Ligand Co2+

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Basic Ligand Information

Molecular Structure
Picture of Co2+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Co
Co2+
XLJKHNWPARRRJB-UHFFFAOYSA-N
Synonyms:
Cobalt ion

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 + Co2+/in = ADP + phosphate + Co2+/out
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Co2+/in = ADP + phosphate + Co2+/out
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (30 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Co2+ + H+ + H2O2 = Co3+ + H2O
show the reaction diagram
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coproporphyrin III + Co2+ = Co-coproporphyrin III + 2 H+
show the reaction diagram
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ATP + H2O + Co2+/in = ADP + phosphate + Co2+/out
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Co2+/in = ADP + phosphate + Co2+/out
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (41 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
or Mn2+, required
-
1 mM activates
-
slight activation
-
activation
-
no effect on liver enzyme form I, 2fold activation of enzyme form from sublingual gland, inhibition of enzyme form from submandibular gland
-
2.5 to 3.5fold activation
-
extracellular enzyme
-
5 mM, 1.39fold activation
-
2.5 mM, 16% increase in activity
-
1.4fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM
-
slight activation at 1 mM
-
activates
-
stimulates, at 1 mM 168% activity relative to control
-
25% increase of activity at 1 mM
-
the enzyme requires a divalent metal ion (Zn2+ or Co2+)
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activates
-
best activator
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
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phosphoglycerate mutase is upregulated in the cobalt-treated mouse cerebrum
-
less efficient activation than Mg2+
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Inhibitor in Enzyme-catalyzed Reactions (1944 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.9 mM, 61% inhibiton
-
complete inhibition at 1 mM
-
1 mM, 51.9% residual activity; 1 mM, 68.7% residual activity
-
91% inhibition
-
29% inhibition at 1 mM
-
0-15% inactivation at 1 mM
-
inhibition of activity at 10 mM
-
slight inhibition at 1 mM
-
weak
-
activates enzyme MGR I, slightly inhibits enzyme MGR II
-
5 mM, inhibition by less than 30%
-
1 mM, about 50% inhibition
-
79.5% residual activity at 1 mM
-
above 0.5 mM
-
6.8% residual activity at 1 mM
-
80.5% inhibition at 1 mM
-
5 mM, 11% inhibition
-
13.3% inhibition
-
1 mM, 50% inhibition
-
0.02 mM, 75% inhibition
-
88% residual activity at 1 mM
-
91% residual activity at 100 mM
-
slight inhibition
-
25% inhibition at 1 mM
-
5 mM, 80% of initial activity
-
about 56% inhibition at 1 mM
-
partial inhibition at 2 mM
-
inhibits at 1 mM
-
65% inhibition at 0.1 mM
-
85% inhibition at 0.1 mM
-
the addition of 0.005 mM Co2+ does inhibit enzyme activity to 53%
-
1 mM, weak inhibition
-
incubation with Fe2+ plus Co2+ in equimolar concentrations inhibits
-
1 mM,89.2% inhibition
-
1 mM, 92% inhibition
-
2 mM abolishes enzyme activity completely
-
slight inhibition
-
0.4 mM, complete inhibition
-
0.5 mM, strong
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
-
cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process. Cobalt ions do not affect JMJD2A protein level but directly inhibit its demethylase activity. Exposure of both lung carcinoma A-549 cells and bronchial epithelial Beas-2B cells, to CoCl2 at 0.2 mM for 24 h increases methylation of histone H3 lysine residues 4, 9, 27 and 36, i.e. H3K4me3, H3K9me2, H3K9me3, H3K27me3, H3K36me3, as well as ubiquitination of histone H2A and H2B, while it decreases acetylation at histone H4, overview
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95% inhibition at 0.25 mM
-
0.04 mM, about 65% inhibition
-
