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Information on EC 2.7.7.15 - choline-phosphate cytidylyltransferase
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2.7.7.15 choline-phosphate cytidylyltransferaseSpecify your search results
Word Map
- 2.7.7.15
- phosphatidylcholine
- phospholipid
- phosphatidylethanolamine
- surfactant
- fetal
- diacylglycerol
- phospholipase
-
ptdcho
- alveolar
-
cholinephosphotransferase
- oleate
- phosphatidylglycerol
-
amphipathic
-
membrane-binding
- n-methyltransferase
-
disaturated
- lysophosphatidylcholine
- phosphatidate
-
3hcholine
-
vance
-
kennedy
-
cytidyltransferase
- 1,2-diacylglycerols
- phosphoethanolamine
-
3hglycerol
-
amphitropic
-
l-forms
-
methyl-14ccholine
- hexadecylphosphocholine
- analysis
- diagnostics
-
choline-deficient
- cdpcholine
-
methyl-3hcholine
-
2.7.8.2
-
14ccholine
-
ctp:phosphoethanolamine
-
choline-containing
- cdp-ethanolamine
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
ctp:phosphocholine cytidylyltransferase, cctalpha, ctalpha, phosphocholine cytidylyltransferase, pcyt1a, cholinephosphate cytidylyltransferase, cctbeta, choline-phosphate cytidylyltransferase, ctp:phosphocholine cytidylyltransferase alpha, ctp:choline-phosphate cytidylyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CCT
CCT-alpha
CCT1
CCT2
CCTalpha
CCTbeta2
CCTbeta3
CDP-choline pyrophosphorylase
-
-
-
-
CDP-choline synthetase
-
-
-
-
choline phosphate cytidylyltransferase
CTP-phosphocholine cytidylyltransferase
-
-
-
-
CTP:cholinephosphate cytidylyltransferase
-
-
-
-
CTP:phosphocholine cytidylyltransferase
CTP:phosphocholine cytidylyltransferase alpha
CTP:phosphocholine cytidylyltransferase beta2
CTP:phosphocholine cytidylyltransferase-alpha
CTP:phosphocholine cytidylyltransferase-beta2
CTP:phosphorylcholine cytidylyltransferase
-
-
-
-
cytidine diphosphocholine pyrophosphorylase
-
-
-
-
cytidylyltransferase, choline phosphate
-
-
-
-
phosphocholine cytidylyltransferase
-
-
-
-
phosphorylcholine cytidylyltransferase
-
-
-
-
phosphorylcholine transferase
-
-
-
-
phosphorylcholine:CTP cytidylyltransferase
-
-
-
-
additional information
CCT
-
-
-
-
choline phosphate cytidylyltransferase
-
-
-
-
CTP:phosphocholine cytidylyltransferase
-
-
-
-
additional information
-
different isoforms, CCTalpha and CCTbeta 2 and -3, CCTbeta 1 is not found in mice
additional information
-
four isoforms, CCTalpha ubiquitously expressed, whereas CCTbeta 1,-2, and -3 restricted in distribution
additional information
-
four isoforms, CCTalpha ubiquitously expressed, whereas CCTbeta 1,-2, and -3 restricted in distribution
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + phosphocholine = diphosphate + CDP-choline
catalytic mechanism
-
CTP + phosphocholine = diphosphate + CDP-choline
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
CTP:choline-phosphate cytidylyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9026-34-0
-
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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
CTP + phosphodimethylethanolamine
diphosphate + CDPdimethylethanolamine
-
-
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine, inhibition of CCT triggers apoptosis, involved in cold acclimation
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine, inhibition of CCT triggers apoptosis
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
-
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine, inhibition of CCT triggers apoptosis, disruption of CCTbeta leads to gonadal dysfunction and reduced fertility
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
-
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
-
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
rate limiting step in synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
dCTP can replace CTP with reduced activity
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
-
642894, 642895, 642896, 642898, 642900, 642902, 642903, 642904, 642905, 642906, 642907, 642908, 642909, 642913, 642914, 642915, 642916, 642919, 642921, 642923, 642924, 642926, 642928
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
highly specific for phosphocholine
-
-
r
CTP + choline phosphate
diphosphate + CDPcholine
-
beta2 isoform specifically up-regulated during neuronal differentiation to increase phosphatidyl choline biosynthesis for growing neuritis
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
rate limiting step in synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
membrane binding segment has important role in cellular lipid metabolism
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
catalyzes a major rate-limiting step in the biosynthesis of phosphocholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
catalyzes a major rate-limiting step in the biosynthesis of phosphocholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
highly specific for CTP or dCTP
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
ATP can replace CTP with less efficiency
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
plays a role in the biosynthesis of the phosphocholine-derivatized cell wall constituents that are critical for cell separation and pathogenesis
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
biosynthesis of the choline containing cell wall antigens, teichoic acid and lipoteichoic acid
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
biosynthesis of the choline containing cell wall antigens, teichoic acid and lipoteichoic acid
-
-
?
CTP + ethanolamine phosphate
diphosphate + CDPethanolamine
-
poor substrate
-
-
?
CTP + phosphocholine
diphosphate + CDP-choline
when dissociated from membranes, a portion of the M domain functions as an auto-inhibitory element to suppress catalysis. It is proposed that membrane binding enables bending of thex02E helices, bringing the active site closer to the membrane surface
-
-
?
CTP + phosphomonomethylethanolamine
diphosphate + CDPmethylethanolamine
-
-
-
-
?
CTP + phosphomonomethylethanolamine
diphosphate + CDPmethylethanolamine
-
-
-
?
additional information
?
-
-
key regulatory enzyme in the CDP-choline pathway for the biosynthesis of phosphatidylcholine, hepatic phosphatidylcholine biosynthesis is an important regulator of plasma high density lipoprotein
-
-
?
additional information
?
-
-
active lipoprotein form, i.e. H-form, is the membrane-associated form of the enzyme in adult lung
-
-
?
additional information
?
-
-
comparison of lipid regulation of yeast and rat enzyme
-
-
?
additional information
?
-
-
H-form is the active form of enzyme in cytoplasm
-
-
?
additional information
?
-
-
change in relative distribution of H-form and L-form in cytosol may be important in the regulation of phosphatidylcholine synthesis
-
-
?
additional information
?
-
-
active form of enzyme on the ER, enzyme in cytosol appears to be latent
-
-
?
additional information
?
-
-
CTbeta2 facilitates neurite outgrowth and branching
-
-
?
additional information
?
-
-
development of an assay method for determination of the catalytic activity measuring the production of radiolabeled CDP-choline from 14C-labeled phosphocholine, and separation of non-radioactive CDP-choline from CTP by C18 reverse phase HPLC using a mobile phase of 0.1 M ammonium bicarbonate (98%) and acetonitrile (2%) at pH 7.4, evaluation, overview
-
-
?
additional information
?
-
-
no substrates: ethanolamine phosphate and phosphodimethylethanolamine
-
-
?
additional information
?
-
-
comparison of lipid regulation of yeast and rat enzyme
-
-
?
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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
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine, inhibition of CCT triggers apoptosis, involved in cold acclimation
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine, inhibition of CCT triggers apoptosis
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine, inhibition of CCT triggers apoptosis, disruption of CCTbeta leads to gonadal dysfunction and reduced fertility
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
rate limiting step in synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
beta2 isoform specifically up-regulated during neuronal differentiation to increase phosphatidyl choline biosynthesis for growing neuritis
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
rate limiting step in synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
membrane binding segment has important role in cellular lipid metabolism
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
catalyzes a major rate-limiting step in the biosynthesis of phosphocholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
catalyzes a major rate-limiting step in the biosynthesis of phosphocholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
plays a role in the biosynthesis of the phosphocholine-derivatized cell wall constituents that are critical for cell separation and pathogenesis
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
biosynthesis of the choline containing cell wall antigens, teichoic acid and lipoteichoic acid
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
-
biosynthesis of the choline containing cell wall antigens, teichoic acid and lipoteichoic acid
-
-
?
additional information
?
-
-
key regulatory enzyme in the CDP-choline pathway for the biosynthesis of phosphatidylcholine, hepatic phosphatidylcholine biosynthesis is an important regulator of plasma high density lipoprotein
-
-
?
additional information
?
-
-
active lipoprotein form, i.e. H-form, is the membrane-associated form of the enzyme in adult lung
-
-
?
additional information
?
-
-
comparison of lipid regulation of yeast and rat enzyme
-
-
?
additional information
?
-
-
H-form is the active form of enzyme in cytoplasm
-
-
?
additional information
?
-
-
change in relative distribution of H-form and L-form in cytosol may be important in the regulation of phosphatidylcholine synthesis
-
-
?
additional information
?
-
-
active form of enzyme on the ER, enzyme in cytosol appears to be latent
-
-
?
additional information
?
-
-
CTbeta2 facilitates neurite outgrowth and branching
-
-
?
additional information
?
