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Literature summary extracted from

  • Maheshwari, S.; Lavigne, M.; Contet, A.; Alberge, B.; Pihan, E.; Kocken, C.; Wengelnik, K.; Douguet, D.; Vial, H.; Cerdan, R.
    Biochemical characterization of Plasmodium falciparum CTP:phosphoethanolamine cytidylyltransferase shows that only one of the two cytidylyltransferase domains is active (2013), Biochem. J., 450, 159-167.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.7.14 drug development given the absence of PE synthesis in red blood cells, PfECT represents a potential antimalarial target opening the way for a rational conception of bioactive compounds Plasmodium falciparum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.14 PfECT, sequence comparison, expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.14 H146A site-directed mutagenesis, the mutant is almost inactive Plasmodium falciparum
2.7.7.14 H422A site-directed mutagenesis, the mutant shows increased kcat and Vmax with ethanolamine phosphate compared to the wild-type enzyme Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.14 additional information
-
 additional information Michaelis-Menten kinetics of wild-type and mutant enzymes, overview Plasmodium falciparum
2.7.7.14 0.373
-
 Ethanolamine phosphate pH 8.0, 37°C, native enzyme Plasmodium falciparum
2.7.7.14 0.374
-
 CTP pH 8.0, 37°C, recombinant His-tagged mutant H146A enzyme Plasmodium falciparum
2.7.7.14 0.452
-
 Ethanolamine phosphate pH 8.0, 37°C, recombinant His-tagged wild-type enzyme Plasmodium falciparum
2.7.7.14 0.465
-
 CTP pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme Plasmodium falciparum
2.7.7.14 0.565
-
 Ethanolamine phosphate pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.14 additional information cellular localization and expression of PfECT along the parasite life cycle, overview Plasmodium falciparum
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.14 Mg2+ required Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.14 CTP + ethanolamine phosphate Plasmodium falciparum
-
 diphosphate + CDP-ethanolamine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.14 Plasmodium falciparum Q8IDM2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.14 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.14 CTP + ethanolamine phosphate
-
 Plasmodium falciparum diphosphate + CDP-ethanolamine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.14 More homology modelling, three-dimensional structural model of Pf ECT, overview Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
2.7.7.14 CTP:phosphoethanolamine CT
-
 Plasmodium falciparum
2.7.7.14 CTP:phosphoethanolamine cytidylyltransferase
-
 Plasmodium falciparum
2.7.7.14 ECT
-
 Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.14 37
-
 assay at Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.14 3.4
-
 Ethanolamine phosphate pH 8.0, 37°C, recombinant His-tagged wild-type enzyme Plasmodium falciparum
2.7.7.14 4.1
-
 Ethanolamine phosphate pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.14 8
-
 assay at Plasmodium falciparum

General Information

EC Number General Information Comment Organism
2.7.7.14 malfunction inhibition of PE biosynthesis leads to parasite death Plasmodium falciparum
2.7.7.14 metabolism the enzyme catalyzes the rate-limiting step of the PE metabolic pathway in the parasite Plasmodium falciparum
2.7.7.14 additional information the N-terminal CT domain is the only catalytically active domain of the enzyme. The inactive C-terminal domain is important for dimer stabilization. Homology modelling, three-dimensional structural model of Pf ECT, overview Plasmodium falciparum
2.7.7.14 physiological function phosphatidylethanolamine is mainly synthesized de novo by the CDP:ethanolamine-dependent Kennedy pathway. Plasmodium falciparum requires massive synthesis of phosphatidylethanolamine that together with phosphatidylcholine constitute the bulk of the malaria membrane lipids Plasmodium falciparum