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Cd2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Cu2+
-
10mM, relative activity under 0.005%
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
Ca2+
-
10mM, relative activity 100%
Ca2+
lower activity as with Mg2+
Co2+
-
10mM, relative activity under 0.005%
Co2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Mg2+
-
required, 2fold increase in activity with 10 mM Mg2+
Mg2+
-
10mM, relative activity 65%
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
Mn2+ is a better activator than Mg2+
Mg2+
-
preference for Mn2+ over Mg2+
Mg2+
Cinchona robusta
-
Mn2+ or Mg2+ required
Mg2+
Cinchona robusta
-
activation by a mixture of Mg2+ and Mn2+ gives the highest activity
Mg2+
Cinchona robusta
-
isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory
Mg2+
Cinchona robusta
-
isomerase II: maximal activation at 2-8 mM Mg2+, the maximal activation is 35% lower than the activation obtained with Mn2+
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
maximal activation at 0.2 mM
Mg2+
-
required for activity
Mg2+
-
the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer
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
Mg2+
-
0.72 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
maximal activation at 20 mM
Mg2+
-
preference for Mn2+ over Mg2+
Mg2+
-
IDI-2 requires a divalent cation such as Mg2+ for activity
Mg2+
-
required. The enzyme requires the combined presence of FMN, NADPH and Mg2+
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
restores activity after EDTA treatment
Mg2+
-
maximal activation at 5 mM
Mg2+
-
preference for Mn2+ over Mg2+
Mg2+
-
required for activity
Mg2+
-
Kd value is 0.13 mM at pH 7.0, 37°C
Mn2+
-
required, 2.5fold increase in activity with 0.1 mM Mn2+
Mn2+
-
10mM, relative activity 17%
Mn2+
lower activity as with Mg2+
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
Mn2+ is a better activator than Mg2+
Mn2+
-
preference for Mn2+ over Mg2+
Mn2+
Cinchona robusta
-
Mn2+ or Mg2+ required
Mn2+
Cinchona robusta
-
activation by a mixture of Mg2+ and Mn2+ gives the highest activity
Mn2+
Cinchona robusta
-
isomerase I is activated by concentrations below 1 mM of Mn2+ or Mg2+, increasing concentrations are inhibitory
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer
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
Mn2+
-
0.10 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Mn2+
-
isomerase I: maximal activation at 0.5 mM, isomerase II, III or IV: maximal activation at 0.25 mM
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
maximal activation at 0.1 mM
Mn2+
-
maximal activity at 0.01 mM
Mn2+
-
preference for Mn2+ over Mg2+
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
maximal activation at 0.5 mM
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
restores activity after EDTA treatment
Mn2+
-
maximal activation at 2 mM, activity maximum obtained with Mn2+ is about 3times that with Mg2+
Mn2+
-
preference for Mn2+ over Mg2+
Ni2+
-
10mM, relative activity under 0.005%
Ni2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Zn2+
-
10mM, relative activity 0.2%
Zn2+
-
0.92 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Zn2+
-
IDI-1 is a zinc-metalloprotein
additional information
-
not activated by Zn2+
additional information
no effects of other divalent cations such as Co2+, Cu2+, Zn2+ at 5mM
additional information
-
no effects of other divalent cations such as Co2+, Cu2+, Zn2+ at 5mM
additional information
-
not activated by Zn2*, Fe2*, or Cu2+
additional information
-
not activated by Zn2+, Fe2+, or Cu2+
5.3.3.2 isopentenyl-diphosphate DELTA-isomerase
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results (
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