-
-
comparison of lipid regulation of yeast and rat enzyme
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Co2+ results in significant activity at a concentration of 25 mM, with 41% of the activity seen with 25 mM Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
Mg2+
Mn2+
Ni2+
Ni2+ yields approximately 9% of the activity seen with Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
Zn2+
Zn2+ results in catalytic activity of only 1% when compared to the activity in the presence of Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
Ca2+
Ca2+ yields approximately 9% of the activity seen with Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
Mg2+
the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
Mg2+
-
maximal activity at 10-40 mM, concentrations above 40 mM are inhibitory
Mn2+
Mn2+ results in significant activity at a concentration of 25 mM, with 51% of the activity seen with 25 mM Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
Mn2+
-
can partially replace Mg2+, maximal activity at 5 mM, concentrations above 5 mM are inhibitory
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calpain
-
calpain degrades CCTalpha, 0.6 pmol of calpain effectively cleaves 80% of purified CCTalpha (0.7 pmol) in the absence of calmodulin
-
NaCl
-
inhibitory above 200 mM, 39% inhibition at 300 mM, 67% inhibition at 500 mM
Trifluoperazine
-
5fold inhibition of microsomal enzyme at 0.025 mM, 50% inhibition at 0.75mM, addition of saturating amounts of rat liver phospholipid reverses inhibition, no inhibition of hepatocytes at 0.02 mM
Urea
-
50% inhibition of wild-type enzyme at 0.75 M, 50% inhibition of H92N mutant enzyme at 0.35 M, 50% inhibition of H92Q mutant enzyme at 0.2 M
1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphatidylcholine
-
ET-18-OCH3, non-hydrolyzable lysophosphatidylcholine analog, competitive with respect to the lipid activator
1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphatidylcholine
-
ET-18-OCH3, non-hydrolyzable lysophosphatidylcholine analog, competitive with respect to the lipid activator
ATP
-
extent of inhibition is dependent on preincubation time, temperature and Mg2+ and Ca2+ concentration
Ca2+
50% inhibition of recombinant enzyme at 0.32 mM, 50% inhibition of native enzyme at 0.27 mM
chlorpromazine
-
5fold inhibition of microsomal enzyme at 0.025 mM, 50% inhibition at 0.75mM, addition of saturating amounts of rat liver phospholipid reverses inhibition, no inhibition of hepatocytes at 0.02 mM
chlorpromazine
-
inhibition of liver enzyme, no inhibition of gut enzyme at 0.08 mM
lysophosphatidylcholine
-
generated as a consequence of the activation of cytosolic phospholipase A2 by protein kinase C-alpha and p38 mitogen-activated protein kinase
lysophosphatidylcholine
-
competitive with respect to the lipid activator, 50% inhibition at 0.025 mM in the presence of phosphatidylcholine/oleic acid
lysophosphatidylcholine
-
99% inhibition of L-form, only partial inhibition of H-form
N-ethylmaleimide
-
80% inhibition at 1.5 mM; CTP and phosphocholine protect
oxidized low density lipoprotein
-
40% inhibition by increase of enzyme degradation; 75% inhibition by increase of enzyme degradation
-
additional information
-
no inhibition by ATP; no inhibition by CDP; no inhibition by CMP
-
additional information
-
inhibited with spore extract from Stachybotrys chartarum isolated in Cleveland, no effect with extracts from the same organism isolated in Hawaii
-
additional information
when dissociated from membranes, a portion of the M domain functions as an auto-inhibitory element to suppress catalysis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activator protein-1
-
potential regulator of CCTbeta2 expression in neuronal cells
-
fatty acids
-
activity slightly enhanced by addition of saturated fatty acids, markedly increased by addition of unsaturated fatty acids regardless of chain length and number of double bonds
phosphatidylcholine
6fold enhancement of activity at 0.025 mM
retinoblastoma protein
-
regulates CTalpha expression by different mechanisms depending on the phase of the cell cycle, the regulation of CTalpha expression requires both the Sp1 and the retinoblastoma control elements
-
Sp1
-
Sp1 stimulates CTalpha transcription, and Sp1-mediated transcription is stimulated by the retinoblastoma protein
-
conduritol-B-epoxide
-
treatment of macrophages with 0.5 mM conduritol-B-epoxide results in elevated activity of CCT
conduritol-B-epoxide
-
treatment of macrophages with 0.5 mM conduritol-B-epoxide results in elevated activity of CCT
Lipids
-
regulation of activity by reversible association with membrane lipids
-
Lipids
-
regulation of activity by reversible association with membrane lipids, preferentially activated by anionic lipids, highest activation with phosphatidylcholine vesicles containing diphosphatidylglycerol (29fold), less activation with vesicles containing phosphatidylserine (16fold), phosphatidylinositol (21fold), phosphatidylethanolamine (17fold), and oleate (13fold), compared to free enzyme 5fold activation with enzyme associated with pure phosphatidylcholine vesicles
-
Lipids
-
regulation of activity by reversible association with membrane lipids
-
Lipids
-
regulation of activity by reversible association with membrane lipids
-
Lipids
-
regulation of activity by reversible association with membrane lipids
-
Lipids
-
regulation of activity by reversible association with membrane lipids
-
Lipids
-
regulation of activity by reversible association with membrane lipids, activation of enzyme when bound to lipid vesicles, vesicles containing 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine or egg phosphatidylglycerol are more effective than vesicles containing 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine, 1,2-dioleoyl-sn-glycerol, or egg phosphatidylcholine
-
Lipids
-
regulation of activity by reversible association with membranes containing anionic lipids
-
additional information
phosphatidylethanolamine and phosphatidic acid do not have a significant effect on CCT1 activity
-
additional information
phosphatidylethanolamine and phosphatidic acid do not have a significant effect on CCT1 activity
-
additional information
-
phosphatidylethanolamine and phosphatidic acid do not have a significant effect on CCT1 activity
-
additional information
-
binding to the lipid droplets activates the enzyme
-
additional information
-
CDP-choline increases enzyme activity after induction of ischemia
-
additional information
probucol does not have any diret stimulatory effect on CCT
-
additional information
probucol does not have any diret stimulatory effect on CCT
-
additional information
-
the full length CCT requires activation via association with lipids and has been reported to have activity 50fold lower in the absence of lipids when compared to the activity of CCTalpha236
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Effects of hypoxia, glucose deprivation and acidosis on phosphatidylcholine synthesis in HL-1 cardiomyocytes. CTP:phosphocholine cytidylyltransferase activity correlates with sarcolemmal disruption.
Adenocarcinoma
Phosphatidylcholine synthesis regulates triglyceride storage and chylomicron secretion by Caco2 cells.
Adenocarcinoma of Lung
PCYT1A suppresses proliferation and migration via inhibiting mTORC1 pathway in lung adenocarcinoma.
Brain Diseases
Kinetic and biochemical properties of CTP:choline-phosphate cytidylyltransferase from the rat brain.
Brain Ischemia
CDP-choline significantly restores phosphatidylcholine levels by differentially affecting phospholipase A2 and CTP: phosphocholine cytidylyltransferase after stroke.
Brain Ischemia
Cytidine-5'-diphosphocholine affects CTP-phosphocholine cytidylyltransferase and lyso-phosphatidylcholine after transient brain ischemia.
Carcinoma
Increased expression of cytosolic chaperonin CCT in human hepatocellular and colonic carcinoma.
Carcinoma, Embryonal
Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle.
Carcinoma, Hepatocellular
Expression of phosphatidylethanolamine N-methyltransferase in Yoshida ascites hepatoma cells and the livers of host rats.
Carcinoma, Hepatocellular
Expression of phosphatidylethanolamine N-methyltransferase-2 in McArdle-RH7777 hepatoma cells inhibits the CDP-choline pathway for phosphatidylcholine biosynthesis via decreased gene expression of CTP:phosphocholine cytidylyltransferase.
Carcinoma, Hepatocellular
Increased expression of cytosolic chaperonin CCT in human hepatocellular and colonic carcinoma.
Carcinoma, Hepatocellular
Phosphatidylethanolamine N-methyltransferase: unexpected findings from curiosity-driven research.
Cerebral Palsy
Morphometric analysis of acetabular dysplasia in cerebral palsy: three-dimensional CT study.
Choline Deficiency
Choline deficiency causes translocation of CTP:phosphocholine cytidylyltransferase from cytosol to endoplasmic reticulum in rat liver.
Choline Deficiency
Effect of choline deficiency on CTP: phosphocholine cytidylyltransferase and choline kinase activities in rat liver subcellular fractions.
choline-phosphate cytidylyltransferase deficiency
Polyploid formation via chromosome duplication induced by CTP:phosphocholine cytidylyltransferase deficiency and Bcl-2 overexpression: identification of two novel endogenous factors.
Cone-Rod Dystrophies
Mutations in PCYT1A cause spondylometaphyseal dysplasia with cone-rod dystrophy.
Cone-Rod Dystrophies
Mutations in PCYT1A, encoding a key regulator of phosphatidylcholine metabolism, cause spondylometaphyseal dysplasia with cone-rod dystrophy.
Cone-Rod Dystrophies
Mutations in the PCYT1A gene are responsible for isolated forms of retinal dystrophy.
Cone-Rod Dystrophies
Novel mutations in PCYT1A are responsible for spondylometaphyseal dysplasia with cone-rod dystrophy.
Dehydration
Identification and characterization of CTP:phosphocholine cytidylyltransferase CpCCT1 in the resurrection plant Craterostigma plantagineum.
Endometriosis
Polymorphic variants of folate and choline metabolism genes and the risk of endometriosis-associated infertility.
Fatty Liver
Mutations disrupting the Kennedy phosphatidylcholine pathway in humans with congenital lipodystrophy and fatty liver disease.
Fatty Liver
Mutations in the PCYT1A gene are responsible for isolated forms of retinal dystrophy.
