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Information on EC 2.7.8.2 - diacylglycerol cholinephosphotransferase and Organism(s) Homo sapiens and UniProt Accession Q9Y6K0
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2.7.8.2 diacylglycerol cholinephosphotransferaseIUBMB Comments
1-Alkyl-2-acylglycerol can act as acceptor; this activity was previously listed separately.
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Word Map
- 2.7.8.2
- diacylglycerols
- acyltransferase
- phosphatidylethanolamine
- cytidylyltransferase
- phospholipase
- phosphatidate
- cdpcholine
-
platelet-activating
-
ctp:phosphocholine
- 1,2-diacylglycerols
-
cholinephosphate
- cmp
- cdp-ethanolamine
- lysophosphatidylcholine
- glycerolipids
- glycerophospholipids
-
14ccholine
- 1,2-diacyl-sn-glycerols
-
ptdcho
-
acetylhydrolase
-
disaturated
- lysolecithin
-
lyso-paf
-
kennedy
- paf-ah
-
phosphotransferases
-
2.7.7.15
-
3hcholine
-
cdp-alcohol
-
methyl-3hcholine
-
alkylacylglycerols
- glycerolphosphate
-
methyl-14ccholine
- 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine
-
phosphatidyltransferase
- paf-acetylhydrolase
- phosphoglycerides
- synthesis
- analysis
- biotechnology
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cholinephosphotransferase, choline phosphotransferase, cept1, paf-cpt, dtt-insensitive cholinephosphotransferase, diacylglycerol cholinephosphotransferase, phosphorylcholine glyceride transferase, 1,2-diacylglycerol cholinephosphotransferase, aapt1, phosphatidylcholine:diacylglycerol cholinephosphotransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CEPT1
1-alkyl-2-acetyl-m-glycerol:CDP-choline choline phosphotransferase
-
-
-
-
1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase
-
-
-
-
1-alkyl-2-acetylglycerol cholinephosphotransferase
-
-
-
-
AAPT
-
-
-
-
alkylacylglycerol choline phosphotransferase
-
-
-
-
alkylacylglycerol cholinephosphotransferase
-
-
-
-
aminoalcoholphosphotransferase
-
-
-
-
CDP-choline diglyceride phosphotransferase
-
-
-
-
CEPT
-
-
-
-
choline phosphotransferase
cholinephosphotransferase
cholinephosphotransferase, 1-alkyl-2-acetylglycerol
-
-
-
-
cholinephosphotransferase, diacylglycerol
-
-
-
-
CPT
cytidine diphosphocholine glyceride transferase
-
-
-
-
cytidine diphosphorylcholine diglyceride transferase
-
-
-
-
diacylglycerol choline phosphotransferase
-
-
-
-
DTT-insensitive CDP-choline: 1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase
-
-
PAF-CPT
-
PAF: platelet activating factor, to be distinguished from PC-CPT, PC: phosphatidylcholine
phosphocholine diacylglyceroltransferase
-
-
-
-
phosphorylcholine-glyceride transferase
-
-
-
-
sn-1,2-diacylglycerol cholinephosphotransferase
-
-
-
-
cholinephosphotransferase
-
-
-
-
CPT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
CDP-choline:1,2-diacyl-sn-glycerol cholinephosphotransferase
1-Alkyl-2-acylglycerol can act as acceptor; this activity was previously listed separately.
CAS REGISTRY NUMBER
COMMENTARY
77237-98-0
formerly, EC 2.7.8.16
9026-13-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylethanolamine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
preferred substrates in decreasing order: di-10:0 diacylglycerol, di-16:1 diacylglycerol, di-8:0 diacylglycerol, di-18:1 diacylglycerol, 16:0/22:6 diacylglycerol
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
preferred substrates in decreasing order, activation by Mg2+: di18:1-diacylglycerol, 16:0/22:6-diacylglycerol, 16:0/18:1-diacylglycerol, 18:0/20:4-diacylglycerol, di16:0-diacylglycerol, preferred substrates in decreasing order, activation by Mn2+: di10:0-diacylglycerol, 18:1/2:0-diacylglycerol, 16:0/22:6-diacylglycerol, di18:1-diacylglycerol, di16:0-diacylglycerol, di14:1-diacylglycerol, di16:1-diacylglycerol
-
?
