5.3.3.2 Mg2+ - 2944, 660882, 660902, 662026, 704638 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 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 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 Ca2+ 10mM, relative activity 100% 661638 5.3.3.2 Mn2+ 10mM, relative activity 17% 661638 5.3.3.2 Mg2+ 10mM, relative activity 65% 661638 5.3.3.2 Co2+ 10mM, relative activity under 0.005% 661638 5.3.3.2 Cu2+ 10mM, relative activity under 0.005% 661638 5.3.3.2 Ni2+ 10mM, relative activity under 0.005% 661638 5.3.3.2 Mg2+ activation by a mixture of Mg2+ and Mn2+ gives the highest activity 2952 5.3.3.2 Mn2+ 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 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+ IDI-1 is a zinc-metalloprotein 714202 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 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 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 Ca2+ lower activity as with Mg2+ 661357 5.3.3.2 Mn2+ lower activity as with Mg2+ 661357 5.3.3.2 Mg2+ maximal acitivity 661357 5.3.3.2 Mn2+ maximal activation at 0.1 mM 2948 5.3.3.2 Mg2+ maximal activation at 0.2 mM 2944 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 Mg2+ maximal activation at 20 mM 2948 5.3.3.2 Mg2+ maximal activation at 5 mM 2936 5.3.3.2 Mn2+ maximal activity at 0.01 mM 680882 5.3.3.2 Mg2+ Mn2+ is a better activator than Mg2+ 2942 5.3.3.2 Mn2+ 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 Mn2+ Mn2+ or Mg2+ required 2938, 2941, 2942, 2944, 2946, 2948, 2952 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 Mg2+ preference for Mn2+ over Mg2+ 727623 5.3.3.2 Mn2+ preference for Mn2+ over Mg2+ 727623 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+ reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme 680346 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 Mg2+ required 2935, 651170 5.3.3.2 Mg2+ required for activity 714202 5.3.3.2 Mn2+ required, 2.5fold increase in activity with 0.1 mM Mn2+ 727624 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 Mn2+ restores activity after EDTA treatment 2936 5.3.3.2 Co2+ slight activation 2937 5.3.3.2 Mg2+ slight activation 2937 5.3.3.2 Ni2+ 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 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 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+ 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