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Information on EC 2.7.7.15 - choline-phosphate cytidylyltransferase and Organism(s) Caenorhabditis elegans

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This record set is specific for:
Caenorhabditis elegans
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 + CDPcholine
show the reaction diagram
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?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
wild-type protein in the presence of 0.01 mM phosphatidylcholine:oleate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis
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?
PCY1_CAEEL
362
0
41769
Swiss-Prot
other Location (Reliability: 2)
Q3HKC4_CAEEL
354
0
40727
TrEMBL
other Location (Reliability: 2)
Q8IU09_CAEEL
272
0
31157
TrEMBL
other Location (Reliability: 2)
V6CIU7_CAEEL
216
0
24973
TrEMBL
other Location (Reliability: 3)
V6CL91_CAEEL
194
0
22107
TrEMBL
other Location (Reliability: 2)
V6CJZ8_CAEEL
138
0
15923
TrEMBL
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme is composed of a catalytic head domain and a regulatory tail
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F260D
part of a putative amphipathic alpha helix
F260K
part of a putative amphipathic alpha helix
F260L
part of a putative amphipathic alpha helix
F260V
part of a putative amphipathic alpha helix
F269I
part of a putative amphipathic alpha helix
I256S
part of a putative amphipathic alpha helix
I257S
part of a putative amphipathic alpha helix
L246S
part of a putative amphipathic alpha helix
L246S/W249S/I256S/I257S
part of a putative amphipathic alpha helix
W249S
part of a putative amphipathic alpha helix
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TALON Co2+ metal affinity chromatography
wild-type and truncated forms
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged version expressed in Sf9 cell using a baculovirus exression system
wild-type and truncated forms
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
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