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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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This record set is specific for:
Rattus norvegicus
UNIPROT: P19836 not found.
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Rattus norvegicus
Synonyms
CCT, CCT-alpha, CCT1, CCT2, CCTalpha, CCTalpha236, CCTbeta2, CCTbeta3, CDP-choline pyrophosphorylase, CDP-choline synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CCTalpha236
248
-
CDP-choline pyrophosphorylase
-
-
-
-
CDP-choline synthetase
-
-
-
-
choline phosphate cytidylyltransferase
CTbeta2
248
-
CTP-phosphocholine cytidylyltransferase
-
-
-
-
CTP:cholinephosphate cytidylyltransferase
-
-
-
-
CTP:phosphocholine cytidylyltransferase
CTP:phosphocholine cytidylyltransferase alpha-isoform
248
-
CTP:phosphocholine cytidylyltransferase beta2
248
-
CTP:phosphocholine cytidylyltransferase-alpha
248
-
CTP:phosphocholine cytidylyltransferase-beta2
248
-
CTP:phosphorylcholine cytidylyltransferase
-
-
-
-
cytidine diphosphocholine pyrophosphorylase
-
-
-
-
cytidylyltransferase
248
-
cytidylyltransferase, choline phosphate
-
-
-
-
phosphocholine cytidylyltransferase
-
-
-
-
phosphorylcholine cytidylyltransferase
-
-
-
-
phosphorylcholine transferase
-
-
-
-
phosphorylcholine:CTP cytidylyltransferase
-
-
-
-
additional information
248
four isoforms, CCTalpha ubiquitously expressed, whereas CCTbeta 1,-2, and -3 restricted in distribution
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + phosphocholine = diphosphate + CDP-choline
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:choline-phosphate cytidylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-34-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + choline phosphate
diphosphate + CDP-choline
show the reaction diagram
-
-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
show the reaction diagram
CTP + choline phosphate
diphosphate + CDPcholine
show the reaction diagram
CTP + ethanolamine phosphate
diphosphate + CDPethanolamine
show the reaction diagram
-
-
-
-
?
CTP + phosphocholine
diphosphate + CDP-choline
show the reaction diagram
-
-
-
-
?
CTP + phosphodimethylethanolamine
diphosphate + CDPdimethylethanolamine
show the reaction diagram
-
-
-
-
?
CTP + phosphomonomethylethanolamine
diphosphate + CDPmethylethanolamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CTP + choline phosphate
diphosphate + CDP-choline
show the reaction diagram
-
rate limiting enzyme for the synthesis of phosphatidylcholine
-
-
?
CTP + choline phosphate
diphosphate + CDPcholine
show the reaction diagram
CTP + phosphocholine
diphosphate + CDP-choline
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
2-20 mM; required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
4-chloromercuribenzoate
5,5'-dithiobis(2-nitrobenzoate)
-
-
CDPcholine
-
competitive to choline phosphate
ceramide
-
-
chlorpromazine
Dibucaine
-
28% inhibition at 0.05 mM
lysophosphatidylcholine
Lysosphingolipids
-
reversible
-
N-ethylmaleimide
oxidized low density lipoprotein
-
-
-
phosphate
-
maximal inhibition of 60% at 120 mM
phosphodimethylethanolamine
-
competitive to phosphocholine
Phosphoethanolamine
-
competitive to phosphocholine
phosphomonomethylethanolamine
-
competitive to phosphocholine
propanolol
-
28% inhibition at 0.05 mM
Sn-3-Lysophosphatidylcholine
-
-
-
Sphingolipids
-
reversed by activating phospholipids
-
sphingomyelin
-
causes inhibition when present in multilamellar vesicles
sphingosine
Tetracaine
-
50% inhibition at 0.05 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
Triton X-100
-
-
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
20 mM
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
glucosylceramide
-
-
Lipids
-
phosphatidylglycerol
-
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 3.2
choline phosphate
7.3 - 8.8
CTP
0.21 - 0.64
CDPcholine
0.167 - 0.52
choline phosphate
0.208 - 35.7
CTP
0.004 - 0.007
diphosphate
0.17 - 212
phosphocholine
4
phosphodimethylethanolamine
-
pH 7, 37°C
69.4
Phosphoethanolamine
-
pH 7, 37°C
6.9
phosphomonomethylethanolamine
-
pH 7, 37°C
0.14 - 0.22
phosphorylcholine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33.3
CTP
-
with choline phosphate, 45000 MW protein
0.21 - 17.7
phosphocholine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
CDPcholine
-
pH 7.4, 37°C
1
phosphodimethylethanolamine
-
pH 7, 37°C
16.7
Phosphoethanolamine
-
pH 7, 37°C
7.8
phosphomonomethylethanolamine
-
pH 7, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
0.00296
-
L-form
0.025
-
H-form
0.35
-
with phosphoethanolamine as substrate
3.45
-
with phosphomonomethylethanolamine as substrate
3.85
-
truncated enzyme mutant CCTalpha236, pH 7.0,37°C
10.7
-
with phosphocholine as substrate
16.12
-
with phosphodimethylethanolamine as substrate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
pH 6: about 80% of activity maximum, pH 8: about 60% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
superior cervical ganglia
Manually annotated by BRENDA team
-
contains only L-form
Manually annotated by BRENDA team
-
phaeochromocytoma cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PCY1A_RAT
367
0
41681
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
x * 45000, catalytic subunit + x * 38000, functional role of this subunit not documented, SDS-PAGE
39000
-
2 * 39000 + 2 * 48000, SDS-PAGE
41700
-
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
44500
-
2 * 44500, SDS-PAGE
45000
48000
-
2 * 39000 + 2 * 48000, SDS-PAGE
50300
-
gel filtration
80000 - 110000
-
diffuse band in SDS-PAGE using chemically cross-linked protein
97000
-
gel filtration, glycerol density gradient centrifugation
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
840000
-
native PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
deletion construct 1-236, crystall structure analysis
?
