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2-oxoglutarate
directly stimulates activity
Al3+
results in 8.91tivity compared to Mg2+
Ba2+
increases the activity of wild-type and mutant enzymes at 1 mM
Fe3+
increases the activity of wild-type and mutant enzymes at 1 mM
NH4+
increases the activity of the mutant enzymes at 1 mM
Ca2+
results in 43.9% activity compared to Mg2+
Ca2+
-
stimulates activity at 1 mM
Ca2+
can partially substitute for Mg2+
Ca2+
can substitute for Mg2+ in biosynthesis of glutamine with 30% of the efficiency obtained with Mg2+
Cd2+
-
0.5 mM, activity rises by 96%
Cd2+
-
activates enzyme form EII more than EI
Cl-
-
increases the affinity of the enzyme 2fold to 4fold for Mg2+ or Mn2+
Cl-
chloride stimulates the production of active enzyme by about 300%, in the absence of chloride in the assay buffer, glutamine synthetase activity is decreased by as much as 90%
Cl-
Cl- dependence of glutamine synthetase activity
Cl-
the enzyme's expression partially and activity strictly depends on chloride, strongly salinity-dependent expression of gene glnA2 with a maximal increase of transcripts of about 4fold at 1.5 M NaCl or higher compared to the value at 0.4 M NaCl, expression of glnA1 is not influenced by different salinities, optimal enzyme activity at 2.5 M NaCl or higher, chloride dependent regulatory network, overview
Co2+
results in 109.1% activity compared to Mg2+
Co2+
-
required, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Co2+
-
strongly increases activity in combination with Mg2+
Co2+
-
supports the enzymatic activity
Co2+
-
maximal activity when Co2+ is in excess of ATP
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective
Co2+
-
maximal activity at a ration of ATP to Co2+ of 1.0. The addition of 3 mM Co2+ to the biosynthetic reaction mixtures containing 4 mM Mg2+ results in a 3-7-fold increase in activity
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective
Co2+
-
maximal activity at a ration of ATP to Co2+ of 1.0. The addition of 3 mM Co2+ to the biosynthetic reaction mixtures containing 4 mM Mg2+ results in a 3-7-fold increase in activity
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective
Co2+
-
activates, isoenzyme GS1
Co2+
-
activates, isoenzyme GS2
Co2+
-
can partially replace Mn2+ in transferase reaction
Co2+
increases the activity of the mutant enzymes at 1 mM
Co2+
-
stimulates activity at 1 mM
Co2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Co2+
-
partially effective as activator of biosynthetic activity and transferase activity, half-maximal activation of biosynthetic reaction at 6.3 mM
Co2+
-
at pH 7.2, Mg2+ is more effective than Co2+
Co2+
-
can partially replace Mg2+ in activation
Co2+
enzyme activity is dependent on the presence of divalent cations. Co2+ is able to support activity levels above 50% compared with magnesium in standard conditions of substrates, temperature and pH
Co2+
-
only enzyme form E1 is activated
Cu2+
results in 22.2% activity compared to Mg2+
Cu2+
-
stimulates activity at 1 mM
Cu2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Cu2+
-
partially effective as activator of transferase activity
Fe2+
results in 22.3% activity compared to Mg2+
Fe2+
-
stimulates activity at 1 mM
K+
-
strongly stimulates transferase activity
K+
increases the activity of wild-type and mutant enzymes at 1 mM
K+
-
0.25 mM as optimal concentration for highest activity
Li+
-
50 mM LiCl increases activity
Li+
increases the activity of the mutant enzymes at 1 mM
Li+
-
50 mM LiCl increases activity
Li+
-
50 mM LiCl increases activity
Li+
-
50 mM LiCl increases activity
Mg2+
-
Mg2+
assay in presence of 55 mM Mg2+
Mg2+
-
required, most effective, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Mg2+
-
required, preferred over Mn2+ at alkaline and neutral pH
Mg2+
-
supports the enzymatic activity
Mg2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal when Mg2+ is in excess of ATP
Mg2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal when Mg2+ is in excess of ATP
Mg2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal when Mg2+ is in excess of ATP
Mg2+
-
the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression
Mg2+
the active site of the apoenzyme structure contains only a single Mg2+, rather than Mn2+, ion bound at the n1 position
Mg2+
-
activates, most effectice cation, isoenzyme GS1
Mg2+
-
activates, most effectice cation, isoenzyme GS2
Mg2+
-
can partially replace Mn2+ in transferase reaction
Mg2+
-
maximal activity at a ratio of Mg2+ to ATP of 2
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
-
maximal activity at 30 mM
Mg2+
binding amino acid residues, overview
Mg2+
-
gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated
Mg2+
required, increases the activity of wild-type and mutant enzymes at 1 mM
Mg2+
-
stimulates activity at 1 mM
Mg2+
the activity increases 225% in the presence of 5 mM Mn2+ compared to 50 mM Mg2+
Mg2+
-
required, less efficient than Mn2+
Mg2+
-
optimal ratio of Mg2+ to ATP is 3:1
Mg2+
assay in presence of 55 mM Mg2+
Mg2+
-
assay in presence of 55 mM Mg2+
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
required, two ions bound to enzyme
Mg2+
activation up to 25 mM, inhibition above
Mg2+
to be in its active state, the enzyme requires magnesium or manganese ions, located in three metal sites designated as n1-n3
Mg2+
-
divalent cation required, order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+, Cu2+, Ni2+
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
-
essential activator for biosynthetic activity, half-maximal activation at 18 mM. Partially effective as activator of transferase activity
