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K+
-
mutant D428N, Km-value 19 mM, mutant D428E, Km-value 35 mM
KCl
-
maximal activity required KCl concentrations of greater than 3.5 M
NaCl
-
while raising the NaCl concentration from 1.5 to 3.5 M leads to an increase in enzyme activity, this increase is 3fold lower than that detected in the presence of optimal KCl levels
Ca2+
activates
Cd2+
activates
Mg2+
-
1 mM used in assay conditions
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the cofactor thiamine diphosphate in the active site
Mg2+
required, the Mg2+ cation is coordinated to residues of a single monomer, binding site structure, overview
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
0.5 mM used in assay conditions
Mg2+
divalent metal ion Mg2+ i required for catalytic activity. In catalysis, a divalent metal ion Mg2+ serves to anchor the diphosphate moiety of thiamine diphosphate at the active site of the catabolic enzyme
Mg2+
-
Km: 0.3 mM for isoenzyme I, 0.4 mM for isoenzyme III
Mg2+
-
wild-type, Km-value 0.01 mM, mutant D428N, Km-value 0.21 mM, mutant D428E, Km-value 0.36 mM
Mg2+
-
activates, binding structure at the regulatory subunit
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
a bivalent metal cation is required
Mg2+
K0.5 value for holoenzyme 0.02 mM, for the isolated large subunit 1.3 mM
Mg2+
the enzyme requires a divalent metal ion
Mg2+
-
Mg2 is probably the natural cofactor of the enzyme. Halofgerax volcanii is thought to contain a high intracellular Mg2+ concentration, as its native habitat, the Dead Sea, contains 1.4 M MgCl2. The endogenous metal is apparently tightly-enough bound so that added Mg2+ does not stimulate the activity
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
strong requirement
Mg2+
-
a divalent metal ion is required
Mg2+
a bivalent metal cation is required
Mg2+
the enzyme requires a divalent metal ion such as Mg2+ to anchor thiamine diphosphate
Mg2+
the enzyme requires a divalent metal ion such as Mg2+ to anchor thiamine diphosphate
Mg2+
-
10 mM used in assay conditions
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
required, spectral analysis and kinetics of Mg2+ binding, overview
Mg2+
-
the enzyme requires a divalent metal ion
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
-
a bivalent metal cation is required
Mg2+
the enzyme requires a divalent metal ion
Mg2+
-
a bivalent metal cation is required
Mg2+
-
the enzyme requires a divalent metal ion
Mg2+
-
a bivalent metal cation is required
Mg2+
-
the enzyme requires a divalent metal ion, involved in anchoring the thiamine diphosphate cofactor in the active site
Mg2+
-
saturated at 1 mM MgCl2
Mn2+
-
-
Mn2+
-
activates, high concentrations inhibit
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
Km: 0.016 mM MnCl2
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
the enzyme requires a divalent metal ion
Mn2+
-
the activity is about 133% for Mn2+ as compared to Mg2+
Mn2+
-
can substitute for Mg2+
Ni2+
-
stimulates
Ni2+
-
the activity is about 50% for Ni2+ as compared to Mg2+
Zn2+
-
stimulates
additional information
-
a divalent ion is required
additional information
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+. Modeling of the activity of the metal ions in the catalytic mechanism of isozyme AHAS II
additional information
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+. Modeling of the activity of the metal ions in the catalytic mechanism of isozyme AHAS II
additional information
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+. Modeling of the activity of the metal ions in the catalytic mechanism of isozyme AHAS II
additional information
-
no effect: Mg2+
additional information
-
no effect: Mn2+, Mg2+, Ca2+
additional information
-
the enzyme does not require a divalent cation for activity
additional information
-
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+
additional information
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+
additional information
-
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+
additional information
-
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+
additional information
the enzyme contains a divalent metal ion as cofactor
additional information
-
AHASII is active in the presence of Mn2+, Mg2+, Ca2+, Cd2+, Co2+, Zn2+, Cu2+, Al3+, Ba2+ or Ni2+, the activity is about 50% for Ni2+ and 133% for Mn2+ as compared to Mg2+
additional information
-
enzyme AHAS is not specific as far as metal ions are concerned. It is active in presence of any metal ion like Mn2+, Mg2+, Ca2+, Cd2+
additional information
-
the AHAS activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (up to 500 mM is tested), suggesting it might be needed to maintain the functional oligomeric state of the enzyme
additional information
the AHAS activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (up to 500 mM is tested), suggesting it might be needed to maintain the functional oligomeric state of the enzyme
additional information
the AHAS activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (up to 500 mM is tested), suggesting it might be needed to maintain the functional oligomeric state of the enzyme