Fetal Death
Polymorphic variants of genes involved in choline pathway and the risk of intrauterine fetal death.
Gaucher Disease
Changes in macrophage morphology in a Gaucher disease model are dependent on CTP:phosphocholine cytidylyltransferase alpha.
Gaucher Disease
Phosphatidylcholine synthesis is elevated in neuronal models of Gaucher disease due to direct activation of CTP:phosphocholine cytidylyltransferase by glucosylceramide.
Infections
Chronic Pseudomonas aeruginosa infection reduces surfactant levels by inhibiting its biosynthesis.
Infections
Enteropathogenic Escherichia coli infection triggers host phospholipid metabolism perturbations.
Insulin Resistance
Accelerated phosphatidylcholine turnover in macrophages promotes adipose tissue inflammation in obesity.
Lipodystrophy
Mutations in the PCYT1A gene are responsible for isolated forms of retinal dystrophy.
Liver Cirrhosis
Metabolomics combined with network pharmacology exploration reveals the modulatory properties of Astragali Radix extract in the treatment of liver fibrosis.
Liver Diseases
Mutations in the PCYT1A gene are responsible for isolated forms of retinal dystrophy.
Lung Injury
Adenoviral gene transfer of a mutant surfactant enzyme ameliorates pseudomonas-induced lung injury.
Lung Injury
Nitric oxide-induced activation of NF-kappaB-mediated NMDA-induced CTP:phosphocholine cytidylyltransferase alpha expression inhibition in A549 cells.
Lung Neoplasms
PCYT1A suppresses proliferation and migration via inhibiting mTORC1 pathway in lung adenocarcinoma.
Lymphoma
MYC is a positive regulator of choline metabolism and impedes mitophagy-dependent necroptosis in diffuse large B-cell lymphoma.
Lymphoma, B-Cell
Polyploid formation via chromosome duplication induced by CTP:phosphocholine cytidylyltransferase deficiency and Bcl-2 overexpression: identification of two novel endogenous factors.
Neoplasms
CTP:phosphocholine cytidylyltransferase inhibition by ceramide via PKC-alpha, p38 MAPK, cPLA2, and 5-lipoxygenase.
Neoplasms
Differential targets and subcellular localization of antitumor alkyl-lysophospholipid in leukemic versus solid tumor cells.
Neoplasms
Increased expression of cytosolic chaperonin CCT in human hepatocellular and colonic carcinoma.
Neoplasms
MYC is a positive regulator of choline metabolism and impedes mitophagy-dependent necroptosis in diffuse large B-cell lymphoma.
Neoplasms
PCYT1A suppresses proliferation and migration via inhibiting mTORC1 pathway in lung adenocarcinoma.
Neoplasms
Pharmacological inhibition of phosphatidylcholine biosynthesis is associated with induction of phosphatidylinositol accumulation and cytolysis of neoplastic cell lines.
Neoplasms
Tumor necrosis factor-alpha inhibits expression of CTP:phosphocholine cytidylyltransferase.
Neuroblastoma
Production of diacylglycerol by exogenous phospholipase C stimulates CTP:phosphocholine cytidylyltransferase activity and phosphatidylcholine synthesis in human neuroblastoma cells.
Pancreatic Neoplasms
Identification of prognostic lipid droplet-associated genes in pancreatic cancer patients via bioinformatics analysis.
Parkinson Disease
Elevated activity of phospholipid biosynthetic enzymes in substantia nigra of patients with Parkinson's disease.
Polycystic Ovary Syndrome
Methylome and transcriptome profiling revealed epigenetic silencing of LPCAT1 and PCYT1A associated with lipidome alterations in polycystic ovary syndrome.
Premature Birth
Evidence for a regulatory role of CTP : choline phosphate cytidylyltransferase in the synthesis of phosphatidylcholine in fetal lung following premature birth.
Quadriplegia
Morphometric analysis of acetabular dysplasia in cerebral palsy: three-dimensional CT study.
Respiratory Insufficiency
Role of phosphocholine cytidylyltransferase alpha in lung development.
Retinal Dystrophies
Mutations in the PCYT1A gene are responsible for isolated forms of retinal dystrophy.
Retinoblastoma
Sp-1 binds promoter elements that are regulated by retinoblastoma and regulate CTP:phosphocholine cytidylyltransferase-alpha transcription.
Sepsis
Adenoviral gene transfer of a mutant surfactant enzyme ameliorates pseudomonas-induced lung injury.
Spinal Dysraphism
CHKA and PCYT1A gene polymorphisms, choline intake and spina bifida risk in a California population.
Starvation
Alteration in the characters of CDP-choline synthetase and phospholipid-choline exchange enzyme upon choline starvation in Chinese hamster ovary cells.
Stroke
CDP-choline significantly restores phosphatidylcholine levels by differentially affecting phospholipase A2 and CTP: phosphocholine cytidylyltransferase after stroke.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.33
choline phosphate
wild-type deletion construct 1-236, 8.8 mM CTP
0.48
choline phosphate
Y173A mutant deletion construct 1-236, 8.8 mM CTP
2.5
choline phosphate
H168A mutant deletion construct 1-236, 8.8 mM CTP
3.2
choline phosphate
H168A/Y173A mutant deletion construct 1-236, 8.8 mM CTP
0.17
CTP
pH and temperature not specified in the publication, wild-type enzyme
0.28
CTP
pH and temperature not specified in the publication, H630N mutant
7.3
CTP
wild-type deletion construct 1-236, 1.5 mM choline phosphate
7.7
CTP
H168A mutant deletion construct 1-236, 1.5 mM choline phosphate
7.7
CTP
Y173A mutant deletion construct 1-236, 1.5 mM choline phosphate
8.8
CTP
H168A/Y173A mutant deletion construct 1-236, 1.5 mM choline phosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
CTP
H630N mutant, pH and temperature not specified in the publication
1.45
CTP
wild-type enzyme, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.021
H168A/Y173A mutant deletion construct 1-236, variable CTP concentration, 1.5 mM choline phosphate
0.034
H168A mutant deletion construct 1-236, variable CTP concentration, 1.5 mM choline phosphate
0.055
H168A/Y173A mutant deletion construct 1-236, variable choline phosphate concentration, 8.8 mM CTP
0.069
H168A mutant deletion construct 1-236, variable choline phosphate concentration, 8.8 mM CTP
0.116
Y173A mutant deletion construct 1-236, variable choline phosphate concentration, 8.8 mM CTP
0.167
Y173A mutant deletion construct 1-236, variable CTP concentration, 1.5 mM choline phosphate
1.724
wild-type deletion construct 1-236, variable choline phosphate concentration, 8.8 mM CTP
10
wild-type protein in the presence of 0.01 mM phosphatidylcholine:oleate
3.399
wild-type deletion construct 1-236, variable CTP concentration, 1.5 mM choline phosphate
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
pH 6: about 80% of activity maximum, pH 8: about 60% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
male Mongolian gerbil, induction of brain ischemia resulted in loss of enzyme activity in cytosol and membrane
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
642889, 642890, 642894, 642895, 642896, 642897, 642898, 642900, 642902, 642903, 642907, 642908, 642914, 642916, 642924, 642929, 661213
brenda
-
BAC1.2F5 cell line, SCF-1-dependent clone derived from the BAC1 line which originated from transfection of splenic adherent cells with SV40
brenda
-
Cortical, primary sympathetic and cultured primary, isozyme CTbeta2 mRNA and protein are abundant in distal axons of mouse sympathetic neurons, whereas isozyme CTalpha mRNA and protein are not detected
brenda
-
CTbeta2 is abundant in axons of sympathetic neurons and retinal ganglion cells
brenda
-
primary sympathetic and cultured primary, isozyme CTbeta2 mRNA and protein are abundant in distal axons of mouse sympathetic neurons, whereas isozyme CTalpha mRNA and protein are not detected
brenda
-
primary sympathetic and cultured primary, isozyme CTbeta2 mRNA and protein are abundant in distal axons of mouse sympathetic neurons, whereas isozyme CTalpha mRNA and protein are not detected
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
nuclear membrane association of CCTa induced by oleate loading is linked to dephosphorylation of S319
brenda
additional information
-
distributed between cytosol and membrane, lipid environment required for activity
brenda
activation of phosphatidylcholine biosynthesis by phospholipase C treatment induces the partial nuclear-to-cytoplasmic translocation of the enzyme
brenda
-
-
642889, 642890, 642893, 642894, 642897, 642900, 642902, 642904, 642905, 642908, 642909, 642913, 642914, 642924, 660981
brenda
CCTbeta expression appears to be cytosolic within these Purkinje cells
brenda
mainly located in the endoplasmic reticulum
brenda
-
CTP:phosphocholine cytidylyltransferase binds stably and via its amphipatic alpha helix to lipid droplet surface during surface expansion, which is essential for the lipid droplet. It is the only enzyme of the phosphatidylecholine synthesis Kennedy pathway that localizes in the lipid droplets
brenda
-
CTP:phosphocholine cytidylyltransferase binds stably and via its amphipatic alpha helix to lipid droplet surface during surface expansion, which is essential for the lipid droplet. It is the only enzyme of the phosphatidylecholine synthesis Kennedy pathway that localizes in the lipid droplets
brenda
-
distributed between cytosol and membrane, lipid environment required for activity
brenda
-
enzyme is activated when bound to vesicles
brenda
-
enzyme is activated when bound to vesicles
brenda
-
L-form binds to microsomal membrane, is formed in to H-form and H-form is released from membrane
-
brenda
-
in CHO cells, CCTalpha is nucleoplasmic and colocalized with GFP-progerin in nuclear folds and invaginations
brenda
-
reversibly translocates to nuclear tubules projecting from the nucleoplasmic reticulum in response to oleate
brenda
-
lipid activation of the enzyme results in its translocation to the nuclear envelope and expansion of an intranuclear membrane network termed the nucleoplasmic reticulum by a mechanism involving membrane deformation
brenda
-
CCT-alpha forms intranuclear foci that colocalise with invaginations in prelamin-A-accumulating cells, overview
brenda
-
lipid activation of the enzyme results in its translocation to the nuclear envelope and expansion of an intranuclear membrane network termed the nucleoplasmic reticulum by a mechanism involving membrane deformation
brenda
