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Literature summary for 2.7.1.40 extracted from
- Biochemical and biophysical characterization of the smallest pyruvate kinase from Entamoeba histolytica (2020), Biochim. Biophys. Acta, 1868, 140296 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene EHI_098420, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Entamoeba histolytica |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics for phosphoenolpyruvate | Entamoeba histolytica | |
| 0.23 | - |
phosphoenolpyruvate | pH 7.5, 37°C | Entamoeba histolytica |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 70000 | - |
recombinant enzyme, gel filtration | Entamoeba histolytica |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + phosphoenolpyruvate | Entamoeba histolytica | - |
ATP + pyruvate | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Entamoeba histolytica | C4LXC4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration, to over 95% purity | Entamoeba histolytica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + phosphoenolpyruvate | - |
Entamoeba histolytica | ATP + pyruvate | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 36000, recombinant enzyme, SDS-PAGE | Entamoeba histolytica |
| More | secondary structure determination by circular dichroism spectrometry. Effect of pH on the tertiary structure, overview | Entamoeba histolytica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EHI_098420 | - |
Entamoeba histolytica |
| EhPyk | - |
Entamoeba histolytica |
| PYK | - |
Entamoeba histolytica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Entamoeba histolytica |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | enzyme EhPyk thermal denaturation study at different pH values, overview | Entamoeba histolytica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 9.79 | - |
phosphoenolpyruvate | pH 7.5, 37°C | Entamoeba histolytica | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Entamoeba histolytica |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
effect of pH on the tertiary structure | Entamoeba histolytica |
| 4 | 10 | activity range, inactive below and above, the enzyme exhibits 73% and 29% at pH 7.0 and pH 8.0, respectively, compared to the maximal activity at pH 7.5 | Entamoeba histolytica |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 10 | stable at, most stable at pH 7.0, enzyme EhPyk is more stable in the alkaline pH range | Entamoeba histolytica |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme EhPyk is the shortest Pyk known to date as it contains only two of the three characterized domains when compared to the other homologues, phylogenetic analysis, the enzyme belongs to a distinct branch from the known type I/II Pyks | Entamoeba histolytica |
| metabolism | the ATP synthesis in the pathogen Entamoeba histolytica is solely dependent on the glycolysis pathway where pyruvate kinase (Pyk) catalyzes the final reaction. This reaction is essentially an irreversible step of the pathway. Pyruvate kinase has been characterized as an enzyme, which is critical for the metabolic flux control of the second half of the Embden-Meyerhof-Parnas pathway. The regulation of Pyk is essential not only for this pathway but also for all other major cellular metabolisms coordinated in the cell | Entamoeba histolytica |
| additional information | homology modelling of EhPyk, molecular dynamics simulation study | Entamoeba histolytica |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 42.57 | - |
phosphoenolpyruvate | pH 7.5, 37°C | Entamoeba histolytica | |
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Release 2023.1 (January 2023)
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