CDP-choline + 1,2-diacylglycerol
CMP + a phosphatidylcholine
-
preferred substrates: di-18:1-diacylglycerol, di-16:1-diacylglycerol, 16:0/18:1-diacylglycerol, 16:0/22:6-diacylglycerol
-
-
?
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
-
platelet activating factor (PAF) de novo biosynthesis
-
-
?
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
-
37°C, 20 min, pH 8, in presence of 15 mM dithiothreitol, 5 mM EDTA, 20 mM MgCl2, 1 mg/ml bovine serum albumin
analysis by thin-layer chromatography
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
CDP-ethanolamine + 1,2-diacylglycerol
CMP + phosphatidylethanolamine
-
preferred substrates in decreasing order: di-18:1 diacylglycerol, di-16:1 diacylglycerol, 16:0/18:1 diacylglycerol, 16:0/22:6 diacylglycerol
-
-
?
CDP-ethanolamine + 1,2-diacylglycerol
CMP + phosphatidylethanolamine
-
preferred substrates: 16:0/18:1 diacylglycerol, di-18:1 diacylglycerol, di-18:1 diacylglycerol
-
-
?
additional information
?
-
the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1
-
-
?
additional information
?
-
the enzyme has dual specificity for both CDP-choline and CDP-ethanolamine, EC 2.7.8.1
-
-
?
additional information
?
-
no substrates: 16:0(O)/2:0-diacylglycerol, 16:0(O)/20:4-diacylglycerol
-
-
?
additional information
?
-
-
no substrates: 16:0(O)/2:0-diacylglycerol, 16:0(O)/20:4-diacylglycerol
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
increase in cholinephosphotransferase gene expression with cadmium in all cell lines, significant increase in 11-9-1-4 cells and MCF-12F cells. Cell lines MCF-12F, MCF-7, BT-549 and 11-9-1-4 show mutations in their nucleotide sequence as the result of cadmium treatment. The effect of cadmium is highest in MCF-12F cell line that shows a total of six mutations
-
-
?
additional information
?
-
the enzyme is specific for CDP-choline, no activity with CDP-ethanolamine. The reaction occurs at the hydrophobic-hydrophilic interface of membranes which impacts kinetic behavior
-
-
?
additional information
?
-
the enzyme is specific for CDP-choline, no activity with CDP-ethanolamine. The reaction occurs at the hydrophobic-hydrophilic interface of membranes which impacts kinetic behavior
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-ethanolamine + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylethanolamine
-
-
-
r
CDP-choline + 1,2-diacyl-sn-glycerol
CMP + a phosphatidylcholine
-
-
-
r
CDP-choline + 1-O-alkyl-2-acetyl-sn-glycerol
CMP + 1-O-alkyl-2-acetyl-sn-glycerol 3-phosphocholine
-
platelet activating factor (PAF) de novo biosynthesis
-
-
?
CDP-choline + sn-1,2-diacylglycerol
?
-
final reaction in synthesis of phosphatidylcholine
-
-
?
additional information
?
-
-
ultimate step in the Kennedy pathway for the genesis of de novo synthesized phosphatidylcholine
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
final step of the biosynthesis of platelet activating factor, PAF, in the de novo pathway
-
-
?
additional information
?