Mg2+
-
activates, optimum: 15 mM
Mg2+
-
optimal ratio of MgCl2 to ATP is 2:1 at 1 mM ATP, inhibition at more than 20 mM excess of MgCl2 over ATP
Mg2+
-
at pH 7.2, Mg2+ is more effective than Mn2+
Mg2+
clear preference for Mg2+ in glutamine biosynthesis, optimal concentration is 50 mM
Mg2+
-
divalent metal ion required, Mg2+ is most effective. Maximal activation of GS1 at 5 mM and of GS2 at 20 mM
Mg2+
-
Mg2+ in excess of that required for formation of MgATP2- is required for maximal activity
Mg2+
required for activity and for stability
Mg2+
strong inhibition on the Thermotoga maritima activity in extracts of Escherichia coli cells grown in the presence of ammonia
Mg2+
-
required for optimum activity of enzyme from strain SA0, no activation of enzyme from strain SA1
Mg2+
enzyme activity is dependent on the presence of divalent cations. Mg2+ is the most effective cation
Mg2+
-
required, Mg2+ is an integral component of the enzyme glutamine synthetase having both a structural and a catalytic role. Mg2+ is relevant for the posttranslational regulation of the enzyme
Mg2+
-
divalent cation required, enzyme form EI is more active with Mg2+ than with Mn2+, but EII is more active with Mn2+ than Mg2+
Mn2+
results in 17.12% activity compared to Mg2+
Mn2+
-
required, preferred over Mg2+ at acidic pH
Mn2+
-
slight activation, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Mn2+
-
supports the enzymatic activity
Mn2+
required for gamma-glutamylhydroxamate synthetase activity
Mn2+
-
MnCl2 stimulates gamma-glutamyl transferase activity of glutamine synthethase from unshocked cells, no effect on the gamma-glutamyl transferase activity of unshocked cells
Mn2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal at a ratio of ATP to Mn2+ of 1.0
Mn2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal at a ratio of ATP to Mn2+ of 1.0
Mn2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal at a ratio of ATP to Mn2+ of 1.0
Mn2+
-
the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression
Mn2+
-
required for transferase activity
Mn2+
-
maximal synthetase activity occurs when the ratio of Mg2+ to ATP is 2
Mn2+
-
maximal activity at 1 mM
Mn2+
-
required for transferase activity
Mn2+
-
gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated
Mn2+
-
most effective cation for stimulation of activity at 1 mM
Mn2+
the activity increases 225% in the presence of 5 mM Mn2+ compared to 50 mM Mg2+
Mn2+
-
required, highest activity at 0.6-1 mM, higher concentrations inhibitory
Mn2+
-
three enzyme-bound Mn2+ ions, an additional Mn2+ ion makes contacts with Glu196 and the inorganic phosphate
Mn2+
can partially substitute for Mg2+
Mn2+
-
supports activity of adenylylated and deadenylylated enzyme, no other divalent cation can support gamma-glutamyl transferase activity, optimal concentration is 0.3 mM
Mn2+
required, two ions bound to enzyme
Mn2+
to be in its active state, the enzyme requires magnesium or manganese ions, located in three metal sites designated as n1-n3
Mn2+
-
divalent cation required, order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+, Cu2+, Ni2+
Mn2+
-
required for transferase activity
Mn2+
-
required for transferase activity
Mn2+
-
required, optimal concentrations of Mn2+ ions for GSI, GSIII-1, and GSIII-2 activities are 0.25, 0.5, and 1 mM, respectively
Mn2+
-
activates with 11% of the efficiency of the activation with Mg2+, optimum: 3-4 mM
Mn2+
-
at pH 7.2, Mg2+ is more effective than Mn2+
Mn2+
-
optimal concentration is 2 mM, 25% of the maximal activity relative to Mg2+ activation
Mn2+
-
required, optimum concentration around 0.5 mM
Mn2+
-
activity of the low-activity form is higher than that of the high-activity form in the Mn2+-dependent biosynthetic assay
Mn2+
optimal concentration is 1 mM, activates gamma-glutamyltransferase activity, glutamine synthetase type III. Can substitute for Mg2+ in biosynthesis of glutamine with 30% of the efficiency obtained with Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
cannot effectively replace Mg2+
Mn2+
required for activity and for stability
Mn2+
-
required for optimum activity of enzyme from strain SA1, highest activity at 0.3 mM, concentration inhibitory for enzyme from SA0
Mn2+
enzyme activity is dependent on the presence of divalent cations. Mn2+ is able to support activity levels above 50% compared with magnesium in standard conditions of substrates, temperature and pH
Mn2+
-
essential for activity, contains three Mn2+ ions per subunit
Mn2+
-
divalent cation required, enzyme form EI is more active with Mg2+ than with Mn2+, but EII is more active with Mn2+ than Mg2+
Na+
increases the activity of wild-type and mutant enzymes at 1 mM
Na+
3 mM, highest activity
Na+
-
0.5 mM as optimal concentration for highest activity
Na+
-
highest activity at 50 mM
Ni2+
results in 8.92% activity compared to Mg2+
Ni2+
increases the activity of the mutant enzymes at 1 mM
Ni2+
-
stimulates activity at 1 mM
Ni2+
can partially substitute for Mg2+
Ni2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Zn2+
results in 9.58% activity compared to Mg2+
Zn2+
increases the activity of the mutant enzymes at 1 mM
Zn2+
-
stimulates activity at 1 mM
Zn2+
can partially substitute for Mg2+
Zn2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Zn2+
-
partially effective as activator of biosynthetic activity, half-maximal activation at 6.3 mM
additional information
-
Mg2+, Cu2+, Co2+, or Ca2+ cannot substitute for Mn2+
additional information
little or no detectable activity with Mg2+, Ca2+, Co2+ or Fe2+
additional information
-
little or no detectable activity with Mg2+, Ca2+, Co2+ or Fe2+