?
-
-
the enzyme shows high substrate specificity for ethanolamine phosphate
-
-
?
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CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
additional information
?
-
-
Pcyt2 is the main regulatory enzyme in the CDP-ethanolamine pathwa
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
rate limiting enzyme in phosphatidylethanolamine biosynthesis. Defects in CTP:phosphorylethanolamine cytidylyltransferase affect embryonic and postembryonic development
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
enzyme activity increases during the dark and then decreases during the light period, while the mRNA level does not alter, providing evidence for posttranslational regulation
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
Pcyt2is necessary for murine development. A single Pcyt2 allele in heterozygotes can maintain phospholipid homeostasis
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
rate-regulatory enzyme of phosphatidylethanolamine synthesis via the CDP-ethanolamine pathway
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
catalyzes a central step in phosphatidylethanolamine synthesis
-
r
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
catalyzes a central step in phosphatidylethanolamine synthesis
-
r
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
at physiological ethanolamine concentrations, the supply of CDPethanolamine, via the expression level of CTP:phosphoethanolamine cytidylyltransferase, together with the amount of cellular diacylglycerol available to CTP:phosphoethanolamine cytidylyltransferase are major factors regulating the flux through the CDPethanolamine pathway
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDP-ethanolamine
-
-
-
-
?
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1-Aminoethylphosphonate
-
inhibitory power stimulated by Mg2+; noncompetitive to phosphorylethanolamine
2-aminoethylphosphonate
-
competitive to phosphorylethanolamine; inhibitory power stimulated by Mg2+
3-Aminopropylphosphonate
-
competitive to phosphorylethanolamine; inhibitory power stimulated by Mg2+
aminoimidazole-4-carboxamide
CTP
-
at concentrations exceeding that of Mg2+
phosphodimethylethanolamine
-
weak, competitive to phosphoethanolamine
phosphoethanolamine methyl-analogues
-
phosphomonomethylethanolamine
-
weak, competitive to phosphoethanolamine
Sphingosine/phosphatidylcholine vesicles
-
inhibit cytosolic and purified enzyme
-
additional information
-
overactivation of the NMDA receptor in neurons inhibits the enzyme, membrane damage by NMDA receptor is preceeded by inhibition of phospholipid synthesis
-
aminoimidazole-4-carboxamide
-
downregulates Pcyt2 activity
aminoimidazole-4-carboxamide
downregulates Pcyt2 activity
aminoimidazole-4-carboxamide
-
downregulates Pcyt2 activity
phosphocholine
-
a weak competitive inhibitor of Pcyt2
phosphocholine
-
a weak competitive inhibitor of Pcyt2
phosphocholine
-
a weak competitive inhibitor of Pcyt2
phosphocholine
-
weak, competitive to phosphoethanolamine
phosphocholine
-
a weak competitive inhibitor of Pcyt2
phosphocholine
-
a weak competitive inhibitor of Pcyt2
phosphocholine
-
a weak competitive inhibitor of Pcyt2
phosphoethanolamine methyl-analogues
-
weak competitive inhibitors of Pcyt2
-
phosphoethanolamine methyl-analogues
-
weak competitive inhibitors of Pcyt2
-
phosphoethanolamine methyl-analogues
-
weak competitive inhibitors of Pcyt2
-
phosphoethanolamine methyl-analogues
-
weak competitive inhibitors of Pcyt2
-
phosphoethanolamine methyl-analogues
-
weak competitive inhibitors of Pcyt2
-
phosphoethanolamine methyl-analogues
-
weak competitive inhibitors of Pcyt2
-
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Atherosclerosis
Liver X Receptor Agonists Inhibit the Phospholipid Regulatory Gene CTP: Phosphoethanolamine Cytidylyltransferase-Pcyt2.
Breast Neoplasms
Breast cancer cells adapt to metabolic stress by increasing ethanolamine phospholipid synthesis and CTP:ethanolaminephosphate cytidylyltransferase-Pcyt2 activity.
Breast Neoplasms
Characterization of transcription factors and cis-acting elements that regulate human CTP: phosphoethanolamine cytidylyltransferase (Pcyt2).
