Ligand Mg2+

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Basic Ligand Information

Molecular Structure
Picture of Mg2+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Mg
Mg2+
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Synonyms:
Magnesium, Magnesium cation, Mg, Mg2 +, Mg2+[side 1], Mg2+[side 2]


Show all pahtways known for Show all BRENDA pathways known for Mg2+

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

In Vivo Product in Enzyme-catalyzed Reactions (14 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Product in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (578 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation, (R)-2,3-butanediol dehydrogenase activity
-
5 mM, 3-5% activation (depending on purification method)
-
stimulates
stimulates the conversion by a factor of 2
-
addition of up to 1 mM MgCl2 stimulates the enzymatic activity 2fold
-
enhances activity of microsomal enzyme
-
dose-dependent stimulation of the thiolytic reaction
1 mM activates
-
8 mM, required for activity
-
5 mM, 6.3fold activation
3 mM, highly dependent on Mg2+
-
required
-
slight stimulation
-
2.5 to 3.5fold activation
-
112% of initial activity
-
required 2.5 mM MgCl2
-
strong decrease of efficiency of oligonucleotide hybridization
-
5 mM, 3.7fold activation, without Mg2+ 33% remaining activity and additionally without D-glucose 6-phosphate 23.1% remaining activity
-
activation of carboxymethylation of 36 kDa subunit of enzyme
-
maximal effect around 2 mM
-
required
-
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
-
1.23fold activation at 1 mM
50 mM, 1.2 fold activation
-
1.65fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 0.25 mM
-
or Mn2+, most efficiently support FAD hydrolysis
-
34% of the activity with Co2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
-
activates
-

Inhibitor in Enzyme-catalyzed Reactions (12345 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
inhibits 19% at 1 mM, reduction reaction
-
slightly inhibitory
-
40% inhibition at 5 mM
-
31.2% inhibition at 10 mM of the reverse reaction
-
1 mM, 0.3% residual activity; 1 mM, 74.3% residual activity
-
0-15% inactivation at 1 mM
-
10 mM inhibits complex formation of ALR 2 with alpha-crystallin, induces ALR 2 aggregation and precipitation
-
73% inhibition at 1 mM
-
6% inhibition at 0.1 mM
-
enzymes MGR I and MGR II
-
83% residual activity at 1 mM
-
acts as an inhibitor above 20 mM
-
strong inhibition of oxidation of 3alpha-hydroxysteroids
-
inhibits the enzyme at high concentrations
-
complete inhibition at 1 mM
33% inhibition at 100 mM
-
inhibits 19% at 1 mM and 31% at 10 mM
-
1 mM, 50% inhibition
-
competitive to Ca2+, Sr2+, or Ba2+, mutants D354N, N355D, and D354N/N355D
-
5 mM, 85% of initial activity
10 mM, 18% inhibition
-
65% inhibition at 0.1 mM
-
50% residual activity at 1 mM
-
65% inhibition at 0.1 mM
-
66% residual activity at 5 mM
-
1 mM, weak inhibition
-
1 mM, 22.8% inhibition
-
2 mM, 91% residual activity
-
concentrations of Mg2+ higher than 1.25 mM inhibit activity strongly (90% of activity lost at 1.75 mM)
-
slight inhibition
-
5 mM, 14% inhibition
-
slight inhibition
-
slight inhibition
-
above 1 mM
-
5 mM Mg2+ inhibits activity by 45%
-
0.001-0.01 mM, complete inhibition
-
5 mM, 14% inhibition
-
15% inhibition at 0.1 mM
-
mitochondrial enzyme
-
0.85% residual activity at 1.0 mM
-
89.93% residual activity at 10 mM
-
1 mM, 25% inhibition
-
inhibitory
-
70% inhibition at 1 mM
-
1 mM, isozyme A, 33% inhibition, isozyme B, 54% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3
-
74% residual activity at 2 mM
-
14% relative activity with 2 mM MgCl2 compared to the activity without metal ions; 2 mM, 14% residual activity
-
89% residual activity at 1 mM
-
inhibits NahF activity by 34%; inhibits NahV activity by 36%
-
1.9fold increased enzyme activity with 1 mM
-
1 mM, 80% loss of activity, possibly due to a decreased dissociation rate of NADH from the enzyme
-
10 mM, about 30% inhibition
-
0.4 M, complete inhibition
1 mM, 12 h, 4C, 24% loss of activity
-
abolishes autophosphorylation of BVR
-
30% inhibition at 1 mM
-
markedly inhibits stimulatory effect of K+
no effect on enzyme activity up to 20 mM, inhibitory above, 40% inhibition at 30 mM
-
65% residual activity at 0.5 mM
-
slight inhibition
-
1 mM, partial inhibition
-
1 mM, partial inhibition
-
0.5 mM, 63% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
-
84.9% residual activity at 10 mM
-
slight inhibition
-
slightly
-
8% inhibition at 0.05 mM
-
2 mM, 81% residual activity
-
slight increase in activity with increasing concentrations of Mg2+ in sodium phosphate buffer, inhibitory in Hepes buffer
-
5 mM, 33% inhibition
-
10 mM, 27% inhibition
-
1 mM, 3% inhibition
-
6 mM, markedly reduces the level of methylation
-
1-10 mM, decrease in methylation rate. 95% inhibition at 10 mM
-
5 mM, 40% inhibition
-
10 mM, 61% inhibition
-
5 mM, mild inhibitory effect, less than 35% reduced activity
-
5 mM, about 5% inhibition
-
inhibits slightly
-
inhibits at low concentrations
-
1 mM, slight inhibition, Dnmt3a; 1 mM, slight inhibition, Dnmt3b
-
28% inhibition by 5 mM
-
above 50 mM
-
almost complete inhibition at 100 mM
-
strong, 5 mM
slightly inhibits the O-methylation of bergaptol
-
slight
-
60% inhibition at 8 mM
-
5 mM chloride salt, strong inhibitory effect, 50-100%, PpSABATH1
-
0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
-