-
x * 45000, catalytic subunit + x * 38000, functional role of this subunit not documented, SDS-PAGE
dimer
homodimer
tetramer
-
2 * 39000 + 2 * 48000, SDS-PAGE
additional information
-
the enzyme is composed of a catalytic head domain and a regulatory tail
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
phosphoprotein
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor-diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H168A
involved in catalysis
H168A/Y173A
involved in catalysis
Y173A
involved in catalysis
C113S
-
no significant effect of activity
C139S
-
no significant effect of activity
C354S
-
no significant effect of activity
C359S
-
no significant effect of activity
C37S
-
unable to form dimers
C68S
-
no significant effect of activity
C73S
-
no significant effect of activity
I272R
-
part of the M-domain
I275R
-
part of the M-domain
K122A
K122R
-
decreased Vmax
L274R
-
part of the M-domain
R196K
-
decreased Vmax, 5fold increased Km for phosphorylcholine, 23fold increased Km for CTP
V267R
-
part of the M-domain
V267R/I272R
-
part of the M-domain
V267R/I272R/L274R
-
part of the M-domain
V267R/I272R/L274R/I275R
-
part of the M-domain
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing once causes more than 90% loss of activity
-
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
-
-70°C, stable in presence of Triton X-100 and 0.2 M potassium phosphate
-
0°C, 80% loss of activity after 6 days
-
4°C, 20% loss of activity per day
-
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
CM- and Blue-Sepharose chromatography, gel filtartion
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
-
deletion mutant which is truncated after residue 236, called CCTalpha236
-
Ni-NTA column chromatography
-
rapid purification method, 687fold purification
-
recombinant enzymes using His-tag
-
recombinant protein
-
recombinant truncated enzyme mutant CCTalpha236 by CM-sepharose chromatography
-
wild-type and truncated form
-
wild-type enzyme and peptides after trypsin digestion
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
deletion construct 1-236: expressed in T.ni cell using a baculovirus expression system, expressed in Escherichia coli BL21
deletion mutant which is truncated after residue 236, called CCTalpha236
-
expressed in A-549 cell
-
expressed in A-549 cells
-
expressed in Escherichia coli Rosetta cells and expressed by baculovirus infection of Trichoplusia ni cells
-
expressed in High 5 cells
-
expressed in insect cells
-
expressed in PC-12 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
-
wild-type and truncated form
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in cultured primary neurons nerve growth factor increases the amount of isozyme CTbeta2, but not CTalpha, mRNA and protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
Vance, D.E.; Pelech, S.D.; Choy, P.C.
CTP:phosphocholine cytidylyltransferase from rat liver
Methods Enzymol.
71
576-581
1981
Rattus norvegicus
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Cornell, R.
Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase
J. Biol. Chem.
264
9077-9082
1989
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Jamil, H.; Vance, D.E.
Substrate specificity of CTP:phosphocholine cytidylyltransferase
Biochim. BIophys. Acta
1086
335-339
1991
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Mansbach II, C.M.; Arnold, A.
CTP:phosphocholine cytidylyltransferase in intestinal mucosa
Biochim. Biophys. Acta
875
516-524
1986
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Caenorhabditis elegans, Drosophila melanogaster, Rattus norvegicus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Brault, J.P.; Friesen, J.A.
Characterization of cytidylyltransferase enzyme activity through high performance liquid chromatography
Anal. Biochem.
510
26-32
2016
Rattus norvegicus
Manually annotated by BRENDA team
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