2.7.7.14: ethanolamine-phosphate cytidylyltransferase
This is an abbreviated version!
For detailed information about ethanolamine-phosphate cytidylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.14
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2.7.7.14
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phosphatidylethanolamine
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phospholipid
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cdp-ethanolamine
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diacylglycerols
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kennedy
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cdp-choline
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ctp:phosphocholine
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phosphocholine
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3hethanolamine
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ptdetn
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ethanolaminephosphotransferase
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14cethanolamine
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drug development
- 2.7.7.14
- phosphatidylethanolamine
- phospholipid
- cdp-ethanolamine
- diacylglycerols
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kennedy
- cdp-choline
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ctp:phosphocholine
- phosphocholine
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3hethanolamine
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ptdetn
- ethanolaminephosphotransferase
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14cethanolamine
- drug development
Reaction
Synonyms
CTP-phosphoethanolamine cytidylyltransferase, CTP:ethanolaminephosphate cytidylyltransferase, CTP:phosphoethanolamine CT, CTP:phosphoethanolamine cytidylyltransferase, CTP:phosphoethanolamine cytidylyltransferase gene, cytidylyltransferase, ethanolamine phosphate, ECT, ET, ethanolamine phosphate cytidylyltransferase, ethanolamine-phosphate cytidylyltransferase, Pcyt2, Pcyt2alpha, Pcyt2beta, PECT1, phosphoethanolamine cytidyltransferase, phosphoethanolamine cytidylyltransferase, phosphorylethanolamine transferase, Tb11.01.5730
ECTree
2.7.7.14 ethanolamine-phosphate cytidylyltransferaseAdvanced search results
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General Information on EC 2.7.7.14 - ethanolamine-phosphate cytidylyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
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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
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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
the enzyme catalyzes the rate-limiting step of the PE metabolic pathway in the parasite
metabolism
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the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview
metabolism
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the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview
metabolism
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the enzyme is important and the main regulatory enzyme in de novo production of phosphatidylethanolamine via the CDP-ethanolamine Kennedy pathway, overview
metabolism
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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
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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
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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
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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
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metabolism
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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physiological function
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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
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additional information
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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
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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
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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
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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
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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
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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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