Plasmodium-specific lysine-rich insertion within the catalytic domain of the enzyme acts as a nuclear localization signal and its deletion decreases the nuclear propensity of the protein in the model cell line. The putative membrane-binding domain also affected the nuclear localization of the protein. Activation of phosphatidylcholine biosynthesis by phospholipase C treatment induces the partial nuclear-to-cytoplasmic translocation of the enzyme
brenda
additional information
-
immunohistochemic analysis of enzyme subcellular localization, overview
-
brenda
additional information
-
CCT1 Is mobile and shuttles between nucleus and cytosol before oleate loading. CCT1 targets to lipid droplets after an initial delay and relocalizes to the nucleus when oleate is removed. CCT1 is targeted to lipid droplets when phosphatidylcholine levels are inadequate
-
brenda
additional information
-
immunohistochemic analysis of enzyme subcellular localization, overview
-
brenda
additional information
-
CCT1 Is mobile and shuttles between nucleus and cytosol before oleate loading. CCT1 targets to lipid droplets after an initial delay and relocalizes to the nucleus when oleate is removed. CCT1 is targeted to lipid droplets when phosphatidylcholine levels are inadequate
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
-
CTP:phosphocholine cytidylyltransferase beta3 (CCTbeta3) may be targeted to suppress prolonged autophagy in cancer cells in vivo
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme is a member of the cytidylyltransferase family of enzymes that utilize cytidine 5'-triphosphate (CTP) to synthesize molecules that are typically precursors to membrane phospholipids
evolution
the conformational malleability of the x02E helix pair that bridges the membrane binding and catalytic domains of the enzyme makes it an ideal element adapted by evolution for transducing signals from membrane to active site
malfunction
-
acute prelamin A accumulation after reduction of the activity of the ZMPSTE24 endoprotease by siRNA knockdown, results in the generation of a complex nucleoplasmic reticulum that depends for its formation on the CTP:phosphocholinecytidylyltransferase-a, this structure can form during interphase, confirming that it is independent of mitosis and therefore not a consequence of disordered nuclear envelope assembly
malfunction
-
isozyme CTbeta2 deficiency in distal axons reduces the incorporation of choline into by 95% whereas phosphatidylcholine synthesis in cell bodies/proximal axons is unaltered. Brains of mice lacking CTbeta2 have normal phosphatidylethanolamine content despite having 35% lower enzyme activity than wild-type brains. Axon branching, but not axon extension, is impaired in CTbeta2-deficient neurons. Phenotypes, overview
malfunction
-
isozyme CTbeta2 deficiency in distal axons reduces the incorporation of choline into by 95% whereas phosphatidylcholine synthesis in cell bodies/proximal axons is unaltered. Brains of mice lacking CTbeta2 have normal phosphatidylethanolamine content despite having 35% lower enzyme activity than wild-type brains. Axon branching, but not axon extension, is impaired in CTbeta2-deficient neurons. Phenotypes, overview
malfunction
mutations in the gene encoding CTP:phosphocholine cytidylyltransferase (PCYT1A) cause three distinct pathologies in humans: lipodystrophy, spondylometaphyseal dysplasia with cone-rod dystrophy (SMD-CRD), and isolated retinal dystrophy
malfunction
without cholinephosphate cytidylyltransferase (CPCT), Leishmania major parasites cannot incorporate choline into phosphatidylcholine, yet the CPCT-null mutants contain similar levels of phosphatidylcholine and phosphatidylethanolamine as wild type parasites. Loss of CPCT does not affect the growth of parasites in complete medium or their virulence in mice. The results suggest that other mechanisms of phosphatidylcholine synthesis can compensate the loss of CPCT. CPCT-null parasites exhibit severe growth defects when ethanolamine and exogenous lipids became limited or when they are co-cultured with certain bacteria that are known to be members of sandfly midgut microbiota
malfunction
-
isozyme CTbeta2 deficiency in distal axons reduces the incorporation of choline into by 95% whereas phosphatidylcholine synthesis in cell bodies/proximal axons is unaltered. Brains of mice lacking CTbeta2 have normal phosphatidylethanolamine content despite having 35% lower enzyme activity than wild-type brains. Axon branching, but not axon extension, is impaired in CTbeta2-deficient neurons. Phenotypes, overview
-
metabolism
-
the enzyme catalyzes a step in the Kennedy pathway for phosphatidylecholine synthesis, overview
metabolism
-
the enzyme catalyzes a step in the Kennedy pathway for phosphatidylecholine synthesis, overview
metabolism
-
the enzyme catalyzes conversion of phosphocholine and CTP to cytidine diphosphocholine (CDP-choline), a step critical for synthesis of the membrane phospholipid phosphatidylcholine
metabolism
CTP:phosphocholine cytidylyltransferase is the key regulatory enzyme in phosphatidylcholine synthesis
metabolism
rate limiting step of the de novo phosphatidylcholine biosynthesis is catalysed by CTP:phosphocholine cytidylyltransferase, which has a key regulatory function within the pathway
metabolism
rate-limiting enzyme of the lipid biosynthesis pathway
metabolism
the enzyme catalyzes the formation of CDP-choline, a key intermediate in the choline branch of the Kennedy pathway
physiological function
-
CTP:phosphocholine cytidylyltransferase alpha is a nuclear enzyme that catalyzes the rate-limiting step in the CDP-choline pathway for phosphatidylcholine synthesis. Lipid activation of the enzyme results in its translocation to the nuclear envelope and expansion of an intranuclear membrane network termed the nucleoplasmic reticulum by a mechanism involving membrane deformation. CCTalpha and lamins specifically cooperate to form the nucleoplasmic reticulum, but the overall structure of the nuclear envelope has a minimal impact on enzyme activity and phosphocholine synthesis
physiological function
-
CTP:phosphocholine cytidylyltransferase alpha is a nuclear enzyme that catalyzes the rate-limiting step in the CDP-choline pathway for phosphatidylcholine synthesis. The enzyme is not involved in the Hutchinson-Gilford progeria syndrome, overview
physiological function
-
CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
-
CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
-
CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
-
CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
physiological function
-
importance of isozyme CTbeta2 for phosphatidylcholine synthesis as well as for axon formation, growth and branching of primary sympathetic neurons
physiological function
-
importance of isozyme CTbeta2 for phosphatidylcholine synthesis as well as for axon formation, growth and branching of primary sympathetic neurons
physiological function
-
nucleoplasmic reticulum development seems dependent on the enzyme CTP:phosphocholine-cytidylyltransferase-alpha, which is responsible for phosphatidylcholine synthesis for the biosynthesis and curvature of membranes, but nucleoplasmic reticulum development is independent of mitosis. Colocalisation of prelamin A and lamin B1 with a developing nucleoplasmic reticulum is dependent on CTP:phosphocholine-cytidylyltransferase-alpha
physiological function
-
phosphatidylcholine acts as a surfactant to prevent lipid droplet coalescence, which otherwise yields large, lipolysis-resistant lipid droplets and triglyceride accumulation. The need for additional phosphatidylecholine to coat the enlarging surface during lipid droplet expansion is provided by the Kennedy pathway, which is activated by reversible targeting of the rate-limiting enzyme, CTP:phosphocholine cytidylyltransferase, to growing lipid droplet surfaces. CCT1 regulates lipid droplet size and triacylgylceride storage in vivo
physiological function
-
phosphatidylcholine acts as a surfactant to prevent lipid droplet coalescence, which otherwise yields large, lipolysis-resistant lipid droplets and triglyceride accumulation. The need for additional phosphatidylecholine to coat the enlarging surface during lipid droplet expansion is provided by the Kennedy pathway, which is activated by reversible targeting of the rate-limiting enzyme, CTP:phosphocholine cytidylyltransferase, to growing lipid droplet surfaces. CCT1 regulates lipid droplet size and triacylgylceride storage in vivo
physiological function
CTP:phosphocholine cytidylyltransferase-alpha (CCTalpha) and CCTbeta catalyze the rate limiting step in phosphatidylcholine biosynthesis
physiological function
-
key regulatory enzyme for phosphatidylcholine synthesis in plants
physiological function
-
phosphatidylcholine synthesis through CCTbeta3 (CTP:phosphocholine cytidylyltransferase beta3) activation on lipid droplets is crucial for sustaining autophagy and long-term cell survival
physiological function
-
importance of isozyme CTbeta2 for phosphatidylcholine synthesis as well as for axon formation, growth and branching of primary sympathetic neurons
-
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan
Show AA Sequence and Transmembrane Helices (5722 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000
-
L-form of enzyme, gel filtration, aggregates in the cytosol to form high molecular weight species (H-form) with a median value of 1200000
284000
-
Hep G2 cells, H-form of enzyme, glycerol density gradient centrifugation
30000
38000
-
x * 45000, catalytic subunit + x * 38000, functional role of this subunit not documented, SDS-PAGE
41724
-
2 * 41724, calculated from the deduced amino acid sequence, 2 * 42211, mass spectrometry, phosphorylated protein
42000
42211
-
2 * 41724, calculated from the deduced amino acid sequence, 2 * 42211, mass spectrometry, phosphorylated protein
45000
48000
80000 - 110000
-
diffuse band in SDS-PAGE using chemically cross-linked protein
42000
-
2 * 42000, SDS-PAGE, if bound to a detergent micelle or membrane vesicle the purified native enzyme is a dimer composed of two noncovalently linked 42000 MW subunits, in the absence of a membrane or micelle, the dimers self-aggregate in a reversible manner
45000
-
x * 45000, catalytic subunit + x * 38000, functional role of this subunit not documented, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
?
