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Ligand Mg2+
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Basic Ligand Information
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Show all BRENDA pathways known for Mg2+
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + H+
ATP + deuteroporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-deuteroporphyrin IX + H+
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+
ATP + H2O + Mg2+/out = ADP + phosphate + Mg2+/in
289130, 289131, 289132, 289133, 289136, 689037, 699248, 686901, 696384, 289134, 695972, 696596, 686274, 701311, 686381, 687696, 685621, 686644, 687845, 689150, 699121, 698035, 697187, 700902
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ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
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In Vivo Product in Enzyme-catalyzed Reactions (14 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Mg2+/out = ADP + phosphate + Mg2+/in
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Substrate in Enzyme-catalyzed Reactions (7 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + H+
ATP + deuteroporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-deuteroporphyrin IX + H+
ATP + deuteroporphyrin + Mg2+ + H2O = ADP + phosphate + Mg-deuteroporphyrin + H+
ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+
ATP + H2O + Mg2+/out = ADP + phosphate + Mg2+/in
289135, 289130, 289131, 289132, 289133, 289136, 689037, 699248, 686901, 696384, 699121, 289134, 695972, 696596, 698035, 719452, 700902, 686274, 701311, 686381, 687696, 685621, 686644, 668575, 687845, 689150, 697187
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ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
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Product in Enzyme-catalyzed Reactions (18 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Mg2+/out = ADP + phosphate + Mg2+/in
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Activator in Enzyme-catalyzed Reactions (582 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
stimulates enzyme activity
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Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
5 mM, 3.7fold activation, without Mg2+ 33% remaining activity and additionally without D-glucose 6-phosphate 23.1% remaining activity
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Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
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1.65fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 0.25 mM
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stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
stimulates activity with increasing amounts from 5 mM (14%) to 20 mM (57%)
Inhibitor in Enzyme-catalyzed Reactions (12787 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
10 mM inhibits complex formation of ALR 2 with alpha-crystallin, induces ALR 2 aggregation and precipitation
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activates at up to 4 mM, inhibition above, probably due to blockage of substrate binding, Km is 0.19 mM
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in the presence of 2 mM Mg2+, the rate of H2O2 removal is inhibited by 60%, 5% and 5% when it is assayed with 2 mM ADP, AMP or phosphate, respectively, total inactivation of 2-Cys Prx is caused by incubation with 3 mM ATP and 3 mM Mg2+
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1 mM, inhibits the free enzyme by 9%, no inhibition of the immobilized enzyme by Mg2+
1 mM, inhibits the free enzyme by 9%, no inhibition of the immobilized enzyme by Mg2+
1 mM, inhibits the free enzyme by 9%, no inhibition of the immobilized enzyme by Mg2+
1 mM, inhibits the free enzyme by 9%, no inhibition of the immobilized enzyme by Mg2+
concentrations of Mg2+ higher than 1.25 mM inhibit activity strongly (90% of activity lost at 1.75 mM)
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1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
1-5 mM, 10-20% inhibition of GDP reduction; inhibition of CDP reduction
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
1 mM, isozyme A, 33% inhibition, isozyme B, 54% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3
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Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
wild type enzyme activity is inhibited (64%) by Mg2+ at pH 7.4, whereas the GFP-tagged enzyme activity is not affected by Mg2+
about 50% inhibition of all-trans- and 9-cis-retinal oxidation above 1 mM
about 50% inhibition of all-trans- and 9-cis-retinal oxidation above 1 mM
about 50% inhibition of all-trans- and 9-cis-retinal oxidation above 1 mM
14% relative activity with 2 mM MgCl2 compared to the activity without metal ions; 2 mM, 14% residual activity
-
1 mM, 80% loss of activity, possibly due to a decreased dissociation rate of NADH from the enzyme
-
near 75% of the activity is lost when 5 mM Mg2+ is included in the incubation medium
-
no effect on enzyme activity up to 20 mM, inhibitory above, 40% inhibition at 30 mM
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20 mM, 50% inhibition at pH 7.0, competitive vs. NADPH and thio-NADP+, noncompetitive vs. acetylpyridine adenine dinucleotide and NADH
-
5 mM, 70% inhibition of the low activity form, no inhibition of high activity form, inhibition is prevented by low concentrations of thiol compounds
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native protein, highly sensitive to Mg2+, recombinant protein, not sensitive. Recombinant protein plus enzyme-free leaf extract of Ricinus communis shows restored high sensitivity to Mg2+, but remains unresponsive to ATP
-
5 mM MgCl2 decreases enzyme activity at pH 7.5, this effect is completely reversed by the addition of EDTA into samples returning the enzyme's activity to its initial level
-
slight increase in activity with increasing concentrations of Mg2+ in sodium phosphate buffer, inhibitory in Hepes buffer
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0.5 mM, 80% residual activity