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Information on EC 2.7.7.15 - choline-phosphate cytidylyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P19836
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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 taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CCT
CDP-choline pyrophosphorylase
-
-
-
-
CDP-choline synthetase
-
-
-
-
choline phosphate cytidylyltransferase
CTP-phosphocholine cytidylyltransferase
-
-
-
-
CTP:cholinephosphate cytidylyltransferase
-
-
-
-
CTP:phosphocholine cytidylyltransferase
CTP:phosphorylcholine cytidylyltransferase
-
-
-
-
cytidine diphosphocholine pyrophosphorylase
-
-
-
-
cytidylyltransferase, choline phosphate
-
-
-
-
phosphocholine cytidylyltransferase
-
-
-
-
phosphorylcholine cytidylyltransferase
-
-
-
-
phosphorylcholine transferase
-
-
-
-
phosphorylcholine:CTP cytidylyltransferase
-
-
-
-
additional information
-
four isoforms, CCTalpha ubiquitously expressed, whereas CCTbeta 1,-2, and -3 restricted in distribution
CCT
-
-
-
-
choline phosphate cytidylyltransferase
-
-
-
-
CTP:phosphocholine cytidylyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + phosphocholine = diphosphate + CDP-choline
catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
CTP:choline-phosphate cytidylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9026-34-0
-
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 + phosphomonomethylethanolamine
diphosphate + CDPmethylethanolamine
-
-
-
-
?
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 + choline phosphate
diphosphate + CDP-choline
-
-
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphatidylcholine
-
ET-18-OCH3, non-hydrolyzable lysophosphatidylcholine analog, competitive with respect to the lipid activator
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
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
-
99% inhibition of L-form, only partial inhibition of H-form
additional information
when dissociated from membranes, a portion of the M domain functions as an auto-inhibitory element to suppress catalysis
-
additional information
-
inhibited with spore extract from Stachybotrys chartarum isolated in Cleveland, no effect with extracts from the same organism isolated in Hawaii
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
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
-
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
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
3.399
wild-type deletion construct 1-236, variable CTP concentration, 1.5 mM choline phosphate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
pH 6: about 80% of activity maximum, pH 8: about 60% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
642889, 642890, 642894, 642895, 642896, 642897, 642898, 642900, 642902, 642903, 642907, 642908, 642914, 642916, 642924, 642929, 661213
-
CTbeta2 is abundant in axons of sympathetic neurons and retinal ganglion cells
-
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
642889, 642890, 642893, 642894, 642897, 642900, 642902, 642904, 642905, 642908, 642909, 642913, 642914, 642924, 660981
CCTbeta expression appears to be cytosolic within these Purkinje cells
-
enzyme is activated when bound to vesicles
-
L-form binds to microsomal membrane, is formed in to H-form and H-form is released from membrane
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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 conversion of phosphocholine and CTP to cytidine diphosphocholine (CDP-choline), a step critical for synthesis of the membrane phospholipid phosphatidylcholine
physiological function
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
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
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). PCY1A_RAT
367
0
41681
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
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
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 45000, catalytic subunit + x * 38000, functional role of this subunit not documented, SDS-PAGE
dimer
homodimer
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail
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
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 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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
deletion construct 1-236 (lacks the regulatory domain, displays constitutive activity)
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
-
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
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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
-
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
-
recombinant truncated enzyme mutant CCTalpha236 by CM-sepharose chromatography
-
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 in Escherichia coli Rosetta cells and expressed by baculovirus infection of Trichoplusia ni cells
-
full length enzyme and various truncated enzymes expressed in transgenic mice
-
native and mutant enzyme expressed as His-tag fusion proteins in COS-1 cells
-
wild-type and deletion mutants delta312-367, delta231-367 and delta257-367
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CCTbeta expression decreases in the Purkinje cells of the cerebellum following cocaine exposure
in cultured primary neurons nerve growth factor increases the amount of isozyme CTbeta2, but not CTalpha, mRNA and protein
-
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
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
Vance, D.E.; Pelech, S.D.; Choy, P.C.
CTP:phosphocholine cytidylyltransferase from rat liver
Methods Enzymol.
71
576-581
1981
Rattus norvegicus
-
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
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
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
Cornell, R.
Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
264
9077-9082
1989
Rattus norvegicus
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
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
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
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
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
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
Saccharomyces cerevisiae, Rattus norvegicus
-
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
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
Jamil, H.; Vance, D.E.
Substrate specificity of CTP:phosphocholine cytidylyltransferase
Biochim. BIophys. Acta
1086
335-339
1991
Rattus norvegicus
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
Mansbach II, C.M.; Arnold, A.
CTP:phosphocholine cytidylyltransferase in intestinal mucosa
Biochim. Biophys. Acta
875
516-524
1986
Rattus norvegicus
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
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
-
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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)
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
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
Brault, J.P.; Friesen, J.A.
Characterization of cytidylyltransferase enzyme activity through high performance liquid chromatography
Anal. Biochem.
510
26-32
2016
Rattus norvegicus
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)
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