5.3.3.2 Ca2+ 10mM, relative activity 100% 661638 5.3.3.2 Ca2+ lower activity as with Mg2+ 661357 5.3.3.2 Cd2+ reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme 680346 5.3.3.2 Co2+ 10mM, relative activity under 0.005% 661638 5.3.3.2 Co2+ reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme 680346 5.3.3.2 Co2+ slight activation 2937 5.3.3.2 Cu2+ 10mM, relative activity under 0.005% 661638 5.3.3.2 Mg2+ - 2944, 660882, 660902, 662026, 704638 5.3.3.2 Mg2+ 0.72 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme 680346 5.3.3.2 Mg2+ 10mM, relative activity 65% 661638 5.3.3.2 Mg2+ activation by a mixture of Mg2+ and Mn2+ gives the highest activity 2952 5.3.3.2 Mg2+ dependent on 727103 5.3.3.2 Mg2+ IDI-2 requires a divalent cation such as Mg2+ for activity 713655 5.3.3.2 Mg2+ isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory 2952 5.3.3.2 Mg2+ isomerase II: maximal activation at 2-8 mM Mg2+, the maximal activation is 35% lower than the activation obtained with Mn2+ 2952 5.3.3.2 Mg2+ Kd value is 0.13 mM at pH 7.0, 37°C 678278 5.3.3.2 Mg2+ maximal acitivity 661357 5.3.3.2 Mg2+ maximal activation at 0.2 mM 2944 5.3.3.2 Mg2+ maximal activation at 20 mM 2948 5.3.3.2 Mg2+ maximal activation at 5 mM 2936 5.3.3.2 Mg2+ Mn2+ is a better activator than Mg2+ 2942 5.3.3.2 Mg2+ Mn2+ or Mg2+ required 2938, 2941, 2942, 2944, 2946, 2948, 2952 5.3.3.2 Mg2+ preference for Mn2+ over Mg2+ 727623 5.3.3.2 Mg2+ required 2935, 651170 5.3.3.2 Mg2+ required for activity 714202 5.3.3.2 Mg2+ required, 2fold increase in activity with 10 mM Mg2+ 727624 5.3.3.2 Mg2+ required. The enzyme requires the combined presence of FMN, NADPH and Mg2+ 651733 5.3.3.2 Mg2+ restores activity after EDTA treatment 2936 5.3.3.2 Mg2+ slight activation 2937 5.3.3.2 Mg2+ the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer 651597 5.3.3.2 Mg2+ the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site 650979 5.3.3.2 Mn2+ - 2944 5.3.3.2 Mn2+ 0.10 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme 680346 5.3.3.2 Mn2+ 10mM, relative activity 17% 661638 5.3.3.2 Mn2+ activation by a mixture of Mg2+ and Mn2+ gives the highest activity 2952 5.3.3.2 Mn2+ isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory 2952 5.3.3.2 Mn2+ isomerase I: maximal activation at 0.5 mM, isomerase II, III or IV: maximal activation at 0.25 mM 2937 5.3.3.2 Mn2+ lower activity as with Mg2+ 661357 5.3.3.2 Mn2+ maximal activation at 0.1 mM 2948 5.3.3.2 Mn2+ maximal activation at 0.5 mM 2946 5.3.3.2 Mn2+ maximal activation at 2 mM, activity maximum obtained with Mn2+ is about 3times that with Mg2+ 2936 5.3.3.2 Mn2+ maximal activity at 0.01 mM 680882 5.3.3.2 Mn2+ Mn2+ is a better activator than Mg2+ 2942 5.3.3.2 Mn2+ Mn2+ or Mg2+ required 2938, 2941, 2942, 2944, 2946, 2948, 2952 5.3.3.2 Mn2+ preference for Mn2+ over Mg2+ 727623 5.3.3.2 Mn2+ required, 2.5fold increase in activity with 0.1 mM Mn2+ 727624 5.3.3.2 Mn2+ restores activity after EDTA treatment 2936 5.3.3.2 Mn2+ the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer 651597 5.3.3.2 Mn2+ the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site 650979 5.3.3.2 additional information no effects of other divalent cations such as Co2+, Cu2+, Zn2+ at 5mM 661357 5.3.3.2 additional information not activated by Zn2*, Fe2*, or Cu2+ 727623 5.3.3.2 additional information not activated by Zn2+ 727624 5.3.3.2 additional information not activated by Zn2+, Fe2+, or Cu2+ 727623 5.3.3.2 Ni2+ 10mM, relative activity under 0.005% 661638 5.3.3.2 Ni2+ reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme 680346 5.3.3.2 Ni2+ slight activation 2937 5.3.3.2 Zinc essential cofactor. Type I enzyme contains an atom of tinc. The metal is located in an unusual six-coordinate pocket and may facilitate protonation of the unactivated carbon-carbon double bond in isopentenyl diphosphate 651597 5.3.3.2 Zn2+ 0.92 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme 680346 5.3.3.2 Zn2+ 10mM, relative activity 0.2% 661638 5.3.3.2 Zn2+ IDI-1 is a zinc-metalloprotein 714202