Breast Neoplasms
Liver X Receptor Agonists Inhibit the Phospholipid Regulatory Gene CTP: Phosphoethanolamine Cytidylyltransferase-Pcyt2.
Breast Neoplasms
Phosphoethanolamine Accumulation Protects Cancer Cells under Glutamine Starvation through Downregulation of PCYT2.
Dwarfism
Defects in CTP:PHOSPHORYLETHANOLAMINE CYTIDYLYLTRANSFERASE affect embryonic and postembryonic development in Arabidopsis.
Epilepsy
Mutations in PCYT2 disrupt etherlipid biosynthesis and cause a complex hereditary spastic paraplegia.
ethanolamine-phosphate cytidylyltransferase deficiency
Choline supplementation restores substrate balance and alleviates complications of Pcyt2 deficiency.
ethanolamine-phosphate cytidylyltransferase deficiency
Mechanism of hypertriglyceridemia in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
ethanolamine-phosphate cytidylyltransferase deficiency
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Fatty Liver
Mechanism of hypertriglyceridemia in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Fatty Liver
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Hypertriglyceridemia
Mechanism of hypertriglyceridemia in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Hypertriglyceridemia
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Insulin Resistance
Mechanism of hypertriglyceridemia in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Insulin Resistance
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Insulin Resistance
Type 2 diabetes-related proteins derived from an in vitro model of inflamed fat tissue.
Metabolic Syndrome
Mechanism of hypertriglyceridemia in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Metabolic Syndrome
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Muscle Spasticity
Mutations in PCYT2 disrupt etherlipid biosynthesis and cause a complex hereditary spastic paraplegia.
Neoplasms
Breast cancer cells adapt to metabolic stress by increasing ethanolamine phospholipid synthesis and CTP:ethanolaminephosphate cytidylyltransferase-Pcyt2 activity.
Neoplasms
Phosphoethanolamine Accumulation Protects Cancer Cells under Glutamine Starvation through Downregulation of PCYT2.
Obesity
Mechanism of hypertriglyceridemia in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Obesity
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice.
Parkinson Disease
Elevated activity of phospholipid biosynthetic enzymes in substantia nigra of patients with Parkinson's disease.
Spastic Paraplegia, Hereditary
A novel PCYT2 mutation identified in a Chinese consanguineous family with hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
Mutations in PCYT2 disrupt etherlipid biosynthesis and cause a complex hereditary spastic paraplegia.
Starvation
Phosphoethanolamine Accumulation Protects Cancer Cells under Glutamine Starvation through Downregulation of PCYT2.
Starvation
Transcriptional suppression of CTP:phosphoethanolamine cytidylyltransferase by 25-hydroxycholesterol is mediated by nuclear factor-Y and Yin Yang 1.
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malfunction
-
downregulation of the enzyme leads to reduced phosphatidylethanolamine content in eukaryotic elongation factor 1A. iRNA silencing of Pcyt2 results in significant structural changes in the inner mitochondrial membrane topology defined by a loss of disk-like cristae, showing that the modified mitochondria is the earliest structural change observed after Pcyt2 knockdown. Silencing of Pcyt2 impairs the synthesis of phosphatidylethanolamine and normal cell-cycle progression while oxidative phosphorylation is unaltered
malfunction
inhibition of PE biosynthesis leads to parasite death
malfunction
-
Pcyt2-yeast mutant is unable to utilize extracellular ethanolamine for phosphatidylethanolamine synthesis
malfunction
knockdown of PECT1 by artificial microRNA in the SAM ( pFD::amiR-PECT1) accelerated flowering under inductive and even non-inductive conditions, in which FT transcription is almost absent, and in ft-10 twin sister of ft-1 double mutants under both conditions
metabolism
important for Kennedy pathway, essential to bloodstream form
metabolism
-
Phosphatidylethanolamine-Kennedy pathway
metabolism
the enzyme catalyzes the rate-limiting step of the PE metabolic pathway in the parasite
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview. Pcyt2 gene is a target of liver X receptor
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview. Pcyt2 gene is a target of liver X receptor