-
x * 45000, catalytic subunit + x * 38000, functional role of this subunit not documented, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE, if bound to a detergent micelle or membrane vesicle the purified native enzyme is a dimer composed of two noncovalently linked 42000 MW subunits, in the absence of a membrane or micelle, the dimers self-aggregate in a reversible manner
dimer
-
2 * 41724, calculated from the deduced amino acid sequence, 2 * 42211, mass spectrometry, phosphorylated protein
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
phosphoprotein
lipoprotein
-
H-form appears to be a lipoprotein consisting of an apoprotein i.e. L-form dimer of 45000 MW subunits complexed with lipids
lipoprotein
-
phosphatidylinositol is present in the H-form isolated from Hep G2 cells
phosphoprotein
-
phosphorylation reduces membrane binding and therefore decreases activity
phosphoprotein
sucrose nonfermenting 1-related protein kinase 1 (SnRK1) mediates the phosphorylation and concomitant inhibition of CTP:phosphocholine cytidylyltransferase 1 (AtCCT1)
phosphoprotein
-
phosphorylated on serine and threonine but not on tyrosine residues
phosphoprotein
-
phosphorylation reduces membrane binding and therefore decreases activity
phosphoprotein
oleate treatment of cultured cells triggers CCTalpha translocation to the nuclear envelope and nuclear lipid droplets and rapid dephosphorylation of pS319. Removal of oleate leads to dissociation of CCTalpha from the nuclear envelope and increased phosphorylation of S319. Choline depletion of cells causes CCTalpha translocation to the nuclear envelope and S319 dephosphorylation. Y359 and S362 are constitutively phosphorylated during oleate addition and removal. The P-domain undergoes negative charge polarization due to dephosphorylation of S319 and possibly other proline-directed sites and retention of Y359 and S362 phosphorylation. Dephosphorylation of S319 and S315 is involved in CCTalpha recruitment to nuclear membranes
phosphoprotein
-
16 serine and 2 tyrosine residues available for phosphorylation, phosphorylation is associated with decreased membrane binding and therefore, decreased activity
phosphoprotein
-
phosphorylation reduces membrane binding and therefore decreases activity
phosphoprotein
-
phosphorylation is confined to 15-16 serine residues near the C-terminus
phosphoprotein
-
phosphorylation is restricted to the C-terminal 52 amino acids and occurs on multiple sites, 0.2 mol phosphate per mol enzyme
phosphoprotein
-
16 serine and 2 tyrosine residues available for phosphorylation, phosphorylation is associated with decreased membrane binding and therefore, decreased activity
phosphoprotein
-
C-terminal region is highly phosphorylated, phosphorylation decreases membrane affinity and is therefore involved in regulation of enzyme activity
phosphoprotein
-
enzyme phosphorylation is involved in regulation of activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L246S/W249S/I256S/I257S
part of a putative amphipathic alpha helix
A93T
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes retinal dystrophy
A99T
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia
A99V
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia
E129K
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia
E280del
a single amino acid deletion in the autoinhibitory helix increases the constitutive (lipid-independent) enzyme activity x024fold. E280del enhances the response of the enzyme to anionic lipid vesicles 4fold. Mutation causes lipodystrophy in heterozygous status. Mutation causes lipodystrophy
F191L
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia
P150A
missense variant in the catalytic domain, low solubility linked to reduced activity in cell lysates, consistent with aberrant folding and aggregation. Mutation causes spondylometaphyseal dysplasia with cone-rod dystrophy
R223S
mutation in a signal-transducing linker between the catalytic and membrane-binding domains, impaired enzymatic activity without fold-destabilization. Mutation causes spondylometaphyseal dysplasia
R283stop
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia
S114T
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia
S333L.fs164
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes lipodystrophy
V142M
missense variant in the catalytic domain, low solubility linked to reduced activity in cell lysates, consistent with aberrant folding and aggregation. Mutation causes lipodystrophy in heterozygous status
K238R/K239R/Y240F
-
increased resistance to calpain cleavage, resistance to enzyme degradation by oxidized low density lipoprotein
Q243A
-
the mutation results in loss of calmodulin binding and leads to complete calpain resistance in vitro and in vivo
H630N
mutation diminishes the catalytic rate constant of the enzyme
H89A
H89G
H89N
H89Q
H92A
H92G
H92N
H92Q
K122A
R196K
-
decreased Vmax, 5fold increased Km for phosphorylcholine, 23fold increased Km for CTP
additional information
additional information
-
mutants truncated after amino acids 225 or 245 are active in the absence of lipids and not further activated in the presence of lipids, mutants truncated after amino acids 226, 281 or 319 are activated by lipid similar to wild-type enzyme
additional information
-
creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Caenorhabditis elegans, the tail domain of the invertebrate CCT is competent for both suppression of catalytic activity and for activation by lipid vesicles
additional information
-
creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Drosophila melanogaster, the tail domain of the invertebrate CCT is competent for both suppression of catalytic activity and for activation by lipid vesicles
additional information
-
deletion of CCTalpha beginning at embryonic day 7.5 does not restrict lung development but results in severe respiratory failure at birth
additional information
loss of the CCTbeta2 isoform expression in mice results in gonadal dysfunction
additional information
loss of the CCTbeta2 isoform expression in mice results in gonadal dysfunction
additional information
-
deletion of 55 C-terminal amino acids has no effect on enzyme activity, deletion of 139 C-terminal amino acids results in 90% decrease of enzyme activity
additional information
-
deletion mutant lacking the putative membrane binding domain
additional information
-
DELTA delta257-367 exhibits significantly lower specific activity and can not be activated by lipid, deletion mutant DELTA231-367 can not be activated by lipid
additional information
-
deletion mutant which is truncated after residue 236, called CCTalpha236, independent of lipids, 50fold increase in activity
additional information
deletion construct 1-236 (lacks the regulatory domain, displays constitutive activity)
additional information
-
creation of chimeric enzymes by fusing the catalytic domain of rat CCTalpha to the regulatory tail of CCTs from Drosophila melanogaster, Caenorhabditis elegans, or Saccharomyces cerevisiae or to alpha-synuclein. Deletion of the a highly amphipathic 22-residue segment in the membrane-inducible amphipathic helix increased the lipid-independent Vmax by 10fold, equivalent to the effect of deleting the entire tail, and severely weakened membrane binding affinity, but membrane binding is required for additional increases in catalytic efficiency. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan
additional information
-
construction of a truncated version of rat CCTalpha, CCTalpha236. The full length CCT requires activation via association with lipids and has been reported to have activity 50fold lower in the absence of lipids when compared to the activity of CCTalpha236
additional information
-
creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Saccharomyces cerevisiae
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54.5
Tm-value for wild-type enzyme isolated from the particulate fraction after denaturation and renaturation
55
Tm-value for wild-type enzyme purified in native form from the soluble fraction of COS cells
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
instability of the highly purified enzyme is partially overcome by addition of 1 mM DTT and 1% bovine serum albumin or 0.5 mM CTP and 2.5 mM magnesium acetate
-
purified enzyme is unstable in presence of DTT. CTP-Mg2+ or bovine serum albumin do not significantly stabilize the enzyme
-
removal of detergents leads to rapid loss of activity and self-aggregation, high tendency to bind to glass and plastic surfaces even in the presence of detergents
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme concentrated to a small volume, 50% glycerol, 20% loss of activity after 2 weeks
-
-70°C, 50 mM Tris-HCl, 150 mM NaCl, 1.0 mM EDTA, 2.0 mM DTT, 0.025% NaN3, pH 7.4, 0.03% Triton X-100, 200 mM phosphate, stable for several months
-
4°C, increase of activity in fresh cytosol obtained by storage is due to an increase of lysophosphatidylethanolamine and a decrease in phosphatidylethanolamine
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, 2 forms: L-form and H-form, L-form: major species in fresh cytosol, H-form: consists of multiple copies of L-form
-
homogeneity
Ni-NTA column chromatography
recombinant truncated enzyme mutant CCTalpha236 by CM-sepharose chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
deletion construct 1-236: expressed in T.ni cell using a baculovirus expression system, expressed in Escherichia coli BL21
expressed as native and His-tag fusion protein in Sf9 insect cells, native protein expressed in Escherichia coli but expressed protein was found to be misfolded
-
expressed in Escherichia coli Rosetta cells and expressed by baculovirus infection of Trichoplusia ni cells
-
expression in COS-1 cells, which have very low endogenous CTP:phosphocholine cytidylyltransferase activity
full length enzyme and various truncated enzymes expressed in transgenic mice
-
heterologous expression of CTP:phosphocholine cytidylyltransferase from Plasmodium falciparum rescues Chinese Hamster Ovary cells deficient in the Kennedy phosphatidylcholine biosynthesis pathway
His-tagged version expressed in Sf9 cell using a baculovirus exression system
native and mutant enzyme expressed as His-tag fusion proteins in COS-1 cells
-
overexpression of the CTP:phosphocholine cytidylyltransferase (AtCCT1) catalytic domain in Nicotiana benthamiana leaves increased phosphatidylcholine content, and sucrose nonfermenting 1-related protein kinase 1 (SnRK1) co-expression reduces this effect
wild-type and deletion mutants delta312-367, delta231-367 and delta257-367
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CCTbeta expression decreases in the Purkinje cells of the cerebellum following cocaine exposure
CpCCT1 expression increased during mannitol and sorbitol treatments in a concentration dependent manner. Phytohormones such as abscisic acid and indole-3-acetic acid trigg transcript accumulation
-
in cultured primary neurons nerve growth factor increases the amount of isozyme CTbeta2, but not CTalpha, mRNA and protein
in plants exposed to low temperature in the dark, the CpCCT1 transcript increases after 4 h at 4°C
-
the enzyme is induced by dehydration and in response to 0.5 M NaCl solutions
-
in cultured primary neurons nerve growth factor increases the amount of isozyme CTbeta2, but not CTalpha, mRNA and protein
-
in cultured primary neurons nerve growth factor increases the amount of isozyme CTbeta2, but not CTalpha, mRNA and protein
-
in cultured primary neurons nerve growth factor increases the amount of isozyme CTbeta2, but not CTalpha, mRNA and protein
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
CTP:phosphocholine cytidylyltransferase enzyme assay that employs separation of non-radioactive CDP-choline from CTP. The assay was tested using a truncated version of rat CCTalpha by measuring CDP-choline product formation, and the HPLC method can be applied to glycerol 3-phosphate cytidylyltransferase and CTP:2-C-methyl-D-erythritol-4-phosphate cytidylyltransferase synthetase (CMS), members of the cytidylyltransferase family that produce CDP-glycerol and CDP-methylerythritol, respectively
diagnostics
CCT-alpha status is not predictive of outcome of neoadjuvant cisplatin-based chemotherapy response in patients with T2-T4 bladder cancer. In the control group with cystectomy only it has prognostic value
medicine
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weinhold, P.A.; Feldman, D.A.
