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Information on EC 2.7.7.15 - choline-phosphate cytidylyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession Q9W0D9

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Drosophila melanogaster
UNIPROT: Q9W0D9 not found.
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The taxonomic range for the selected organisms is: Drosophila melanogaster
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:choline-phosphate cytidylyltransferase, cctbeta2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CTP:phosphocholine cytidylyltransferase
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CDP-choline pyrophosphorylase
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CDP-choline synthetase
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choline phosphate cytidylyltransferase
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CTP-phosphocholine cytidylyltransferase
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CTP:cholinephosphate cytidylyltransferase
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CTP:phosphocholine cytidylyltransferase
CTP:phosphorylcholine cytidylyltransferase
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cytidine diphosphocholine pyrophosphorylase
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cytidylyltransferase, choline phosphate
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phosphocholine cytidylyltransferase
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phosphorylcholine cytidylyltransferase
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phosphorylcholine transferase
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phosphorylcholine:CTP cytidylyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
CTP:choline-phosphate cytidylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-34-0
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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
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-
-
?
CTP + choline phosphate
diphosphate + CDP-choline
show the reaction diagram
CTP + phosphocholine
diphosphate + CDP-choline
show the reaction diagram
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-
-
-
?
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
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rate limiting enzyme for the synthesis of phosphatidylcholine
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-
?
CTP + phosphocholine
diphosphate + CDP-choline
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
Ca2+ yields approximately 9% of the activity seen with Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
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+
the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+
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+
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+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphatidylglycerol
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phosphatidylcholine
6fold enhancement of activity at 0.025 mM
phosphatidylglycerol
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phosphatidylinositol
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diphosphatidylglycerol
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Lipids
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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
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phosphatidylcholine
6fold enhancement of activity at 0.025 mM
phosphatidylglycerol
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phosphatidylinositol
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63
choline phosphate
isozyme CCT2
0.5 - 2.29
choline phosphate
0.72 - 1.21
CTP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
Manually annotated by BRENDA team
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enzyme is activated when bound to vesicles
Manually annotated by BRENDA team
additional information
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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
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme catalyzes a step in the Kennedy pathway for phosphatidylecholine synthesis, overview
physiological function
additional information
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9W0D9_DROME
381
0
43751
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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x * 44000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 44000, SDS-PAGE
additional information
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the enzyme is composed of a catalytic head domain and a regulatory tail
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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phosphorylated on serine and threonine but not on tyrosine residues
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Talon metal affinity column chromatography
native and His-tag protein
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Talon metal affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 cells and Schneider 2 cells
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
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expressed in Sf9 cells and Schneider 2 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
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
Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Rattus norvegicus
Manually annotated by BRENDA team