Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cd2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Cu2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Fe
-
cysteine-iron promotes arginase activity
Fe3+
-
the enzyme retains 38.7% of its original activity after dialysis. In the presence of Mn2+ as a cofactor, the enzyme regains 95% of its initial activity
Guanidinium chloride
the single mutant R308A changes to a trimeric and kinetically cooperative form, whereas the other enzyme variants are not altered
Hg2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Magnesium
stabilizes the protein. In the absence of Mg2+, a complete loss of secondary structure is observed for certain elements
Manganese
the more deeply buried Mn2+ ion A is coordinated by residues His193, Asp216, Asp220 and Asp323. The second metal, Mn2+B is co-ordinated by His218, Asp216, Asp323, Asp325
NaCl
the enzyme is optimally active at 100 mM NaCl, but as the salt concentration increase, the activity of the enzyme is reduced to almost half of the maximal activity but the enzyme is still partially active
Ca2+
-
60% of the activation as compared to Mn2+
Ca2+
-
52% of the activity with Mn2+
Ca2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Ca2+
Vigna catjang
-
35% of the activity with Mn2+
Co2+
-
displays remarkable activity in the absence of exogenous metals, although manganese, cobalt, and nickel all improve activity. Enzyme shifts its metal preference from Ni, Co,and Mn (decreasing order) when assayed at pH 6 to Ni, Mn, and Co (decreasing order) at pH 9
Co2+
-
45% of the activity with Mn2+
Co2+
-
the enzyme retains 38.7% of its original activity after dialysis. In the presence of Mn2+ as a cofactor, the enzyme regains 95% of its initial activity
Co2+
-
0.5 mM, 43% of the activity compared to activity with Mn2+
Co2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Co2+
enhances the activity
Co2+
-
required, activates, best metal cofactor
Co2+
-
enzyme is optimally active with cobalt at pH 6
Co2+
-
enzyme is selective for Co2+
Co2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
Co2+
-
the Co2+- and Mn2+-reconstituted enzymes exhibit cooperative mechanism of arginine hydrolysis, and undergo self-association and activation with increasing concentrations. Co2+ ions play a more important role in the local tertiary structure of the protein than Mn2+
Co2+
effective activator, 144% activity at 1 mM
Co2+
-
activates isozyme II 1.46fold, no activation of isozyme I
Co2+
Vigna catjang
-
66% of the activity with Mn2+
Fe2+
-
slight activation
Fe2+
Vigna catjang
-
52% of the activity with Mn2+
Mg2+
-
90% of the activation as compared to Mn2+
Mg2+
-
93% of the activity with Mn2+
Mg2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Mg2+
Vigna catjang
-
61% of the activity with Mn2+
Mn2+
-
displays remarkable activity in the absence of exogenous metals, although manganese, cobalt, and nickel all improve activity. Enzyme shifts its metal preference from Ni, Co,and Mn (decreasing order) when assayed at pH 6 to Ni, Mn, and Co (decreasing order) at pH 9
Mn2+
-
acts as co-factor and as activator
Mn2+
-
metalloenzyme binding 4 mol Mn2+ per mol enzyme
Mn2+
-
3fold increase in Vmax-value in presence of 0.1 mM Mn2+
Mn2+
-
exogenous addition of Mn2+ results in increased sensitivity to inhibitor sodium fluoride
Mn2+
-
maximal activity at 2.0 mM
Mn2+
-
maximum activity at 0.1 mM, presence of Mn2+ results in increase in Vmax, and a higher sensitivity to product and L-lysine inhibition, with no change in KM-value for L-arginine
Mn2+
-
full activation after preincubation for 20 min at 55°C with 2 mM Mn2+
Mn2+
-
the enzyme retains 38.7% of its original activity after dialysis. In the presence of Mn2+ as a cofactor, the enzyme regains 96% of its initial activity
Mn2+
-
maximum activity (100%) with 1 mM Mn2+. 0.5mM of Mn2+ exhibits 70% of total activity
Mn2+
two Mn2+ ions are required for the enzyme to be fully functional
Mn2+
-
required for catalysis, enhances lectin function of enzyme
Mn2+
optimum metal cofactor. The optimal concentration of Mn2+ is approximately 2 mM. When the concentration is higher than 2 mM, there is a slight drop in relative activity. The active site of L-arginase contains two Mn2+ ions (Mn2+A and Mn2+B), which are coordinated by Asp and His residues. When Mn2+ concentration increases from 0 to 10 mM, the ellipticity of L-arginase at 208 nm and 222 nm increases accordingly. The percentage of helix increases to 66% in the presence of 10 mM Mn2+. This suggests that the addition of Mn2+ can affect the structure of L-arginase by increasing the helix content of the enzyme
