Ligand manganese(2+)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Basic Ligand Information

Molecular Structure
Picture of manganese(2+) (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Mn
manganese(2+)
WAEMQWOKJMHJLA-UHFFFAOYSA-N
Synonyms:
manganese(II), Mn(II), Mn2+, Mn2+/cis, Mn2+/trans, Mn2+[side 2]
Pathway Source
Pathways

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-

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

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-
-
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-
-
ATP + H2O + Mn2+[side 1] = ADP + phosphate + Mn2+[side 2]
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (126 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Mn2+ + H2O2 = ?
show the reaction diagram
-
deuteroporphyrin + Mn2+ = ? + H+
show the reaction diagram
-
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-
-
ATP + H2O + Mn2+/out = ADP + phosphate + Mn2+/in
show the reaction diagram
-
-
ATP + H2O + Mn2+[side 1] = ADP + phosphate + Mn2+[side 2]
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (166 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation, (R)-2,3-butanediol dehydrogenase activity
-
activating effect is limited to peptide substrate with vicinal glutamyl residues
-
or Co2+, required
-
1 mM activates
-
2-4fold activation of sucrose synthesis, inhibition of cleavage
-
at 10 mM activity increases 2fold
-
slight activation
-
can partially replace Mg2+ in activation
-
activation
-
significantly enhances the binding of nucleotide to primase,which correlates with higher catalytic efficiency in vitro
-
strong activation of both isozymes
-
2.5 to 3.5fold activation
-
10% activation of recombinant BioHs at 10 mM
-
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
-
5 mM, 4.4fold activation
-
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
5 mM, 1.43fold activation
-
3 mM, 18% increase in activity
-
the enzyme is activated by 51% at 5 mM
-
1 mM, 155% of initial activity
-
41% activation at 1 mM
-
activates
-
1 mM, 105% of inital activity
-
1.2fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM
-
2 mM, slight activation
-
or Mg2+, most efficiently support FAD hydrolysis
-
isoenzyme HODHI is inhibited, isoenzyme HODHII is activated
-
1.4-2fold increase in activity of oligoalginate lyase at 1 mM
-
stabilization of enzyme
-
activates
-
Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
-
less efficient activation than Mg2+
-

