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sulfate
-
2 molecules bound per enzyme dimer, 1 at each active site, binding structure
Triton
-
3 Triton (T1, T2, and T3) are located in the two monomers with one on the top portion of the active site tunnel in monomer A and the other two occupying the overall tunnel of monomer B
Co2+
-
divalent cation required
Co2+
-
divalent cation required
Co2+
-
enzyme is equally stimulated by 0.2 mM Mg2+, 0.2 mM Co2+ or 0.1 mM Mn2+
Co2+
-
maximal stimulation at 0.1-0.3 mM
Co2+
-
divalent cation required
Co2+
-
enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+
K+
-
stimulates in presence of Mg2+
K+
stimulates in presence of Mg2+
K+
-
stimulates in presence of Mg2+
Mg2+
-
divalent cation required
Mg2+
-
best stimulation by Mg2+. Mn2+ and Zn2+ may partially replace Mn2+
Mg2+
-
optimal activity at 5 mM, required
Mg2+
-
Mg2+ or Mn2+ required. Optimal concentration for Mg2+ is 1.0 mM
Mg2+
-
required, best at 0.5 mM MgCl2, 2 Mg2+ are bound at the subunit interface, binding structure
Mg2+
-
required, enzyme utilizes a Asp-rich motif for substrate binding via Mg2+
Mg2+
role of the metal ion in catalysis, required for binding of isopentenyl diphosphate to the enzyme, best at 1 mM, low activity at 50 mM, Asp26 is required for efficient binding, Mg2+ is bound to the diphosphate of farnesyl diphosphate in the wild-type enzyme, but to the diphosphate of isopentenyl diphosphate in the mutant D26A, Mg2+ is not required for the overall structure stability, overview
Mg2+
-
or Mn2+ required. Optimal concentration 1.0 mM
Mg2+
-
is chelated by His199 and Glu213 from different subunits and possibly plays astructural rather than catalytic role
Mg2+
-
optimal concentration between 0.5 and 2 mM, dependend on
Mg2+
-
required, structures of Mg2+ binding of wild-type and mutant UPPS, overview
Mg2+
-
divalent cation required
Mg2+
-
enzyme is equally stimulated by 0.2 mM Mg2+, 0.2 mM Co2+ or 0.1 mM Mn2+
Mg2+
-
maximal stimulation at 0.1-0.3 mM
Mg2+
-
divalent cation required
Mg2+
-
enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+
Mg2+
divalent metal ion required, Mg2+ is most effective, optimal concentration is 240 nM
Mg2+
-
maximal stimulation at 0.1 mM
Mg2+
-
required, structures of Mg2+ binding of wild-type and mutant UPPS, overview
Mg2+
required, structures of Mg2+ binding of wild-type and mutant UPPS, overview
Mn2+
-
can partially replace Mg2+
Mn2+
-
best stimulation by Mg2+. Mn2+ and Zn2+ may partially replace Mn2+
Mn2+
-
can partially replace Mg2+, optimal activity at 0.5 mM
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
maximal stimulation at 0.05-0.1 mM, Mg2+ or Mn2+ required
Mn2+
-
enzyme is equally stimulated by 0.2 mM Mg2+, 0.2 mM Co2+ or 0.1 mM Mn2+
Mn2+
-
effective in stimulation at 0.05-0.1 mM
Mn2+
-
enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+
Na+
-
stimulates in presence of Mg2+
Na+
stimulates in presence of Mg2+
Na+
-
stimulates in presence of Mg2+
NH4+
-
stimulates in presence of Mg2+
NH4+
stimulates in presence of Mg2+
NH4+
-
stimulates in presence of Mg2+
Zn2+
-
can partially replace Mg2+
Zn2+
-
maximal stimulation at 0.1-0.3 mM
Zn2+
optimal concentration for activation is about 240 nM