less than 15% activity at 1 mM
-
0.5 mM, complete inhibition
-
cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process. cobalt ions do not affect JMJD2A protein level but directly inhibit its demethylase activity. Exposure of both lung carcinoma A549 cells and bronchial epithelial Beas-2B cells, to CoCl2 at 0.2 mM for 24 h increases methylation of histone H3 lysine residues 4, 9, 27 and 36, i.e. H3K4me3, H3K9me2, H3K9me3, H3K27me3, H3K36me3, as well as ubiquitination of histone H2A and H2B, while it decreases acetylation at histone H4, overview
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0.2 mM, 40% inhibition
-
inhibits at 5 mM
-
slightly, sMMO
slight effect, crude enzyme extract
-
63% residual activity at 1 mM
-
0.4 mM, significant inhibition
-
1 mM inhibits by 20%; 20% inhibition at 1 mM
-
62.4% inhibition at 0.5 mM
-
80% inhibition at 0.1 mM
-
0.4 mM, 100% inhibition
-
completely abolishes activity of WelO5 toward 12-epi-fischerindole U
-
40% inhibition at 0.1 mM
-
mitochondrial enzyme
-
RNR activity chelates with copper leading to inactivation
-
1 mM, 29% inhibition
-
1 mM, isozyme A, 71% inhibition, isozyme B, 51% inhibition, complete inhibition of isozyme A from pyridoxine auxotroph mutant strain WG3
-
30-40% inhibition at 1.0 mM
-
1 mM, enzyme a and e
-
50% inhibition at 2.5 mM
-
42% residual activity at 2 mM
-
89% residual activity at 1 mM
-
1 mM, 40.2% inhibition
-
both isoforms, concentration above 3 mM
-
1 mM, 1.5% residual activity
-
weakly inhibits
-
only after preincubation with cation
-
complete inhibition at 1 mM
-
inhibition above 5 mM
-
inhibitory
-
34% residual activity at 0.5 mM
-
slight inhibition
-
82% activity in the presence of 1 mM Co2+
-
0.5 mM, 71% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
-
15% residual activity at 1 mM
-
there is a sharp decrease in activity when 1 mM Co2+ is added to the reaction assay
-
strong inhibition
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
-
5 mM, 65% inhibition
-
almost total inhibition at 0.1 mM
-
1 mM, about 10% inhibition
-
strong inhibition at 1 mM
-
0.1 mM, 31% inhibition
-
0.5 mM
-
1 mM, strong inhibition
-
not inhibitory at 1 mM
-
strong inhibition
-
5 mM
-
1 mM, 22% inhibition
-
1 mM, 87% inhibition
-
5 mM, 39% inhibition
-
strong inhibition
-
strongly inhibits, relative activity 7% of control
-
1 mM, 20-50% inhibition
-
5 mM, 53% inhibition
-
53% inhibition at 5 mM
-
53% inhibition at 5 mM
-
0.1 mM, 44% residual activity
divalent cations at concentrations of more than 5 mM are inhibitory, 10 mM, total inhibition
-
partial inhibition
-
slight
-
5 mM, strong inhibition
-
5 mM, strong inhibition
-
1 mM, 83% inhibition
-
strong, above 5 mM
-
22% inhibition at 2 mM
-
1 mM, 87% inhibition
-
5 mM, strong
-
0.05 mM, 20% loss of activity
-
strong, 1 mM, even in the presence of Mn2+, wild-type
-
in the presence of Mn2+
-
the additon of 2.5 mM of Co2+ slightly inhibits the enzyme
-
60% inhibition at 1 mM
-
strong inhibition at 1 mM and 10 mM
-
over 90% inhibition
-
about 30% residual activity at 10 mM; about 35% residual activity at 10 mM
-
10 mM, 54.2% inhibition
-
69% inhibition
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
1 mM, 80% inhibition
-
about 90% residual activity in the presence of 2 mM
-
32% inhibition at 1 mM
-
1 mM, 31% residual activity
-
43% inhibition at 1 mM
-
the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 45%; the addition of 5 mM Co2+ reduces the activation by 5 mM MnCl2 of the enzyme by 76%
-
8.2% residual activity at 5 mM
-
above 5 mM
-
25 mM, 1% residual activity
-
complete inhibition at 5 mM
-
6 mM: 50% inhibition
-
20 mM, 98% inhibition
-
inhibits at high concentrations, inhibits Mn2+-activated enzyme
-
less than 20% residual activity at 2 mM
-
in the presence of Mn2+
-
0.25 mM CoCl2, 12.7% inhibition
-
inhibits Mg2+-activation
-
Co2+ reduces activity by more than 60% at 5 mM
-
10 mM
-