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview. Pcyt2 gene is a target of liver X receptor
metabolism
rate-limiting enzyme in mammalian phosphatidylethanolamine biosynthesis
metabolism
rate-limiting enzyme in mammalian phosphatidylethanolamine biosynthesis
metabolism
the enzyme regulates phosphatidylethanolamine biosynthesis and controls the phosphatidylethanolamine:phosphatidylcholine ratio
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview. Pcyt2 gene is a target of liver X receptor
-
metabolism
-
the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview. Pcyt2 gene is a target of liver X receptor
-
physiological function
phosphatidylethanolamine is mainly synthesized de novo by the CDP:ethanolamine-dependent Kennedy pathway. Plasmodium falciparum requires massive synthesis of phosphatidylethanolamine that together with phosphatidylcholine constitute the bulk of the malaria membrane lipids
physiological function
-
serum-deficient MCF-7 cells adapt to stress conditions by increasing synthesis and content of phosphatidylethanolamine and diacylglycerol. The biosynthesis of phosphatidylethanolamine from diacylglycerol and ethanolamine is regulated at the level of formation of CDP-ethanolamine, the metabolic step catalyzed by Pcyt2. The catalytic activity of Pcyt2 is elevated 2-3fold, yet the enzyme remains rate-limiting in serum-deficient cells. The mRNA levels of two splice variants, Pcyt2alpha and Pcyt2beta, are 1.5-3fold higher in deficient cells. Elevated diacylglycerol formation and the increased activity of the rate-regulatory enzyme Pcyt2 are critical modulators of the phosphatidylethanolamine Kennedy pathway, and total phosphatidylethanolamine content in serum-deprived breast cancer cells
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis. Phosphatidylethanolamine is the precursor of the ethanolamine phosphoglycerol moiety bound to eukaryotic elongation factor 1A, which plays a crucial role in binding aminoacyl-tRNAs during protein synthesis. The role of Pcyt2 extends to the regulation of mitochondrial function, protein translation and survival in the parasite
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis. Transcriptional regulation of Pcyt2, and Pcyt2 expression in the metabolic syndrome and related disorders, overview. Function of Pcyt2 in cancer cell growth, and Pcyt2 expression in lipid-related disorders and cancer, detailed overview. Phosphatidylethanolamine is the precursor of the ethanolamine phosphoglycerol moiety bound to eukaryotic elongation factor 1A, which plays a crucial role in binding aminoacyl-tRNAs during protein synthesis, the upregulation of Pcyt2 expression in methotrexate-resistant HT-29 cells may be important for the production of phosphoethanolamine as a precursor of ethanolamine-phosphoglycerol moiety bound to eEF1A
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis. Transcriptional regulation of Pcyt2, Pcyt2 expression in lipid-related disorders and cancer, and and Pcyt2 expression in the metabolic syndrome and related disorders, detailed overview
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis. Transcriptional regulation of Pcyt2, Pcyt2 expression in lipid-related disorders and cancer, and and Pcyt2 expression in the metabolic syndrome and related disorders, detailed overview
physiological function
enzyme is composed of two tandem cytidylyltransferase domains. The histidines, especially the first histidine, in the CTP-binding motif HxGH in the N-terminal CT domain are critical for its catalytic activity in vitro, while those in the C-terminal CT domain are not. Overexpression of the wild-type mutants containing amino acid substitutions in the HxGH motif in the C-terminal CT domain suppresses the growth defect of the Saccharomyces cerevisiae mutant of ECT1 in the absence of a phosphatidylethanolamine supply via the decarboxylation of phosphatidylserine, but overexpression of ECT mutants of the N-terminal CT domain does not
physiological function
mouse isoform Pcyt2 can be spliced at introns 7 and 8 to produce a unique isoform, Pcyt2gamma, in which the second cytidylyltransferase domain at the C-terminus becomes deleted. Pcyt2gamma is ubiquitously expressed in embryonic and adult mouse tissues, and is the most abundant in the kidney, skeletal muscle and testis. Pcyt2gamma splicing mechanism dominates over splice variant Pcyt2beta exon-skipping mechanism in most examined tissues. Pcyt2gamma maintains the N-terminal cytidylyltransferase domain, but the lack of the C-terminal cytidylyltransferase domain causes a complete loss of catalytic activity. Pcyt2gamma interacts with the active isoform, splice variant Pcyt2alpha, and significantly reduces Pcyt2alpha homodimerization and activity
