EC Number   |
Reference |
|---|
    1.15.1.1 | activity cannot be restored by Fe2+, Cu2+, Zn2+, and Cu2+/Zn2+, but by Mn2+ |
438191 |
| 1.15.1.1 | after reconstitution with Fe3+ instead of Mn2+, the enzyme shows properties similar to Fe-SODs |
438161 |
| 1.15.1.1 | apoprotein expressed in insect cells can be restored by addition of Cu2+, fully active |
438174 |
| 1.15.1.1 | enzyme folding and unfolding kinetic mechanism of wild-type and mutant enzymes at pH 7.8 and 25°C, role of metal ions, overview |
705133 |
| 1.15.1.1 | incubation of purified apoprotein with metal salts at ambient temperatures, no restauration of activity. Reactivation by heating apoprotein with manganese salts at elevated temperatures, both manganese and iron bind to protein, but only manganese restores activity. Mechanism of metallation |
657896 |
| 1.15.1.1 | recombinant EC-SOD refolds from inclusion bodies in E. coli after denaturing |
438180 |
| 1.15.1.1 | reconstitution of active enzyme after withdrawal of metal by either Mn or Fe yielding an active enzyme irrespective of the metal ion initially present |
438097, 438112 |
| 1.15.1.1 | reconstitution of active enzyme after withdrawal of metal either with the native metal or with cadmium, chromium or iron |
438096 |
| 1.15.1.1 | reconstitution of active enzyme after withdrawal of Mn2+ by addition of Mn2+ to apoprotein in 8 M urea at acid pH |
438155 |
| 1.15.1.1 | reconstitution of active protein after withdrawal of metal, higher activity with Mn2+, lower activity with Fe3+ |
438171, 438188 |