Inhibitor in Enzyme-catalyzed Reactions (4863 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
slightly inhibitory
-
1 mM: weak
-
25% inhibition at 5 mM
-
31.3% inhibition at 50 mM of the reverse reaction
-
46% inhibition at 1 mM
-
1 mM, 14.3% residual activity; 1 mM, 23.4% residual activity
-
29% inhibition
-
0-15% inactivation at 1 mM
-
84% residual activity at 1 mM
-
slight inhibition
-
93% inhibition of activity at 10 mM
-
slight inhibition at 1 mM
-
1 mM completely inactivates the enzyme
-
enzymes MGR I, MGR II
-
inhibitory above 1 mM
-
25 mM, 95% inhibition
-
weak inhibition at 2.5 mM
-
inhibits the reductive carboxylation reaction, inhibitory effect is about 20fold reduced by binding of fumarate and L-malate
-
81.1% residual activity at 1 mM
-
50% inhibition at 36.6 mM
-
with acetolactate as substrate, Mn2+ behaves as a competitive inhibitor in presence of Mg2+
8.4% residual activity at 1 mM
-
21% activation at 1 mM, and 61% inhibition at 10 mM
-
1 mM complete inhibition
-
50% inhibition at 10 mM
slight
-
7% inhibition at 1 mM
-
slight inhibitory effect
-
complete inhibition at 1 mM
-
inhibits activity at 0.01 mM
-
marked inhibition at 1 mM
-
85% 92% inhibition at 2 mM, in the presence of 3 mM ATP
-
10 mM, 97% inhibition
-
95% inhibition at 0.1 mM
-
95% inhibition at 0.1 mM
-
1 mM, weak inhibition
-
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enyzme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate
-
1 mM, 65.5% inhibition
-
inhibits by 13% at 5 mM
-
2 mM, 31% residual activity
-
slight inhibition
-
0.5 mM, strong
-
causes a 20-30% fall in activity
-
60% inhibition at 0.25 mM
-
0.04 mM, about 80% inhibition
-
less than 15% activity at 1 mM
-
slight inhibition
-
slight inhibition
-
1 mM, moderate inhibition
-
complete inhibition at 5 mM
-
complete inhibition at 5 mM
-
0.001-0.01 mM, complete inhibition
-
50% inhibition at 0.01 mM
-
50% inhibition at 0.01 mM
-
0.4 mM, 95% inhibition
-
completely abolishes activity of WelO5 toward 12-epi-fischerindole U
-
weak inhibition
-
mitochondrial enzyme
-
inhibitory
-
1 mM, isozyme A, 20% inhibition, isozyme C, 44% inhibition
-
50% inhibition at 10 mM
-
30-40% inhibition at 1.0 mM
-
84.8% residual activity at 1 mM
50% inhibition at 0.024 mM
-
slight
-
inhibits and activates
-
21% residual activity at 2 mM
-
partial
-
1 mM causes 37% inhibition
-
89% residual activity at 1 mM
-
10 mM, about 30% inhibition
-
1 mM, 12 h, 4°C, 44% loss of activity
-
1 mM, 15.2% inhibition
-
1 mM, about 65% of initial activity
-
1 mM: less than 20% inhibition
-
only after preincubation with cation
-
complete inhibition at 1 mM
-
markedly inhibits stimulatory effect of K+
-
inhibition above 5 mM
-
has no significant effect on enzyme activity up to 10 mM
-
1 mM, 72% inhibition of the recombinant enzyme
-
10 mM, 60% inhibition of reductive amination
-
1 mM, 60% inhibition
-
0.5 mM, 52% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
-
about 65% residual activity at 1 mM
-
5 mM, 45% inhibition
-
almost total inhibition at 0.1 mM
-
30% inhibition at 1 mM
-
moderate inhibition
-
; 67% residual activity at 2 mM
-
0.1 mM, about 20% inhibition
-
0.1 mM, about 20% inhibition
-
not inhibitory at 1 mM
-
complete inhibition of nitrite synthesis at 0.1 mM; complete inhibition of the oxidation of HNO to NO at 0.001 mM, inhibition of HNO2 synthesis is the same at pH 6,7,8 and 9
-
strong inhibition
-
5 mM MnSO4, 82% loss of activity
-
35% inhibition at 1 mM
-
moderate inhibition
-
1 mM, 59% inhibition
-
inhibits activity by 41%, inhibition prevented by inclusion of 10 mM EDTA; inhibits TNMT activity by 41%, can be prevented by the inclusion of EDTA
-
5 mM
-
above 1 mM
-
1 mM: 21% inhibition, 10 mM: 57% inhibition
-
1 mM, 48% inhibition
-
1 mM, 79% residual activity
-
5 mM, complete inhibition
-
2.5 mM, 35% inhibition
-
5 mM, about 15% inhibition
-
4-fold decrease of enzyme activity
-
inhibits at low concentrations
-
strong inhibition, Dnmt3a; strong inhibition, Dnmt3b
-
1 mM, 43% inhibition
-
26% inhibition by 5 mM
-
relative activity 24% of control
-
5 mM chloride salt, strong inhibitory effect, 50-100%, PpSABATH1
-
5 mM, 31% inhibition
-
31% inhibition at 5 mM
-
31% inhibition at 5 mM
-
strong inhibition at 1 mM
-
0.1 mM
-
20 mM, 50-60% inhibition
-
35% inhibition at 2 mM
-
2 mM, 82% residaul activity; slightly decreases activity, relative activity: 81.5% (2 mM)
-
2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity
-
slight
-
73% inhibition at 2.5 mM
-
85.5% inhibition at 2.5 mM, inhibition of Mg2+ and bovine serum albumin is antagonistic
-
2 mM, 80% inhibition
-
in crude enzyme extract
-
50% inhibition above 10 mM
-
weak
-
relative activity: 71%
-
strong, above 5 mM
-
50% inhibition at 5 mM
-
weak
-
40% inhibition at 2 mM
-
5 mM, 16% residual activity
-
above 25 mM
-
slight inhibition
-
0.1-10 mM: 20-80% inhibition
-
40.9% residual activity at 1 mM, complete inhibition at 10 mM
-
above 10 mM, wild-type
-
at high concentration
-
2 mM, 20% inhibition
-
the additon of 2.5 mM of Mn2+ slightly inhibits the enzyme
-
45% inhibition at 10 mM
-
weak effect
-
at concentrations above 40 mM
-
10 mM, 24.7% inhibition
-
5 mM, 82% loss of activity
-
10% inhibition at 1 mM
-
strong inhibition at 5 mM
-
47.41% residual activity at 5 mM
-
above 2.5 mM
-
inhibitory in presence of optimal Mg2+-concentration
-
20 mM, 40% inhibition below pH 8.0
-
soluble enzyme, above 50 mM
-
slight inhibition
-
moderate inhibitory effect
-
1 mM, 80.3% inhibition
10 mM
-
above 10 mM
-
10 mM, 98% inhibition
-
reduces base exchange activity by 87-99% at 1 mM
-
weak
-
90% inhibition at 5 mM
-
inhibitory above 5 mM
-
5 mM, 6% activity
-
required, activates up to 5 mM, inhibitory above 5 mM
-
above 2 mM
-
weak
-
optimal at 0.1 mM, the enzyme absolutely requires a divalent cation, inhibition by Mn2+ at higher concentration of 5.0 mM
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
-
reduced activity
-
enzyme is inhibited by an excess of free divalent metal ion, Mg2+ or Mn2+
-
above 6 mM
-
about 70% activity at 2.5 mM
-
50 mM inhibit
-
3.5 mM, instead of Mg2+, almost complete inhibition
-
activates the protein phopshorylation, but inhibits the inositol-1,3,4-trisphosphate 5/6-kinase reaction
-
1.6 mM, 50% inhibition
-
93% activity in the presence of 10 mM Mn2+ compared to Mg2+
-
abolishes detectable DAG kinase activity
-
200 mM
-
strong inhibition above 1 mM
-
5 mM, 80% loss of activity
-
above 1 mM
in excess, activating below
-
excess free divalent cations inhibit the enzyme
-
can partially replace Mg2+ in activation, inhibition above 0.5 mM at 1 mM ATP
-
inhibits forward reaction above 0.5 mM
-
divalent cation required, most effective at a ratio of Mn2+ and ATP of 1:3, deviation from this ratio is inhibitory at several concentration levels
-
21% residual activity at 3 mM
-
complete inhibition at 0.01 M
-
at a Mn2+/ATP ratio of more than 2
-
at 1 mM, in presence of 1 mM Mg2+, strong inhibition, but activation in absence of Mg2+
-
at 1 mM or above
-
inhibitory above 1 mM
-
above 20 mM
-
at high concentrations noncompetitive inhibition of MgATP2-
-
1.67 mM, 49% inhibition
-
slight inhibition
-
complete inhibition above 0.4 mM
-
5 mM
-
53% of the activation with Mg2+, excess of Mn2+ inhibits the reaction in both directions
-