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Information on EC 2.7.7.15 - choline-phosphate cytidylyltransferase and Organism(s) Plasmodium falciparum

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Plasmodium falciparum
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The taxonomic range for the selected organisms is: Plasmodium falciparum
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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-
-
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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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-
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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 + CDPcholine
show the reaction diagram
-
dCTP can replace CTP with reduced activity
-
-
?
CTP + phosphocholine
diphosphate + CDP-choline
show the reaction diagram
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 + phosphocholine
diphosphate + CDP-choline
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
maximal activity at 10-40 mM, concentrations above 40 mM are inhibitory
Mn2+
-
can partially replace Mg2+, maximal activity at 5 mM, concentrations above 5 mM are inhibitory
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mg2+
-
concentrations above 40 mM are inhibitory
Mn2+
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concentrations above 5 mM are inhibitory
NaCl
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inhibitory above 200 mM, 39% inhibition at 300 mM, 67% inhibition at 500 mM
sphingosine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 28.9
CTP
0.49 - 0.66
phosphocholine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007 - 1.45
CTP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
activation of phosphatidylcholine biosynthesis by phospholipase C treatment induces the partial nuclear-to-cytoplasmic translocation of the enzyme
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9BMP5_PLAFA
370
0
42657
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H45N/H630N
inactive enzyme
H630N
mutation diminishes the catalytic rate constant of the enzyme
R96H/R681H
thermosensitive mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme H630N
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologous expression of CTP:phosphocholine cytidylyltransferase from Plasmodium falciparum rescues Chinese Hamster Ovary cells deficient in the Kennedy phosphatidylcholine biosynthesis pathway
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team