Choline-phosphate cytidylyltransferase
Methods Enzymol.
209
248-258
1992
Rattus norvegicus
brenda
Vance, D.E.; Pelech, S.D.; Choy, P.C.
CTP:phosphocholine cytidylyltransferase from rat liver
Methods Enzymol.
71
576-581
1981
Rattus norvegicus
-
brenda
Price-Jones, M.J.; Harwood, J.L.
Purification and properties of CTP:cholinephosphate cytidylyltransferase from pea (Pisum sativum L.)
Biochem. Soc. Trans.
13
1243-1245
1985
Pisum sativum
-
brenda
Hunt, A.N.; Postle, A.D.
Dye-affinity chromatography of CTP:cholinephosphate cytidylyltransferase
Biochem. Soc. Trans.
14
1279-1281
1986
Homo sapiens
-
brenda
Mages, F.; Rey, C.; Fonlupt, P.; Pacheco, H.
Kinetic and biochemical properties of CTP:choline-phosphate cytidylyltransferase from the rat brain
Eur. J. Biochem.
178
367-372
1988
Rattus norvegicus
brenda
Weinhold, P.A.; Rounsifer, M.E.; Feldman, D.A.
The purification and characterization of CTP:phosphorylcholine cytidylyltransferase from rat liver
J. Biol. Chem.
261
5104-5110
1986
Rattus norvegicus
brenda
Feldman, D.A.; Weinhold, P.A.
CTP:phosphorylcholine cytidylyltransferase from rat liver. Isolation and characterization of the catalytic subunit
J. Biol. Chem.
262
9075-9081
1987
Rattus norvegicus
brenda
Cornell, R.
Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
264
9077-9082
1989
Rattus norvegicus
brenda
Choy, P.C.; Lim, P.H.; Vance, D.E.
Purification and characterization of CTP: cholinephosphate cytidylytransferase from rat liver cytosol
J. Biol. Chem.
252
7673-7677
1977
Rattus norvegicus
brenda
Choy, P.C.; Vance, D.E.
Lipid requirements for activation of CTP:phosphocholine cytidylyltransferase from rat liver
J. Biol. Chem.
253
5163-5167
1978
Rattus norvegicus
brenda
Wang, X.; Moore, T.S.
Partial purification and characterization of CTP:cholinephosphate cytidylyltransferase from castor bean endosperm
Arch. Biochem. Biophys.
274
338-347
1989
Ricinus communis
brenda
Choy, P.C.; Vance, D.E.
Purification of cholinephosphate cytidylyltransferase from rat liver by affinity chromatography
Biochem. Biophys. Res. Commun.
72
714-719
1976
Rattus norvegicus
brenda
Wang, X.; Moore, T.S.
Phosphatidylylcholine biosynthesis in castor bean endosperm. Purification and properties of cytidine 5'-triphosphate:choline-phosphate cytidylyltransferase
Plant Physiol.
93
250-255
1990
Ricinus communis
brenda
Weinhold, P.A.; Rounsifer, M.E.; Charles, L.; Feldman, D.A.
Characterization of cytosolic forms of CTP:choline-phosphate cytidylyltransferase in lung, isolated alveolar type II cells, A549 cell and Hep G2 cells
Biochim. Biophys. Acta
1006
299-310
1989
Homo sapiens, Rattus norvegicus
brenda
Sohal, P.S.; Cornell, R.B.
Sphingosine inhibits the activity of rat liver CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
265
11746-11750
1990
Rattus norvegicus
brenda
Johnson, J.E.; Kalmar, G.B.; Sohal, P.S.; Walkey, C.J.; Yamashita, S.; Cornell, R.B.
Comparison of the lipid regulation of yeast and rat CTP:phosphocholine cytidylyltransferase expressed in COS cells
Biochem. J.
285
815-820
1992
Rattus norvegicus, Saccharomyces cerevisiae
-
brenda
Feldman, D.A.; Rounsifer, M.E.; Charles, L.; Weinhold, P.A.
CTP:phosphocholine cytidylyltransferase in rat lung: relationship between cytosolic and membrane forms
Biochim. Biophys. Acta
1045
49-57
1990
Rattus norvegicus
brenda
Weinhold, P.A.; Charles, L.G.; Feldman, D.A.
Microsomal CTP:choline phosphate cytidylyltransferase: kinetic mechanism of fatty acid stimulation
Biochim. Biophys. Acta
1086
57-62
1991
Rattus norvegicus
brenda
Jamil, H.; Vance, D.E.
Substrate specificity of CTP:phosphocholine cytidylyltransferase
Biochim. BIophys. Acta
1086
335-339
1991
Rattus norvegicus
brenda
Pelech, S.L.; Jetha, F.; Vance, D.E.
Trifluoperazine and other anaesthetics inhibit rat liver CTP: phosphocholine cytidylyltransferase
FEBS Lett.
158
89-92
1983
Rattus norvegicus
brenda
Mansbach II, C.M.; Arnold, A.
CTP:phosphocholine cytidylyltransferase in intestinal mucosa
Biochim. Biophys. Acta
875
516-524
1986
Rattus norvegicus
brenda
Awasthi, S.; Vivekananda, J.; Awasthi, V.; Smith, D.; King, R.J.
CTP:phosphocholine cytidylyltransferase inhibition by ceramide via PKC-a, p38 MAPK, cPLA2, and 5-lipoxygenase
Am. J. Physiol.
281
L108-L118
2001
Homo sapiens
brenda
Boggs, K.P.; Rock, C.O.; Jackowski, S.
Lysophosphatidylcholine and 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine inhibit the CDP-choline pathway of phosphatidylcholine synthesis at the CTP:phosphocholine cytidylyltransferase step
J. Biol. Chem.
270
7757-7764
1995
Mus musculus
brenda
Campbell, H.A.; Kent, C.
The CTP:phosphocholine cytidylyltransferase encoded by the licC gene of Streptococcus pneumoniae: cloning, expression, purification, and characterization
Biochim. Biophys. Acta
1534
85-95
2001
Streptococcus pneumoniae (Q93MI4), Streptococcus pneumoniae
brenda
Carter, J.M.; Waite, K.A.; Campenot, R.B.; Vance, J.E.; Vance, D.E.
Enhanced expression and activation of CTP:phosphocholine cytidylyltransferase b2 during neurite outgrowth
J. Biol. Chem.
278
44988-44994
2003
Rattus norvegicus
brenda
Cornell, R.B.; Kalmar, G.B.; Kay, R.J.; Johnson, M.A.; Sanghera, J.S.; Pelech, S.L.
Functions of the C-terminal domain of CTP:phosphocholine cytidylyltransferase. Effects of C-terminal deletions on enzyme activity, intracellular localization and phosphorylation potential
Biochem. J.
