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Literature summary for 2.7.7.15 extracted from

  • 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 (2020), Sci. Rep., 10, 19739 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm activation of phosphatidylcholine biosynthesis by phospholipase C treatment induces the partial nuclear-to-cytoplasmic translocation of the enzyme Plasmodium falciparum 5737
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nucleus 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 Plasmodium falciparum 5634
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CTP + phosphocholine Plasmodium falciparum
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diphosphate + CDP-choline
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?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum P49587
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + phosphocholine
-
Plasmodium falciparum diphosphate + CDP-choline
-
?

Synonyms

Synonyms Comment Organism
CTP:phosphocholine cytidylyltransferase
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Plasmodium falciparum
PfCCT
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Plasmodium falciparum

General Information

General Information Comment Organism
metabolism rate limiting step of the de novo phosphatidylcholine biosynthesis is catalysed by CTP:phosphocholine cytidylyltransferase, which has a key regulatory function within the pathway Plasmodium falciparum