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Literature summary for 2.6.1.52 extracted from
- Biophysical characterization of Entamoeba histolytica phosphoserine aminotransferase (EhPSAT): role of cofactor and domains in stability and subunit assembly (2011), Eur. Biophys. J., 40, 599-610.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Entamoeba histolytica |
General Stability
| General Stability | Organism |
|---|---|
| Cm values obtained from the denaturation profile for holo-enzyme and apo- | Entamoeba histolytica |
| enzyme are 2.8 and 2 M, respectively. | Entamoeba histolytica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Entamoeba histolytica | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PSAT | - |
Entamoeba histolytica |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
apo-enzyme | Entamoeba histolytica |
| 67 | - |
holo-enzyme | Entamoeba histolytica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | presence of cofactor influences the tertiary structure. The cofactor does not influence the secondary structure of the enzyme. Stability of the protein is significantly affected by the cofactor as holo-enzyme shows higher values for thermal and GdnHCl-induced denaturation, respectively, when compared to the apoenzyme. The cofactor also influences the unfolding pathway of the enzyme. Although urea-dependent unfolding of both holo- and apo-EhPSAT is a three-state process, the intermediates stabilized during unfolding are significantly different. For the holo-enzyme a dimeric holo-intermediate is stabilized, whereas for the apo-enzyme, a monomeric intermediate is stabilized | Entamoeba histolytica |  |
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