physiological function
PECT1 affects flowering by regulating SHORT VEGETATIVE PHASE (SVP) and GIBBERELLIN 20 OXIDASE 2
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis. Transcriptional regulation of Pcyt2, Pcyt2 expression in lipid-related disorders and cancer, and and Pcyt2 expression in the metabolic syndrome and related disorders, detailed overview
-
physiological function
-
the enzyme is important in de novo production of phosphatidylethanolamine, which is the most abundant lipid on the cytoplasmic layer of cellular membranes, with significant roles in cellular processes such as membrane fusion, cell cycle, autophagy, and apoptosis. Transcriptional regulation of Pcyt2, Pcyt2 expression in lipid-related disorders and cancer, and and Pcyt2 expression in the metabolic syndrome and related disorders, detailed overview
-
additional information
-
both isoforms are unique cytidylyltransferases, containing two CTP binding HXGH motifs and large repetitive sequences within the N- and C-domains made by gene duplication. Overexpression of Pcyt2 increases the level of CDP-ethanolamine, but phosphatidylethanolamine content remains unchanged since no adequate diacylglacerol is present
additional information
-
both isoforms are unique cytidylyltransferases, containing two CTP binding HXGH motifs and large repetitive sequences within the N- and C-domains made by gene duplication. Overexpression of Pcyt2 increases the level of CDP-ethanolamine, but phosphatidylethanolamine content remains unchanged since no adequate diacylglacerol is present. Neither the activity of Pcyt2 nor the activities of the other enzymes of the PE Kennedy pathway are changed after partial hepatectomy
additional information
-
the isoforms Pcyt2alpha and Pcyt2beta are unique cytidylyltransferases, containing two CTP binding HXGH motifs and large repetitive sequences within the N- and C-domains made by gene duplication. Overexpression of Pcyt2 increases the level of CDP-ethanolamine, but phosphatidylethanolamine content remains unchanged since no adequate diacylglacerol is present
additional information
the N-terminal CT domain is the only catalytically active domain of the enzyme. The inactive C-terminal domain is important for dimer stabilization. Homology modelling, three-dimensional structural model of Pf ECT, overview
additional information
-
the N-terminal CT domain is the only catalytically active domain of the enzyme. The inactive C-terminal domain is important for dimer stabilization. Homology modelling, three-dimensional structural model of Pf ECT, overview
additional information
-
the isoforms Pcyt2alpha and Pcyt2beta are unique cytidylyltransferases, containing two CTP binding HXGH motifs and large repetitive sequences within the N- and C-domains made by gene duplication. Overexpression of Pcyt2 increases the level of CDP-ethanolamine, but phosphatidylethanolamine content remains unchanged since no adequate diacylglacerol is present
-
additional information
-
both isoforms are unique cytidylyltransferases, containing two CTP binding HXGH motifs and large repetitive sequences within the N- and C-domains made by gene duplication. Overexpression of Pcyt2 increases the level of CDP-ethanolamine, but phosphatidylethanolamine content remains unchanged since no adequate diacylglacerol is present. Neither the activity of Pcyt2 nor the activities of the other enzymes of the PE Kennedy pathway are changed after partial hepatectomy
-
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25-hydroxycholesterol, an endogenous activator of liver X receptor, and the liver X receptor synthetic agonist TO901317 both significantly reduce the biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway by inhibiting the promoter function and expression of Pcyt2 in human MCF-7 cells. The enzyme is downregulated in insulin-resistant muscle
-
increased Pcyt2 mRNA levels after serum starvation
increased Pcyt2 mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
increases after serum starvation
induction of the enzyme by phorbol-12-myristate-13-acetate in hepatocytes. Liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. The enzyme is upregulated in obesity-resistant rats and by thiamine supplementation
liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. Pcyt2 is transcriptionally up-regulated by serum-deficiency induced differentiation of the skeletal muscle cells C2C12. The core mouse promoter (-111/+29)is dependent on binding of cEBP to an inverse CCAT box located at the position -82/-77 bp, ncreased amount of muscle-specific regulator, MyoD, reduced the content of Sp1 (binds to region -508/-378 bp), which, together with the decrease in ratio of Sp1 to Sp3, is responsible for the stimulation of transcription of Pcyt2 gene in differentiated C2C12 myotubes relative to undifferentiated myoblasts. The enzyme is upregulated in Sirtuin null mice and in adipose tissue of high-weight gainers
liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. Pcyt2 is upregulated in methotrexate-resistant HT-29 cells in comparison to a methotrexate-sensitive colon cancer cell line
-
oxysterols, 24-hydroxycholesterol, 25-hydroxycholesterol, 27-hydroxycholesterol, and 24(S),25-epoxycholesterol, and mevalonolactate are partially responsible for the inhibition of Pcyt2 transcription. 25-Hydroxycholesterol, an endogenous activator of liver X receptor, and the liver X receptor synthetic agonist TO901317 both significantly reduce the biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway by inhibiting the promoter function and expression of Pcyt2 in mouse embryonic fibroblasts. The enzyme is downregulated in sphingosine 1-phosphate lyase null mice and in livers of copper-transporting ATPase ATP7B null mice, downregulation in ATF2 null mice
significantly upregulated during muscle cell differentiation
-
the important element for transcriptional control of Pcyt2 by 25-HC resides between -56 and -36 in NIH 3T3 cells. Nuclear factor-Y binds at C(-37)CAAT(-41) and Yin Yang1 binds at C(-42)AT(-40) in the Pcyt2 promoter. Nuclear factor-Y is involved in the inhibitory effects of 25-hydroxycholesterol on Pcyt2 transcription
-
increased Pcyt2 mRNA levels after serum starvation
increased Pcyt2 mRNA levels after serum starvation
increased Pcyt2 mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
increased Pcyt2 mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
increases after serum starvation
-
increases after serum starvation
-
induction of the enzyme by phorbol-12-myristate-13-acetate in hepatocytes. Liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. The enzyme is upregulated in obesity-resistant rats and by thiamine supplementation
-
induction of the enzyme by phorbol-12-myristate-13-acetate in hepatocytes. Liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. The enzyme is upregulated in obesity-resistant rats and by thiamine supplementation
-
-
liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. Pcyt2 is transcriptionally up-regulated by serum-deficiency induced differentiation of the skeletal muscle cells C2C12. The core mouse promoter (-111/+29)is dependent on binding of cEBP to an inverse CCAT box located at the position -82/-77 bp, ncreased amount of muscle-specific regulator, MyoD, reduced the content of Sp1 (binds to region -508/-378 bp), which, together with the decrease in ratio of Sp1 to Sp3, is responsible for the stimulation of transcription of Pcyt2 gene in differentiated C2C12 myotubes relative to undifferentiated myoblasts. The enzyme is upregulated in Sirtuin null mice and in adipose tissue of high-weight gainers
-
liver X receptor, LXR, can modulate and activate promoter activity and transcription of Pcyt2. Pcyt2 is transcriptionally up-regulated by serum-deficiency induced differentiation of the skeletal muscle cells C2C12. The core mouse promoter (-111/+29)is dependent on binding of cEBP to an inverse CCAT box located at the position -82/-77 bp, ncreased amount of muscle-specific regulator, MyoD, reduced the content of Sp1 (binds to region -508/-378 bp), which, together with the decrease in ratio of Sp1 to Sp3, is responsible for the stimulation of transcription of Pcyt2 gene in differentiated C2C12 myotubes relative to undifferentiated myoblasts. The enzyme is upregulated in Sirtuin null mice and in adipose tissue of high-weight gainers
-
-
oxysterols, 24-hydroxycholesterol, 25-hydroxycholesterol, 27-hydroxycholesterol, and 24(S),25-epoxycholesterol, and mevalonolactate are partially responsible for the inhibition of Pcyt2 transcription. 25-Hydroxycholesterol, an endogenous activator of liver X receptor, and the liver X receptor synthetic agonist TO901317 both significantly reduce the biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway by inhibiting the promoter function and expression of Pcyt2 in mouse embryonic fibroblasts. The enzyme is downregulated in sphingosine 1-phosphate lyase null mice and in livers of copper-transporting ATPase ATP7B null mice, downregulation in ATF2 null mice
