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Literature summary for 2.7.7.14 extracted from
- 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.
Application
| Application | Comment | Organism |
|---|---|---|
| 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)
| Cloned (Comment) | Organism |
|---|---|
| PfECT, sequence comparison, expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Plasmodium falciparum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H146A | site-directed mutagenesis, the mutant is almost inactive | Plasmodium falciparum |
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics of wild-type and mutant enzymes, overview | Plasmodium falciparum | |
| 0.373 | - |
Ethanolamine phosphate | pH 8.0, 37°C, native enzyme | Plasmodium falciparum |  |
| 0.374 | - |
CTP | pH 8.0, 37°C, recombinant His-tagged mutant H146A enzyme | Plasmodium falciparum | |
| 0.452 | - |
Ethanolamine phosphate | pH 8.0, 37°C, recombinant His-tagged wild-type enzyme | Plasmodium falciparum | |
| 0.465 | - |
CTP | pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme | Plasmodium falciparum | |
| 0.565 | - |
Ethanolamine phosphate | pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme | Plasmodium falciparum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | cellular localization and expression of PfECT along the parasite life cycle, overview | Plasmodium falciparum | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Plasmodium falciparum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CTP + ethanolamine phosphate | Plasmodium falciparum | - |
diphosphate + CDP-ethanolamine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | Q8IDM2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CTP + ethanolamine phosphate | - |
Plasmodium falciparum | diphosphate + CDP-ethanolamine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | homology modelling, three-dimensional structural model of Pf ECT, overview | Plasmodium falciparum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CTP:phosphoethanolamine CT | - |
Plasmodium falciparum |
| CTP:phosphoethanolamine cytidylyltransferase | - |
Plasmodium falciparum |
| ECT | - |
Plasmodium falciparum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Plasmodium falciparum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.4 | - |
Ethanolamine phosphate | pH 8.0, 37°C, recombinant His-tagged wild-type enzyme | Plasmodium falciparum | |
| 4.1 | - |
Ethanolamine phosphate | pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme | Plasmodium falciparum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Plasmodium falciparum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | inhibition of PE biosynthesis leads to parasite death | Plasmodium falciparum |
| metabolism | the enzyme catalyzes the rate-limiting step of the PE metabolic pathway in the parasite | Plasmodium falciparum |
| 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 |
| 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 |
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