-
-
increase in cholinephosphotransferase gene expression with cadmium in all cell lines, significant increase in 11-9-1-4 cells and MCF-12F cells. Cell lines MCF-12F, MCF-7, BT-549 and 11-9-1-4 show mutations in their nucleotide sequence as the result of cadmium treatment. The effect of cadmium is highest in MCF-12F cell line that shows a total of six mutations
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
activation, 10fold more than Mn2+, preferred substrates in decreasing order, activation by Mg2+: di18:1-diacylglycerol, 16:0/22:6-diacylglycerol, 16:0/18:1-diacylglycerol, 18:0/20:4-diacylglycerol, di16:0-diacylglycerol
Mn2+
-
activates, acts mostly on ethanolaminephosphotransferase activity, inhibitory above 10 mM
Mn2+
activation, but much less than Mg2+, preferred substrates in decreasing order, activation by Mn2+: di10:0-diacylglycerol, 18:1/2:0-diacylglycerol, 16:0/22:6-diacylglycerol, di18:1-diacylglycerol, di16:0-diacylglycerol, di14:1-diacylglycerol, di16:1-diacylglycerol
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
0.1 mM (14.1% activity left) or 1 mM (1.41% activity left), estimated in presence of 20 mM Mg2+, inhibition partially reduced in presence of 0.5 mM EDTA: 33.3% or 3.70% activity left for 0.1 mM or 1 mM Ca2+, respectively (100% activity: 20 mM Mg2+, 0.5 mM EDTA, no Ca2+)
INFalpha
-
250 inhibitory units/microl, 51% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
polar lipids from olive oil
-
5.2 ng/microl, 33% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
polar lipids from olive pomace
-
1.8 ng/microl, 48% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
polar lipids from sea bass
-
59 ng/microl, 45% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
polar lipids from sea bream
-
123 ng/microl, 17% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
resveratrol
-
100 microM, 39% inhibition of enzyme activity in microsomal fraction of mesangial cells
rupatadine
-
20 ng/microl, 60% inhibition of enzyme activity in microsomal fraction of mesangial cells
salicylic acid
-
250 ng/microl, 38% inhibition of enzyme activity in microsomal fraction of mesangial cells
simvastatine
-
40 ng/microl, 92% inhibition of enzyme activity in microsomal fraction of mesangial cells
tinzaparin
-
0.25 inhibitory units/microl, 30% inhibition of enzyme activity in microsomal fraction of mesangial cells
-
additional information
detergent micelles that are used to deliver the DAG substrate for the assay can inhibit the reaction
-
additional information
detergent micelles that are used to deliver the DAG substrate for the assay can inhibit the reaction
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
specific activity increases in presence of 0.5-2 mg/ml bovine serum albumin, microsomal fraction of human mesangial cells
-
dithiothreitol
-
specific activity slightly increases at dithiothreitol (DTT) concentrations above 1 mM, optimum stimulation at 15 mM DTT, microsomal fraction of human mesangial cells
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0593
1-O-alkyl-2-acetyl-sn-glycerol
-
optimum reaction conditions, in presence of 100 microM CDP-choline
0.0166
CDP-choline
-
optimum reaction conditions, in presence of 100 microM 1-O-alkyl-2-acetyl-sn-glycerol
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00036
-
microsomal fraction of human mesangial cells, maximum activity in presence of 1 mg/ml bovine serum albumin, 15 mM dithiothreitol, 20 mM Mg2+, 0.5 mM EDTA
additional information
additional information
-
linear relationship between initial velocity and protein concentration in microsomal fraction of human mesangial cells up to 0.1 mg/ml
additional information
-
Pefabloc has no affect on enzyme activity, microsomal fraction of human mesangial cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
microsomal fraction of human mesangial cells (HMC), bell-shaped temperature activity profile
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
CEPT1 is elevated in diseased lower extremity arterial intima of individuals with peripheral arterial disease and diabetes
CEPT1 is elevated in carotid plaque of patients with diabetes
CEPT1 is elevated in diseased lower extremity arterial intima of individuals with peripheral arterial disease and diabetes
-
normal: MCF-12A and MCF-12F and cancerous: MCF-7, BT-549 and 11-9-1-4
-