-
oxysterols, 24-hydroxycholesterol, 25-hydroxycholesterol, 27-hydroxycholesterol, and 24(S),25-epoxycholesterol, and mevalonolactate are partially responsible for the inhibition of Pcyt2 transcription. 25-Hydroxycholesterol, an endogenous activator of liver X receptor, and the liver X receptor synthetic agonist TO901317 both significantly reduce the biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway by inhibiting the promoter function and expression of Pcyt2 in mouse embryonic fibroblasts. The enzyme is downregulated in sphingosine 1-phosphate lyase null mice and in livers of copper-transporting ATPase ATP7B null mice, downregulation in ATF2 null mice
-
-
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Sundler, R.
Ethanolaminephosphate cytidylyltransferase. Purification and characterization of the enzyme from rat liver
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Ethanolamine-phosphate cytidylyltransferase
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Vermeulen, P.S.; Geelen, M.J.H.; van Golde, L.M.G.
Substrate specificity of CTP: phosphoethanolamine cytidylyltransferase purified from rat liver
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Membrane lipid biosynthesis in Chlamydomonas reinhardtii: expression and characterization of CTP:phosphoethanolamine cytidylyltransferase
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Chlamydomonas reinhardtii (Q84JV7), Chlamydomonas reinhardtii
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Crystallization and preliminary X-ray analysis of CTP:phosphoethanolamine cytidylyltransferase (ECT) from Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
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Saccharomyces cerevisiae
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Metabolic and molecular aspects of ethanolamine phospholipid biosynthesis: the role of CTP:phosphoethanolamine cytidylyltransferase (Pcyt2)
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Developmental and metabolic effects of disruption of the mouse CTP:phosphoethanolamine cytidylyltransferase gene (Pcyt2)
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Mus musculus
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Mizoi, J.; Nakamura, M.; Nishida, I.
Defects in CTP:phosphorylethanolamine cytidylyltransferase affect embryonic and postembryonic development in Arabidopsis
Plant Cell
18
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2006
Arabidopsis thaliana
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Signorell, A.; Jelk, J.; Rauch, M.; Buetikofer, P.
Phosphatidylethanolamine is the precursor of the ethanolamine phosphoglycerol moiety bound to eukaryotic elongation factor 1A
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283
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2008
Trypanosoma brucei
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Tie, A.; Bakovic, M.
Alternative splicing of CTP:phosphoethanolamine cytidylyltransferase produces two isoforms that differ in catalytic properties
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48
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2007
Mus musculus (Q922E4), Mus musculus
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Stimulation of the human CTP:phosphoethanolamine cytidylyltransferase gene by early growth response protein 1
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49
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2008
Homo sapiens
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Ando, H.; Horibata, Y.; Yamashita, S.; Oyama, T.; Sugimoto, H.
Low-density lipoprotein and oxysterols suppress the transcription of CTP:Phosphoethanolamine cytidylyltransferase in vitro
Biochim. Biophys. Acta
1801
487-495
2010
Homo sapiens, Mus musculus
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Zhu, L.; Michel, V.; Bakovic, M.
Regulation of the mouse CTP: phosphoethanolamine cytidylyltransferase gene Pcyt2 during myogenesis
Gene
447
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2009
Mus musculus
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Fullerton, M.D.; Hakimuddin, F.; Bonen, A.; Bakovic, M.