310
699-708
1995
Rattus norvegicus
-
brenda
Drobnies, A.E.; Van der Ende, B.; Thewalt, J.L.; Cornell, R.B.
CTP:phosphocholine cytidylyltransferase activation by oxidized phosphatidylcholines correlates with a decrease in lipid prder: A 2H NMR analysis
Biochemistry
38
15606-15614
1999
Rattus norvegicus
brenda
Friesen, J.A.; Campbell, H.A.; Kent, C.
Enzymic and cellular characterization of a catalytic fragment of CTP:phosphocholine cytidylyltransferase a
J. Biol. Chem.
274
13384-13389
1999
Rattus norvegicus
brenda
Friesen, J.A.; Liu, M.F.; Kent, C.
Cloning and characterization of a lipid-activated CTP:phosphocholine cytidylyltransferase from Caenorhabditis elegans: identification of a 21-residue segment critical for lipid activation
Biochim. Biophys. Acta
1533
86-98
2001
Caenorhabditis elegans
brenda
Friesen, J.A.; Seo Park, Y.; Kent, C.
Purification and kinetic characterization of CTP:phosphocholine cytidylyltransferase from Saccharomyces cerevisiae
Protein Expr. Purif.
21
141-148
2001
Saccharomyces cerevisiae
brenda
Helmink, B.A.; Braker, J.D.; Kent, C.; Friesen, J.A.
Identification of lysine 122 and arginine 196 as important functional residues of rat CTP:phosphocholine cytidylyltransferase a
Biochemistry
42
5043-5051
2003
Rattus norvegicus
brenda
Lykidis, A.; Baburina, I.; Jackowski, S.
Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTb splice variant
J. Biol. Chem.
274
26992-27001
1999
Homo sapiens
brenda
Ridsdale, R.; Tseu, I.; Wang, J.; Post, M.
CTP:phosphocholine cytidylyltransferase a is a cytosolic protein in pulmonary epithelial cells and tissues
J. Biol. Chem.
276
49148-49155
2001
Mus musculus, Rattus norvegicus
brenda
Rock, C.O.; Heath, R.J.; Park, H.W.; Jackowski, S.
The licC gene of Streptococcus pneumoniae encodes a CTP:phosphocholine cytidylyltransferase
J. Bacteriol.
183
4927-4931
2001
Streptococcus pneumoniae
brenda
Taneva, S.; Johnson, J.E.; Cornell, R.B.
Lipid-induced conformational switch in the membrane binding domain of CTP:phosphocholine cytidylyltransferase: A circular dichroism study
Biochemistry
42
11768-11776
2003
Rattus norvegicus
brenda
Veitch, D.P.; Gilham, D.; Cornell, R.B.
The role of histidine residues in the HXGH site of CTP:phosphocholine cytidylyltransferase in CTP binding and catalysis
Eur. J. Biochem.
255
227-234
1998
Rattus norvegicus
brenda
Whiting, G.C.; Gillespie, S.H.
Investigation of a choline phosphate synthesis pathway in Streptococcus pneumoniae: evidence for choline phosphate cytidylyltransferase activity
FEMS Microbiol. Lett.
143
279-284
1996
Streptococcus pneumoniae, Streptococcus pneumoniae R36A
brenda
Yang, W.; Boggs, K.P.; Jackowski, S.
The association of lipid activators with the amphipathic helical domain of CTP:phosphocholine cytidylyltransferase accelerates catalysis by increasing the affinity of the enzyme for CTP
J. Biol. Chem.
270
23951-23957
1995
Rattus norvegicus
brenda
Yeo, H.J.; Larvor, M.P.; Ancelin, M.L.; Vial, H.J.
Plasmodium falciparum CTP:phosphocholine cytidylyltransferase expressed in Escherichia coli: purification, characterization and lipid regulation
Biochem. J.
324
903-910
1997
Plasmodium falciparum
-
brenda
Zhou, J.; Ryan, A.J.; Medh, J.; Mallampalli, R.K.
Oxidized lipoproteins inhibit surfactant phosphatidylcholine synthesis via calpain-mediated Cleavage of CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
278
37032-37040
2003
Mus musculus, Rattus norvegicus
brenda
MacDonald, J.I.S.; Kent, C.
Identification of phosphorylation sites in rat liver CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
269
10529-10537
1994
Rattus norvegicus
brenda
Ryan, A.J.; Fisher, K.; Thomas, C.P.; Mallampalli, R.K.
Transcriptional repression of the CTP:phosphocholine cytidylyltransferase gene by sphingosine
Biochem. J.
382
741-750
2004
Mus musculus, Rattus norvegicus
brenda
Taneva, S.G.; Patty, P.J.; Frisken, B.J.; Cornell, R.B.
CTP:phosphocholine cytidylyltransferase binds anionic phospholipid vesicles in a cross-bridging mode
Biochemistry
44
9382-9393
2005
Rattus norvegicus
brenda
Helmink, B.A.; Friesen, J.A.
Characterization of a lipid activated CTP:phosphocholine cytidylyltransferase from Drosophila melanogaster
Biochim. Biophys. Acta
1683
78-88
2004
Drosophila melanogaster
brenda
Xie, M.; Smith, J.L.; Ding, Z.; Zhang, D.; Cornell, R.B.
Membrane binding modulates the quaternary structure of CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
279
28817-28825
2004
Rattus norvegicus
brenda
Ridsdale, R.; Tseu, I.; Roth-Kleiner, M.; Wang, J.; Post, M.
Increased phosphatidylcholine production but disrupted glycogen metabolism in fetal type II cells of mice that overexpress CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
279
55946-55957
2004
Mus musculus, Rattus norvegicus
brenda
Bogan, M.J.; Agnes, G.R.; Pio, F.; Cornell, R.B.
Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry
J. Biol. Chem.
280
19613-19624
2005
Rattus norvegicus
brenda
Jackowski, S.; Fagone, P.
CTP:phosphocholine cytidylyltransferase: Paving the way from gene to membrane
J. Biol. Chem.
280
853-856
2005
Arabidopsis thaliana, Homo sapiens, Mus musculus
brenda
Adibhatla, R.M.; Hatcher, J.F.; Dempsey, R.J.
Cytidine-5'-diphosphocholine affects CTP-phosphocholine cytidylyltransferase and lyso-phosphatidylcholine after transient brain ischemia
J. Neurosci. Res.
76
390-396
2004
Meriones unguiculatus
brenda
Hastings, C.; Rand, T.; Bergen, H.T.; Thliveris, J.A.; Shaw, A.R.; Lombaert, G.A.; Mantsch, H.H.; Giles, B.L.; Dakshinamurti, S.; Scott, J.E.
Stachybotrys chartarum alters surfactant-related phospholipid synthesis and CTP:cholinephosphate cytidylyltransferase activity in isolated fetal rat type II cells
Toxicol. Sci.
84
186-194
2005
Rattus norvegicus
brenda
Tilley, D.M.; Evans, C.R.; Larson, T.M.; Edwards, K.A.; Friesen, J.A.
Identification and characterization of the nuclear isoform of Drosophila melanogaster CTP:phosphocholine cytidylyltransferase
Biochemistry
47
11838-11846
2008
Drosophila melanogaster (Q7K4C7), Drosophila melanogaster (Q9W0D9), Drosophila melanogaster
brenda
Gunter, C.; Frank, M.; Tian, Y.; Murti, K.G.; Rehg, J.E.; Jackowski, S.
Probucol therapy overcomes the reproductive defect in CTP: phosphocholine cytidylyltransferase beta2 knockout mice
Biochim. Biophys. Acta
1771
845-852
2007
Mus musculus (P49586), Mus musculus (Q811Q9)
brenda
Marcucci, H.; Elena, C.; Gilardoni, P.; Banchio, C.
Characterization of the murine CTP:phosphocholine cytidylyltransferase beta gene promoter
Biochim. Biophys. Acta
1781
254-262
2008
Mus musculus
brenda
Kacher, Y.; Golan, A.; Pewzner-Jung, Y.; Futerman, A.H.
Changes in macrophage morphology in a Gaucher disease model are dependent on CTP:phosphocholine cytidylyltransferase alpha
Blood Cells Mol. Dis.
39
124-129
2007
Homo sapiens, Mus musculus
brenda
Banchio, C.; Lingrell, S.; Vance, D.E.
Sp-1 binds promoter elements that are regulated by retinoblastoma and regulate CTP:phosphocholine cytidylyltransferase-alpha transcription
J. Biol. Chem.
282
14827-14835
2007
Mus musculus
brenda
Chen, B.B.; Mallampalli, R.K.
Calmodulin binds and stabilizes the regulatory enzyme, CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
282
33494-33506
2007
Mus musculus
brenda
Carter, J.M.; Demizieux, L.; Campenot, R.B.; Vance, D.E.; Vance, J.E.
Phosphatidylcholine biosynthesis via CTP:phosphocholine cytidylyltransferase beta2 facilitates neurite outgrowth and branching
J. Biol. Chem.
283
202-212
2008
Rattus norvegicus
brenda
Jacobs, R.L.; Lingrell, S.; Zhao, Y.; Francis, G.A.; Vance, D.E.
Hepatic CTP:phosphocholine cytidylyltransferase-alpha is a critical predictor of plasma high density lipoprotein and very low density lipoprotein
J. Biol. Chem.
283
2147-2155
2008
Mus musculus
brenda
Taneva, S.; Dennis, M.K.; Ding, Z.; Smith, J.L.; Cornell, R.B.
