EC Number |
Metals/Ions |
Reference |
---|
5.6.1.7 | Ca2+ |
is found to protect against proteolysis of a form of GroEL, ox-GroEL, prepared by exposing GroEL to hydroxide peroxide, induces a conformational change |
684903 |
5.6.1.7 | Ca2+ |
the enzyme is less active, when Ca2+, Cu2+, Co2+, and Ni2+ are used ar the same concentration instead of Mn2+ |
668673 |
5.6.1.7 | Co2+ |
2 mM, 41% of activity with Mg2+ |
654945 |
5.6.1.7 | Co2+ |
divalent cation required for ATP hydrolysis, mediate nucleoside triphosphate-dependent refolding of malate dehydrogenase |
698649 |
5.6.1.7 | Co2+ |
Pf Cpn shows increased ATPase activity in the presence of either Co2+ or Mn2+ |
711001 |
5.6.1.7 | Co2+ |
relatively low ATPase activity in presence of Co2+ or Mn2+ |
711541 |
5.6.1.7 | Co2+ |
Ta-cpn beta1 shows ATPase activity in the presence of Co2+. A weak ATPase activity is observed in the presence of Mn2+ or Mg2+ |
711214 |
5.6.1.7 | Co2+ |
Ta-cpn R1 hydrolyzes ATP in the presence of Co2+, Mn2+, or Mg2+. ATPase activity of the monomeric enzyme is the highest in the presence of Co2+ |
711214 |
5.6.1.7 | Co2+ |
the enzyme is less active, when Ca2+, Cu2+, Co2+, and Ni2+ are used ar the same concentration instead of Mn2+ |
668673 |
5.6.1.7 | Cs+ |
1 mM, 81% of K+ activation |
289233 |