20 mM, 85% loss of activity
-
1 mM, 96% inhibition
-
10 mM CoCl2, 44% inhibition
-
0.1-1 mM, complete inhibition
-
5 mM, 50-80% inhibition
-
complete inhibition at 1 mM
-
stabilizes at low and inhibits at higher concentrations
-
1 mM, 15% decrease of activity
-
about 45% residual activity at 10 mM
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
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order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
-
weak inhibition
-
0.004 M, 80% inhibition
-
above 6 mM
-
1.6 mM, 40% inhibition; 1.6 mM, 61% inhibition
-
200 mM
-
complete inhibition at 20 mM
-
2 mM, 58% inhibition, even in presence of optimal Mg2+ concentrations
-
above 0.1 mM
-
weak, NDP-arsenolysis or NDP/phosphate-exchange reaction
-
inhibits uridylyl removing activity
-
moderate inhibition
-
at high concentration inhibits the phosphoenolpyruvate, pyruvate exchange reaction
-
inhibits the synthesis of s4U
-
slight inhibition at 1 mM
-
1 mM, almost complete inhibition
-
isoenzyme BSS II
-
slight inhibition at 2 mM
-
at low concentration
-
strong inhibition
-
sensitive to metal ions, almost complete inhibition at 6.0 mM
-
52% residual activity at 100 mM
-
47% residual activity at 1 mM
-
10.7% residual activity at 1 mM
-
43% inhibition at 2 mM
-
low inhibition at 1 mM
-
pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition
-
1.0 mM, 68% relative residual activity
-
5 mM, 23% inhibition
-
3 mM gradually decreases activity about 78fold
-
slightly inhibits the mitochondrial enzyme
-
slightly inhibits the mitochondrial enzyme
-
complete inhibition at 1 mM
-
almost complete inhibition of 3'-AMP hydrolysis by 1 mM CoCl2
-
0.1 mM, 80% inhibition
-
no activity with
-
80.6% inhibition at 2 mM
-
1.0 mM, complete inhibition of isoenzyme PII, 21% inhibition of isoenzyme PI
-
18% inhibition at 0.1 mM
-
40% residual activity
-
53% residual activity at 10 mM
-
2 mM, 15% of initial activtiy
-
4 mM, 32% inhibition
-
1 mM, 22% inhibition
-
1 mM, 37% loss of activity
-
1 mM, 15% of initial activity
-
50% inhibition at 50 mM for beta-D-fucosidase I, 22% inhibition for beta-D-fucosidase II
-
complete inhibition at 5 mM
-
10 mM cause 37% inhibition
-
29% inhibition at 5 mM
-
F1 and F2 form 47% inhibition
-
about 18% residual activity at 1 mM
-
1 mM, strong inhibition
-
complete inhibition at 1 mM
-
moderate inhibition at 1 mM
-
5 mM, 12% inhibition
-
10 mM, 75% inhibition
-
5 mM, 18% inhibition
-
1 mM, 14% inhibition
-
mixed-type inhibition
-
24.2% residual activity at 0.1 M using inosine as substrate, 25.8% residual activity at 0.1 M using guanosine as substrate, 33.3% residual activity at 0.1 M using adenosine as substrate
-
complete inhibition at 5 mM
-
above 3-7 mM
-
1 mM, complete inhibition
-
25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM
65-90% inhibition at 1 mM
-
7-DMATS, FgaPT1, and CdpNPT show 10.2%, 32.3%, and 46.9% relative activity at 5 mM Co2+, respectively
-
1 mM, 50% residual activity
-
1 mM, 10% inhibition
-
activation up to 50% at 0.001-0.0001 mM, inbhibitory above 0.002 mM
-
partial
-
at 0.01 mM 59.7% activity relative to control
-
hydrolysis of hippuryl-L-Arg
-
1 mM, 71% inhibition
-
at 37°C and pH of 7.5, 1 mM reduces prosubtilisin JB1 relative activity to 14% and 5 mM reduces prosubtilisin JB1 relative activity to 24%
-
inhibition of amidolytic activity
-
competitive to other metal ions
-
inhibits at 2 mM
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+, 50% inhibition at 0.25 mM
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
-
0.05 mM
-
strong inhibition
-
5.09% residual activity at 5 mM
-
6.85% residual activity at 5 mM
-
inhibits 74% at 0.2 mM and precipitates the enzyme at 1 mM
-
inhibitory below 5 mM
-
10 mM, complete inhibition
-
0.1 mM, caseinolytic activity
-
50% inhibition at 0.625 mM
-
protease II inactive in presence of, protease I slightly stimulated
-
above 1-2 mM, native or apoenzyme
-