HMC, immortilized by transfection with T-antigen of SV40 and Hras oncogene
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
co-purifies with crude mitochondria during subcellular fractionation of organelles
-
additional information
additional information
CPT/CEPT enzymes reside in multiple subcellular membranes that can move among organelles
-
additional information
CPT/CEPT enzymes reside in multiple subcellular membranes that can move among organelles
-
additional information
-
no activity detectable in cytoplasmic fraction of mesangial cells
-
additional information
the enzyme localization is not altered upon treatment of cells with brefeldin A
-
additional information
the enzyme localization is not altered upon treatment of cells with brefeldin A
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
reduction of phosphatidylcholine, e.g. by bacterial infection, results in apoptosis
metabolism
the CDP-choline and CDP-ethanolamine pathways are separate routes of phospholipid biosynthesis in mammalian cells, although the CEPT is probably a participant in both pathways. The CPT activity responsible for the synthesis of platelet-activating factor (PAF) is different from those responsible for PtdCho synthesis on the basis of the enzyme's sensitivity to dithiothreitol. Molecular regulation of the CDP-choline pathway, overview. The CDP-choline pathway of phosphatidylcholine synthesis is essential in proliferating cells. The phosphatidylcholine pool is dynamic and the amount of PtdCho represents a balance between synthesis and degradation. Physiological role of the CDP-choline pathway, overview
physiological function
CEPT1 is important for phosphatidylethanolamine formation from fatty acids such as 32:2, 32:1, 34:2, and 34:1, i.e. reaction of EC 2.7.8.1. Brefeldin A treatment does not significantly affect the levels of the different phosphatidylethanolamine species. CEPT1 greatly prefers diacylglycerols 16:0-18:1 to other acceptors
malfunction
inhibition of the CPT activity reduces phospholipid synthesis and results in accumulation of CPT substrates. Reduction of phosphatidylcholine, e.g. by bacterial infection, results in apoptosis
metabolism
CPT catalyzes the final step in the synthesis of phosphatidylcholine via the Kennedy pathway by the transfer of phosphocholine from CDP-choline to 1,2-diacyl-sn-glycerol. The CDP-choline and CDP-ethanolamine pathways are separate routes of phospholipid biosynthesis in mammalian cells, although the CEPT is probably a participant in both pathways. Molecular regulation of the CDP-choline pathway, DNA synthesis and phosphatidylcholine synthesis are not linked, overview. The CDP-choline pathway of phosphatidylcholine synthesis is essential in proliferating cells. The phosphatidylcholine pool is dynamic and the amount of PtdCho represents a balance between synthesis and degradation. phosphatidylcholine and other phospholipids are synthesized in the G2/M phase, rather than S phase. Physiological role of the CDP-choline pathway, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CEPT1_HUMAN
416
8
46554
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46500
-
x * 46500, hCEPT1, SDS-PAGE and deduced from gene sequence, seven membrane-spanning helices
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
integral membrane-bound protein, overview on structure and properties
?
-
x * 46500, hCEPT1, SDS-PAGE and deduced from gene sequence, seven membrane-spanning helices
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
20 min heating results in loss of 80% of activity, microsomal fraction of human mesangial cells (HMC)
60
-
20 min heating results in total loss of activity, microsomal fraction of human mesangial cells (HMC)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the gene encoding CPT, but not CEPT, EC 2.7.8.1, increases during lipopolysaccahride-induced endoplasmic reticulum biogenesis in B-lymphocytes
expression of the gene encoding CPT, but not CEPT, EC 2.7.8.1, increases during lipopolysaccahride-induced endoplasmic reticulum biogenesis in B-lymphocytes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
since CPT expression is associated with elaboration of new endoplasmic reticulum membrane, it may be useful as a marker protein for endoplasmic reticulum expansion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, T.C.; Snyder, F.