The development of a metabolic disease phenotype in CTP:phosphoethanolamine cytidylyltransferase-deficient mice
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284
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Mus musculus
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Leonardi, R.; Frank, M.W.; Jackson, P.D.; Rock, C.O.; Jackowski, S.
Elimination of the CDP-ethanolamine pathway disrupts hepatic lipid homeostasis
J. Biol. Chem.
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Mus musculus
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Gibellini, F.; Hunter, W.N.; Smith, T.K.
The ethanolamine branch of the Kennedy pathway is essential in the bloodstream form of Trypanosoma brucei
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73
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2009
Trypanosoma brucei (B9WNA0), Trypanosoma brucei
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Zhu, L.; Bakovic, M.
Breast cancer cells adapt to metabolic stress by increasing ethanolamine phospholipid synthesis and CTP:ethanolaminephosphate cytidylyltransferase-Pcyt2 activity
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90
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2012
Homo sapiens
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Maheshwari, S.; Lavigne, M.; Contet, A.; Alberge, B.; Pihan, E.; Kocken, C.; Wengelnik, K.; Douguet, D.; Vial, H.; Cerdan, R.
Biochemical characterization of Plasmodium falciparum CTP:phosphoethanolamine cytidylyltransferase shows that only one of the two cytidylyltransferase domains is active
Biochem. J.
450
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Plasmodium falciparum (Q8IDM2), Plasmodium falciparum
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Pavlovic, Z.; Bakovic, M.
Regulation of phosphatidylethanolamine homeostasis - the critical role of CTP:phosphoethanolamine cytidylyltransferase (Pcyt2)
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14
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Homo sapiens, Mus musculus, Mus musculus C57BL/6, Plasmodium berghei, Rattus norvegicus, Rattus norvegicus Wistar, Saccharomyces cerevisiae, Trypanosoma brucei
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Tian, S.; Ohtsuka, J.; Wang, S.; Nagata, K.; Tanokura, M.; Ohta, A.; Horiuchi, H.; Fukuda, R.
Human CTP:phosphoethanolamine cytidylyltransferase: enzymatic properties and unequal catalytic roles of CTP-binding motifs in two cytidylyltransferase domains
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449
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Homo sapiens (Q99447), Homo sapiens
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Ando, H.; Aoyama, C.; Horibata, Y.; Satou, M.; Mitsuhashi, S.; Itoh, M.; Hosaka, K.; Sugimoto, H.
Transcriptional suppression of CTP:phosphoethanolamine cytidylyltransferase by 25-hydroxycholesterol is mediated by nuclear factor-Y and Yin Yang 1
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471
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Mus musculus
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Pavlovic, Z.; Singh, R.K.; Bakovic, M.
A novel murine CTP:phosphoethanolamine cytidylyltransferase splice variant is a post-translational repressor and an indicator that both cytidylyltransferase domains are required for activity
Gene
543
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2014
Mus musculus (Q540F5), Mus musculus
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Pavlovic, Z.; Zhu, L.; Pereira, L.; Singh, R.; Cornel, R.; Bakovic, M.
Isoform-specific and protein kinase C-mediated regulation of CTP:phosphoethanolamine cytidylyltransferase phosphorylation
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Homo sapiens (Q99447), Homo sapiens
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Susila, H.; Nasim, Z.; Gawarecka, K.; Jung, J.Y.; Jin, S.; Youn, G.; Ahn, J.H.
Phosphorylethanolamine cytidyltransferase 1 modulates flowering in a florigen-independent manner by regulating SVP
Development
148
dev193870
2020
Arabidopsis thaliana (Q9ZVI9), Arabidopsis thaliana
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Ando, H.; Horibata, Y.; Aoyama, C.; Shimizu, H.; Shinohara, Y.; Yamashita, S.; Sugimoto, H.
Side-chain oxysterols suppress the transcription of CTP phosphoethanolamine cytidylyltransferase and 3-hydroxy-3-methylglutaryl-CoA reductase by inhibiting the interaction of p300 and NF-Y, and H3K27 acetylation
J. Steroid Biochem. Mol. Biol.
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Mus musculus (Q922E4), Homo sapiens (Q99447)
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