Cloned (Comment) | Organism |
---|---|
- |
Entamoeba histolytica |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Entamoeba histolytica | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
PSAT | - |
Entamoeba histolytica |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
apo-enzyme | Entamoeba histolytica |
67 | - |
holo-enzyme | Entamoeba histolytica |
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 |