Mn2+
-
activates slightly, 14.6% of the activity with Co2+
Mn2+
-
15-20% of the activity with Co2+
Mn2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
Mn2+
-
the Co2+- and Mn2+-reconstituted enzymes exhibit cooperative mechanism of arginine hydrolysis, and undergo self-association and activation with increasing concentrations. Co2+ ions play a more important role in the local tertiary structure of the protein than Mn2+
Mn2+
effective activator, 207% activity at 1 mM
Mn2+
-
essentiell for activity
Mn2+
-
activates, role of weakly and tightly bound metal ions in wild-type and mutant enzymes, metal content, overview
Mn2+
-
manganese-metalloenzyme, binuclear cluster, binding structure
Mn2+
-
activation. after dialysis with EDTA, wild-type and mutant H145N contain 1.1 and 1.3 Mn2+ per subunit, resp., and are hlaf-.active. Mutant H120N contains less than 0.1 Mn2+ per subunit and is inactive
Mn2+
manganese metalloenzyme, each monomer contains two manganese ions
Mn2+
-
binuclear manganese metalloenzyme
Mn2+
increase in enzyme activity by incubation with 5 mM Mn2+ for 10 min at 60°C
Mn2+
manganese metalloenzyme
Mn2+
-
a manganese wash at room temperature is the best condition to purify active enzyme, activity in the presence of 10 mM Mn2+ is at least 15fold higher than in the absence of Mn2+
Mn2+
binuclear manganese metalloenzyme
Mn2+
Pista pacifica
-
activating
Mn2+
-
no effect on rat kidney enzyme
Mn2+
-
dependent on, manganese-metalloenzyme, activates isozyme I, slightly, and isozyme II
Mn2+
-
dependent on, manganese-metalloenzyme, wild-type enzyme contains 1.97 mol Mn2+ per mol of subunit, mutants R308A and R308E contain 2.1 mol, and mutant R308K 1.25 mol per mol of subunit
Mn2+
-
arginase is a better biological catalyst for arginine hydrolysis when both cations are retained and a hydroxide ion is present in the active site bridging the two Mn metal centers
Mn2+
binuclear manganese metalloenzyme
Mn2+
manganese metalloenzyme, Mn2+-Mn2+ cluster in the active site of each monomer
Mn2+
Vigna catjang
-
maximal activity at 0.6 mM
Mn2+
Vigna catjang
-
full activation after preincubation for 8 min at 35°C with 0.6 mM Mn2+
Mn2+
-
required for catalysis, enhances lectin function of enzyme
Mn2+
-
binds one Mn atom per subunit
Mn2+
all recombinant variants are active even in the absence of added Mn2+ but express about2.5-fold increased activity in the presence of 2 mM Mn2+. After extensive dialysis against 25 mM EDTA, they became totally dependent on added Mn2+ for catalytic activity. The manganese-reactivation of all fully inactivated species followed hyperbolic kinetics
Ni2+
-
optimal arginase activity occurrs with nickel at an alkaline pH
Ni2+
-
51% of the activity with Mn2+
Ni2+
-
1 mM, 15% of the activity compared to activity with Mn2+
Ni2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Ni2+
enhances the activity
Ni2+
-
activates slightly, 6.1% of the activity with Co2+
Ni2+
-
6-30% of the activity with Co2+
Ni2+
metal preference in decreasing order: Co2+, Ni2+, Mn2+. Heat-activation in presence of metal ion is essential for activation of apo-enzyme
Ni2+
Vigna catjang
-
55% of the activity with Mn2+
Zn2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Zn2+
Vigna catjang
-
38% of the activity with Mn2+
additional information
-
Fe2+, Ca2+, Mg2+, Zn2+, Cu2+ have no effect on enzyme activity
additional information
-
no activity with Fe2+, Zn2+
additional information
-
metalloenzyme, a metal ion is absolutely required for activity, no activation with Zn2+, Cu2+, Fe2+, Ca2+, and Mg2+
additional information
Ca2+, Na+, K+, Mg2+, and Ni2+ do not show any significant effect on enzyme activity
additional information
Ca2+, Na+, K+, Mg2+, and Ni2+ do not show any significant effect on enzyme activity
additional information
-
Ca2+, Na+, K+, Mg2+, and Ni2+ do not show any significant effect on enzyme activity
additional information
pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I shows that several metal binding ligands are actually quite tolerant to amino acid substitutions. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution
additional information
-
pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I shows that several metal binding ligands are actually quite tolerant to amino acid substitutions. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution
additional information
-
isozymes are not affected by Mg2+ and Ca2+