1-Alkyl-2-acetyl-sn-glycerol cholinephosphotransferase
Methods Enzymol.
209
279-283
1992
Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Heller, R.; Bussolino, F.; Ghigo, D.; Garbarino, G.; Pescarmona, G.; Till, U.; Bosia, A.
Stimulation of platelet-activating factor synthesis in human endothelial cells by activation of the de novo pathway. Phorbol 12-myristate 13-acetate activates 1-alkyl-2-lyso-sn-glycero-3-phosphate:acetyl-CoA acetyltransferase and dithiothreitol-insensitive 1-alkyl-2-acetyl-sn-glycerol:CDP-choline cholinephosphotransferase
J. Biol. Chem.
266
21358-21361
1991
Homo sapiens
Henneberry, A.L.; McMaster, C.R.
Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine
Biochem. J.
339
291-298
1999
Homo sapiens
-
McMaster, C.R.; Bell, R.M.
CDP-choline:1,2-diacylglycerol cholinephosphotransferase
Biochim. Biophys. Acta
1348
100-110
1997
Saccharomyces cerevisiae, Glycine max, Homo sapiens, Mesocricetus auratus, Rattus norvegicus
Wright, M.M.; McMaster, C.R.
PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1)
Lipids
37
663-672
2002
Homo sapiens
Henneberry, A.L.; Wistow, G.; McMaster, C.R.
Cloning, genomic organization, and characterization of a human cholinephosphotransferase
J. Biol. Chem.
275
29808-29815
2000
Homo sapiens (Q8WUD6), Homo sapiens
Roy, S.S.; Mukherjee, S.; Mukhopadhyay, S.; Das, S.K.
Differential effect of cadmium on cholinephosphotransferase activity in normal and cancerous human mammary epithelial cell lines
Mol. Cancer Ther.
3
199-204
2004
Homo sapiens
Sriburi, R.; Bommiasamy, H.; Buldak, G.L.; Robbins, G.R.; Frank, M.; Jackowski, S.; Brewer, J.W.
Coordinate regulation of phospholipid biosynthesis and secretory pathway gene expression in XBP-1(S)-induced endoplasmic reticulum biogenesis
J. Biol. Chem.
282
7024-7034
2007
Homo sapiens (Q8WUD6)
Fagone, P.; Sriburi, R.; Ward-Chapman, C.; Frank, M.; Wang, J.; Gunter, C.; Brewer, J.W.; Jackowski, S.
Phospholipid biosynthesis program underlying membrane expansion during B-lymphocyte differentiation
J. Biol. Chem.
282
7591-7605
2007
Homo sapiens
Tsoupras, A.B.; Fragopoulou, E.; Nomikos, T.; Iatrou, C.; Antonopoulou, S.; Demopoulos, C.A.
Characterization of the de novo biosynthetic enzyme of platelet activating factor, DDT-insensitive cholinephosphotransferase, of human mesangial cells
Mediators Inflamm.
2007
27683
2007
Homo sapiens
Fagone, P.; Jackowski, S.
Phosphatidylcholine and the CDP-choline cycle
Biochim. Biophys. Acta
1831
523-532
2013
Glycine max (I1KH05), Saccharomyces cerevisiae (P17898), Saccharomyces cerevisiae, Homo sapiens (Q8WUD6), Homo sapiens (Q9Y6K0)
Zayed, M.A.; Jin, X.; Yang, C.; Belaygorod, L.; Engel, C.; Desai, K.; Harroun, N.; Saffaf, O.; Patterson, B.W.; Hsu, F.F.; Semenkovich, C.F.
CEPT1-mediated phospholipogenesis regulates endothelial cell function and ischemia-induced angiogenesis through PPARalpha
Diabetes
70
549-561
2020
Homo sapiens (Q9Y6K0), Homo sapiens, Mus musculus (Q8BGS7)
EXTERNAL LINKS (specific for EC-Number 2.7.8.2)
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