Contribution of each membrane binding domain of the CTP:phosphocholine cytidylyltransferase-alpha dimer to its activation, membrane Binding, and membrane cross-bridging
J. Biol. Chem.
283
28137-28148
2008
Rattus norvegicus
brenda
Gehrig, K.; Cornell, R.B.; Ridgway, N.D.
Expansion of the nucleoplasmic reticulum requires the coordinated activity of lamins and CTP:phosphocholine cytidylyltransferase alpha
Mol. Biol. Cell
19
237-247
2008
Homo sapiens
brenda
Tian, Y.; Zhou, R.; Rehg, J.E.; Jackowski, S.
Role of phosphocholine cytidylyltransferase alpha in lung development
Mol. Cell. Biol.
27
975-982
2007
Mus musculus
brenda
Ridsdale, R.; Tseu, I.; Wang, J.; Post, M.
Functions of membrane binding domain of CTP:phosphocholine cytidylyltransferase in alveolar type II cells
Am. J. Respir. Cell Mol. Biol.
43
74-87
2009
Rattus norvegicus
brenda
Braker, J.D.; Hodel, K.J.; Mullins, D.R.; Friesen, J.A.
Identification of hydrophobic amino acids required for lipid activation of C. elegans CTP:phosphocholine cytidylyltransferase
Arch. Biochem. Biophys.
492
10-16
2009
Caenorhabditis elegans (Q3HKC4), Caenorhabditis elegans
brenda
Gehrig, K.; Lagace, T.A.; Ridgway, N.D.
Oxysterol activation of phosphatidylcholine synthesis involves CTP:phosphocholine cytidylyltransferase alpha translocation to the nuclear envelope
Biochem. J.
418
209-217
2009
Cricetulus griseus
brenda
Okamura, K.; Yamashita, S.; Ando, H.; Horibata, Y.; Aoyama, C.; Takagishi, K.; Izumi, T.; Vance, D.E.; Sugimoto, H.
Identification of nuclear localization and nuclear export signals in Ets2, and the transcriptional regulation of Ets2 and CTP:phosphocholine cytidylyltransferase alpha in tetradecanoyl-13-acetate or macrophage-colony stimulating factor stimulated RAW264 cells
Biochim. Biophys. Acta
1791
173-182
2009
Mus musculus
brenda
Lee, J.; Johnson, J.; Ding, Z.; Paetzel, M.; Cornell, R.B.
Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold
J. Biol. Chem.
284
33535-33548
2009
Rattus norvegicus (P19836)
brenda
Fagone, P.; Gunter, C.; Sage, C.R.; Gunn, K.E.; Brewer, J.W.; Jackowski, S.
CTP:phosphocholine cytidylyltransferase alpha is required for B-cell proliferation and class switch recombination
J. Biol. Chem.
284
6847-6854
2009
Mus musculus
brenda
Inatsugi, R.; Kawai, H.; Yamaoka, Y.; Yu, Y.; Sekiguchi, A.; Nakamura, M.; Nishida, I.
Isozyme-specific modes of activation of CTP:phosphorylcholine cytidylyltransferase in Arabidopsis thaliana at low temperature
Plant Cell Physiol.
50
1727-1735
2009
Arabidopsis thaliana
brenda
Gehrig, K.; Ridgway, N.
CTP:phosphocholine cytidylyltransferase alpha (CCTalpha) and lamins alter nuclear membrane structure without affecting phosphatidylcholine synthesis
Biochim. Biophys. Acta
1811
377-385
2011
Cricetulus griseus, Homo sapiens
brenda
Strakova, J.; Demizieux, L.; Campenot, R.B.; Vance, D.E.; Vance, J.E.
Involvement of cin axonal phosphatidylcholine synthesis and branching of neurons
Biochim. Biophys. Acta
1811
617-625
2011
Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Krahmer, N.; Guo, Y.; Wilfling, F.; Hilger, M.; Lingrell, S.; Heger, K.; Newman, H.W.; Schmidt-Supprian, M.; Vance, D.E.; Mann, M.; Farese, R.V.; Walther, T.C.
Phosphatidylcholine synthesis for lipid droplet expansion is mediated by localized activation of CTP:phosphocholine cytidylyltransferase
Cell Metab.
14
504-515
2011
Drosophila melanogaster, Mus musculus
brenda
Ding, Z.; Taneva, S.G.; Huang, H.K.; Campbell, S.A.; Semenec, L.; Chen, N.; Cornell, R.B.
A 22-mer segment in the structurally pliable regulatory domain of metazoan CTP:phosphocholine cytidylyltransferase facilitates both silencing and activating functions
J. Biol. Chem.
287
38980-38991
2012
Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Rattus norvegicus
brenda
Goulbourne, C.N.; Malhas, A.N.; Vaux, D.J.
The induction of a nucleoplasmic reticulum by prelamin A accumulation requires CTP:phosphocholine cytidylyltransferase-alpha
J. Cell Sci.
124
4253-4266
2011
Homo sapiens
brenda
Brault, J.P.; Friesen, J.A.
Characterization of cytidylyltransferase enzyme activity through high performance liquid chromatography
Anal. Biochem.
510
26-32
2016
Rattus norvegicus
brenda
Ramezanpour, M.; Lee, J.; Taneva, S.G.; Tieleman, D.P.; Cornell, R.B.
An auto-inhibitory helix in CTP phosphocholine cytidylyltransferase hijacks the catalytic residue and constrains a pliable, domain-bridging helix pair
J. Biol. Chem.
293
7070-7084
2018
Rattus norvegicus (P19836)
brenda
Cornell, R.B.; Taneva, S.G.; Dennis, M.K.; Tse, R.; Dhillon, R.K.; Lee, J.
Disease-linked mutations in the phosphatidylcholine regulatory enzyme CCTalpha impair enzymatic activity and fold stability
J. Biol. Chem.
294
1490-1501
2019
Homo sapiens (P49585), Homo sapiens
brenda
Caldo, K.M.P.; Xu, Y.; Falarz, L.; Jayawardhane, K.; Acedo, J.Z.; Chen, G.
Arabidopsis CTP phosphocholine cytidylyltransferase 1 is phosphorylated and inhibited by sucrose nonfermenting 1-related protein kinase 1 (SnRK1)
J. Biol. Chem.
294
15862-15874
2019
Arabidopsis thaliana (Q9ZV56)
brenda
Pati, S.; Ingram, L.M.; Sun, M.K.; Wagner, J.J.; Cummings, B.S.
Localization and expression of CTP phosphocholine cytidylyltransferase in rat brain following cocaine exposure
J. Chem. Neuroanat.
96
1-6
2019
Rattus norvegicus (Q9QZC4)
brenda
Yue, L.; McPhee, M.J.; Gonzalez, K.; Charman, M.; Lee, J.; Thompson, J.; Winkler, D.F.H.; Cornell, R.B.; Pelech, S.; Ridgway, N.D.
Differential dephosphorylation of CTP phosphocholine cytidylyltransferase upon translocation to nuclear membranes and lipid droplets
Mol. Biol. Cell
31
1047-1059
2020
Homo sapiens (P49585)
brenda
Ogasawara, Y.; Cheng, J.; Tatematsu, T.; Uchida, M.; Murase, O.; Yoshikawa, S.; Ohsaki, Y.; Fujimoto, T.
Long-term autophagy is sustained by activation of CCTbeta3 on lipid droplets
Nat. Commun.
11
4480
2020
Mus musculus
brenda
Liu, X.; Giarola, V.; Quan, W.; Song, X.; Bartels, D.
Identification and characterization of CTP phosphocholine cytidylyltransferase CpCCT1 in the resurrection plant Craterostigma plantagineum
Plant Sci.
302
110698
2021
Craterostigma plantagineum
brenda
Hemdan, T.; Turker, P.; Malmstroem, P.U.; Segersten, U.
Choline-phosphate cytidylyltransferase-alpha as a possible predictor of survival and response to cisplatin neoadjuvant chemotherapy in urothelial cancer of the bladder
Scand. J. Urol.
52
200-205
2018
Homo sapiens (P49585)
brenda
Izrael, R.; Marton, L.; Nagy, G.N.; Palinkas, H.L.; Kucsma, N.; Vertessy, B.G.
Identification of a nuclear localization signal in the Plasmodium falciparum CTP phosphocholine cytidylyltransferase enzyme
Sci. Rep.
10
19739
2020
Plasmodium falciparum (P49587), Plasmodium falciparum
brenda
Marton, L.; Hajdu, F.; Nagy, G.N.; Kucsma, N.; Szakacs, G.; Vertessy, B.G.
Heterologous expression of CTP phosphocholine cytidylyltransferase from Plasmodium falciparum rescues Chinese Hamster Ovary cells deficient in the Kennedy phosphatidylcholine biosynthesis pathway
Sci. Rep.
8
8932
2018
Plasmodium falciparum (Q8IEE9), Plasmodium falciparum
brenda
Moitra, S.; Pawlowic, M.C.; Hsu, F.F.; Zhang, K.
Phosphatidylcholine synthesis through cholinephosphate cytidylyltransferase is dispensable in Leishmania major
Sci. Rep.
9
7602
2019
Leishmania major (Q4QDQ6), Leishmania major
brenda
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