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Ca2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Fe3+
-
1 mM, 5-10% stimulation
Li+
-
1 mM, 5-10% stimulation
Magnesium
wild-type enzyme contains 0.05 mol of magnesium per mol of enzyme, mutant enzyme N26C contains 0.4 mol of magnesium per mol of enzyme
Sr2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Ba2+
-
1 mM, 5-10% stimulation
Ba2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cd2+
-
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
Cd2+
-
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
Cd2+
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
Cd2+
-
maximal activation below 0.1 mM
Cd2+
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
Cd2+
increase in steady-state rate of wild-type enzyme, Km: 0.0006 mM
Cd2+
-
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
Cd2+
-
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
Cd2+
-
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
Cd2+
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
Cd2+
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cd2+
-
destabilizes the enzyme, overview
Co2+
-
presence of Co2+ restores activity to metal-free enzyme
Co2+
-
stimulates wild-type enzyme above 0.4 mM, no stimulation of mutant enzyme C11A
Co2+
-
full reactivation of EDTA-treated enzyme
Co2+
-
monomer and dimer are each bound with 1 metal ion, tetramer with 2
Co2+
no activation of wild type enzyme, adverse effect on mutant N23C, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cu2+
-
maximal activation below 0.1 mM
Cu2+
third in enzyme activity, octahedral or distorted tetrahedral delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization, product is bound in its linear conformation in the crystal structure of the enzyme with Cu2+, greenish color of enzyme, new absorption peak at 380 nm instead of 505 nm
Cu2+
-
inhibits at high concentrations, stimulates below 0.001 mM
Cu2+
-
4 Cu2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer
Cu2+
no activation of mutant enzymes containing the N23C substitution, slight reduction of wild type enzyme activity, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Fe2+
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations. Mutation H185G decreases the ability of the enzyme to bind Fe2+, but not Zn2+. Maximal activity, about 8-10% of the wild-type activity is obtained when the native metal is replaced with Cd2+
Fe2+
-
contains 0.2-0.3 equivalents of iron per enzyme subunit. FeSO4 stimulates
Fe2+
unsubstituted enzyme with lowest enzyme activity
Fe2+
no activation of wild type enzyme and metal-independent mutants, activation of N23C/D247E, N23C/C246S/D247E, inhibitory for N23C, N23C/C246S/P249A, N23C/C246S/D247E/P249A, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Iron
-
enzyme contains 0.19 mol of iron per mol of subunit
Iron
wild-type enzyme contains 0.19 mol of iron per mol of enzyme, mutant enzyme c11N contains 0.22 mol of iron per mol of enzyme
Mg2+
-
1 mM, 5-10% stimulation
Mg2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Mn2+
-
presence of Mn2+ restores activity to metal-free enzyme
Mn2+
200fold increase in steady-state rate of wild-type enzyme, Km: 0.01 mM. Addition of Mn2+ up to 2 mM does not stimulate the reaction rate of C11N mutant
Mn2+
-
stimulates wild-type enzyme above 0.4 mM, no stimulation of mutant enzyme C11A
Mn2+
-
full reactivation of EDTA-treated enzyme, Km value 0.130 mM
Mn2+
-
1 mM, 5-10% stimulation
Mn2+
no activation of wild type enzyme, activation of metal-dependent mutants, 15% reduced activity above 200 microM for mutant N23C/D247E/P249A, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Ni2+
-
full reactivation of EDTA-treated enzyme
Ni2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Zinc
-
enzyme contains 0.26 mol of zinc per mol of subunit
Zinc
wild-type enzyme contains 0.26 mol per mol of enzyme, mutant enzyme c11N contains 0.02 mol of zinc per mol of enzyme.
Zinc
wild-type enzyme contains 0.05 mol of zinc per mol of enzyme, mutant enzyme N26C contains 0.2 mol of zinc per mol of enzyme
Zn2+
-
enzyme contains approximately 0.4 equivalents of zinc per enzyme subunit. Maximal activation below 0.1 mM Zn2+
Zn2+
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations
Zn2+
highest enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
Zn2+
-
the enzyme contains one mol of Zn per monomer, apoenzyme is catalytically inactive
Zn2+
-
4 Zn2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer
Zn2+
activates, stabilizes, active site bound
Zn2+
no activation of wild type enzyme, inhibitory for all cloned enzymes, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
additional information
-
divalent metal ion required, with Mn2+, Co2+ and Cd2+ in decreasing order being able to restore activity to metal-free enzyme
additional information
the type of metal bound in the active site affects the behavior of the enzyme in vivo and the rate of product release in the crystal environment
additional information
-
the type of metal bound in the active site affects the behavior of the enzyme in vivo and the rate of product release in the crystal environment
additional information
-
non-metallo enzyme, no metal requirement
additional information
-
reactivation of EDTA-treated enzyme, in decreasing order: Mn2+ = Co2+ = Ni2+ = Fe2+ > Ca2+ = Mg2+ = Cd2+ > Zn2+ > Cu2+
additional information
-
no metal requirement
additional information
-
no metal requirement
additional information
-
divalent metal ions play an important role in the quaternary structure of the protein
additional information
the enzyme is specifically coordinated with Cd2+ or Zn2+ ions, and isothermal titration calorimetry and differential scanning fluorimetry reveal that Cd2+ thermally stabilizes the protein structure more efficiently than Zn2
additional information
-
the enzyme is specifically coordinated with Cd2+ or Zn2+ ions, and isothermal titration calorimetry and differential scanning fluorimetry reveal that Cd2+ thermally stabilizes the protein structure more efficiently than Zn2
additional information
-
no metal requirement
additional information
the metal chelator EDTA has no effect on the activity of the metal-independent wild type enzyme and on the metal-independent mutants C246S, D247E, D247E/P249A or P249A
additional information
-
the metal chelator EDTA has no effect on the activity of the metal-independent wild type enzyme and on the metal-independent mutants C246S, D247E, D247E/P249A or P249A
additional information
-
metal-independent enzyme. Mn2+ or Co2+ have no effect on enzyme stability
additional information
-
no stimulation by divalent cations