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 5.6.1.7 Cu2+ 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 K+ 1 mM, 100fold activation in the absence of Cpn10, half-maximal rate at 0.080 mM K+ 289236 5.6.1.7 K+ 100 mM used in assay conditions 749868 5.6.1.7 K+ 2fold activation in the absence of Cpn10 289233 5.6.1.7 K+ 2fold activation with 25 mM KCl 289227 5.6.1.7 K+ 50 mM used in assay conditions 750509 5.6.1.7 K+ ATPase activity is dependent on Mn2+ and K+ 668673 5.6.1.7 K+ essential for hydrolysis of ATP, ATPase activity is barely retained in the absence of K+ 720255 5.6.1.7 K+ K+ concentration of half-maximal ATPase activity, 1.3 mM 289221 5.6.1.7 K+ required for activity, maximal activity at 2 mM 654945 5.6.1.7 K+ required for activity, no activity below 10 mM, maximal activity at 600 mM 655574 5.6.1.7 K+ required for hydrolysis 682745 5.6.1.7 K+ strong activation of CTT complex, almost no activity at 800 mM, maximal activity above 3.2 M 655565 5.6.1.7 K+ strong ATPase activity in presence of K+, optimal concentration: 2 M 711541 5.6.1.7 KCl 50-500 mM, stimulates ATPase activity. ATPase activity decreases significantly at higher KCl concentrations (1-2 M) 711001 5.6.1.7 Li+ 1 mM, 74% of K+ activation 289233 5.6.1.7 Mg2+ 10 mM used in assay conditions 749868 5.6.1.7 Mg2+ 2 mM used in assay conditions 752034 5.6.1.7 Mg2+ 20 mM used in assay conditions 750509 5.6.1.7 Mg2+ absolutely required for activity of CTT complex 655565 5.6.1.7 Mg2+ ATPase activity depends on K+ and Mg2+, optimal concentration: 5-7.5 mM Mg2+ 711541 5.6.1.7 Mg2+ ATPase activity of Pf Cpn is dependent on Mg2+ with uniform activity from 1 to 50 mM 711001 5.6.1.7 Mg2+ half maximal ATPase activation at 2.6 mM 289226 5.6.1.7 Mg2+ highest ATP hydrolysis activity, mediate ATP-dependent refolding of malate dehydrogenase and green fluorescent protein, suppression of rhodanese and luciferase thermal aggregation 698649 5.6.1.7 Mg2+ 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 Mg2+ required 733223, 733278, 733538, 733876, 734278, 734473, 735006, 735322 5.6.1.7 Mg2+ required for activity, maximal activity at 2 mM 654945 5.6.1.7 Mg2+ required for activity, similar activation between 1 and 50 mM 655574 5.6.1.7 Mg2+ 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 Mg2+ Ta-cpn R1 hydrolyzes ATP in the presence of Co2+, Mn2+, or Mg2+ 711214 5.6.1.7 Mn2+ 2 mM, 64% of activity with Mg2+ 654945 5.6.1.7 Mn2+ ATPase activity is dependent on Mn2+ and K+. Optimal Mn2+ concentration: 10 mM 668673 5.6.1.7 Mn2+ divalent cation required for ATP hydrolysis, mediate ATP-dependent refolding of malate dehydrogenase and green fluorescent protein, suppression of rhodanese and luciferase thermal aggregation, increased substrate protein binding of Ta-cpn alpha 698649 5.6.1.7 Mn2+ half maximal ATPase activation at 2.3 mM 289226 5.6.1.7 Mn2+ 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 Mn2+ Pf Cpn shows increased ATPase activity in the presence of either Co2+ or Mn2+ 711001 5.6.1.7 Mn2+ relatively low ATPase activity in presence of Co2+ or Mn2+ 711541 5.6.1.7 Mn2+ 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 Mn2+ Ta-cpn R1 hydrolyzes ATP in the presence of Co2+, Mn2+, or Mg2+ 711214 5.6.1.7 additional information in the presence of Cd2+, Ba2+, Ca2+ or Sr2+, little ATPase activity occurrs. Little activity is found in the presence of Na+ or Li+ 711541 5.6.1.7 additional information recombinant enzyme remains active in high ionic strength 711001 5.6.1.7 Na+ 1 mM, 87% of K+ activation 289233 5.6.1.7 NaCl 50-500 mM, stimulates ATPase activity. The enzyme maintains full ATPase activity up to 2 M 711001 5.6.1.7 NH4+ 200 mM, approx. 40% of activity with 200 mM KCl 655574 5.6.1.7 NH4+ can fully substitute for K+ 654945 5.6.1.7 NH4+ strong ATPase activity in presence of NH4+ 711541 5.6.1.7 NH4Cl 50-500 mM, stimulate ATPase activity. The enzyme maintains full ATPase activity up to 2 M 711001 5.6.1.7 Ni2+ 2 mM, 29% of activity with Mg2+ 654945 5.6.1.7 Ni2+ 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 Ni2+ 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 Rb+ - 289236 5.6.1.7 Rb+ can fully substitute for K+ 654945 5.6.1.7 Zn2+ His45, Cys51, and Cys53 make up an oxidation-sensitive zinc-binding site that may donate the bound metal to a zinc acceptor. Wild-type HpGroES binds two Zn2+ per monomer, HpGroESDELTAMBD (MBD i.e. metal-binding domain) contains 0.71 per monomer. H45A, C51A, and C53A decreased to 0.3-0.5 Zn2+ per monomer. The double-cysteine mutant (C51A/C53A) gives only 0.12 Zn2+ per monomer 713424 5.6.1.7 Zn2+ 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