Any feedback?
Please rate this page
(ligand.php)
(0/150)

BRENDA support

Ligand Co2+

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 Co2+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Co
Co2+
XLJKHNWPARRRJB-UHFFFAOYSA-N
Synonyms:
Cobalt ion, cobalt nanoparticle


Show all pahtways known for Show all BRENDA pathways known for Co2+

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (20 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
-

In Vivo Product in Enzyme-catalyzed Reactions (5 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
-

Substrate in Enzyme-catalyzed Reactions (41 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Co2+ + H+ + H2O2 = Co3+ + H2O
show the reaction diagram
-
coproporphyrin III + Co2+ = Co-coproporphyrin III + 2 H+
show the reaction diagram
-
ATP + H2O + Co2+/in = ADP + phosphate + Co2+/out
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (9 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Co-heme + NADPH + H+ + O2 = biliverdin Ixalpha + Co2+ + CO + NAD+ + H2O
show the reaction diagram
-
Co2+-protoporphyrin + H+ = protoporphyrin + Co2+
show the reaction diagram
-
ATP + H2O + Co2+/in = ADP + phosphate + Co2+/out
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (46 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, about 90% inhibition
-
1 mM, 111% of initial activity
-
or Mn2+, required
-
1 mM activates
-
slight activation
-
cobalt nanoparticles with particle size less than 50 nm significantly activate the enzyme in the serum, liver, and kidney of rats at concentration-dependent order with a maximum activation of 175% at 10 mM
-
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
-
activates
-
1.4fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM
-
20.6% activation at 1 mM
slight activation at 1 mM
-
2 mM, slight activation
-
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+)
-
activates
-
best activator
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
-
phosphoglycerate mutase is upregulated in the cobalt-treated mouse cerebrum
-
less efficient activation than Mg2+
-

Inhibitor in Enzyme-catalyzed Reactions (2253 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
-
29% inhibition at 1 mM
-
0-15% inactivation at 1 mM
-
1 mM, 81.9% residual activity
-
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
-
1 mM complete inhibition
-
13.3% inhibition
-
1 mM, 72% inhibition
-
1 mM, 50% inhibition
-
5 mM, complete inhibition of activity
-
0.02 mM, 75% inhibition
-
88% residual activity at 1 mM
-
91% residual activity at 100 mM
-
slight inhibition
-
25% inhibition at 1 mM
-
inhibits the enzyme at 1-10 mM
-
5 mM, 80% of initial activity
-
partial inhibition at 2 mM
-
1.3 mM, 30 min, 24% loss of activity
-
inhibits at 1 mM
-
65% inhibition at 0.1 mM
-
85% inhibition at 0.1 mM
-
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
-
0.4 mM, complete inhibition
-
0.5 mM, strong
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
-
95% inhibition at 0.25 mM
-
0.04 mM, about 65% inhibition
-
less than 15% activity at 1 mM
-
more than 50% decrease in activity
-
0.5 mM, complete inhibition
-
has an activating on multiple histone modifications at the global level. Cobalt ions significantly increase global histone H3K4me3, H3K9me2, H3K9me3, H3K27me3 and H3K36me3, as well as uH2A and uH2B and decreases acetylation at histone H4 (AcH4) in vivo. Cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process in vivo. And cobalt ions directly inhibit demethylase activity of JMJD2A in vitro. Cobalt ions do not increase the level of uH2A in the in vitro histone ubiquitinating assay and inhibit histone-deubiquitinating enzyme activity in vitro
-
has an activating on multiple histone modifications at the global level. Cobalt ions significantly increase global histone H3K4me3, H3K9me2, H3K9me3, H3K27me3 and H3K36me3, as well as uH2A and uH2B and decreases acetylation at histone H4 (AcH4) in vivo. Cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process in vivo. And cobalt ions directly inhibit demethylase activity of JMJD2A in vitro. Cobalt ions do not increase the level of uH2A in the in vitro histone ubiquitinating assay and inhibit histone-deubiquitinating enzyme activity in vitro
-
0.2 mM, 40% inhibition
-
inhibits at 5 mM
-
inhibits the enzyme activity at 0.5 mM by about 30%
-
1 mM, 80% residual activity
-
slightly, sMMO
slight effect, crude enzyme extract
-
63% residual activity at 1 mM
-
67% inhibition
-
0.4 mM, significant inhibition
-
1 mM inhibits by 20%; 20% inhibition at 1 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
-
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
-
40-50% inhibition
-
1 mM, 1.5% residual activity
-
weakly inhibits
-
1 mM, 14.2% loss of activity
-
only after preincubation with cation
-
complete inhibition at 1 mM
-
inhibition above 5 mM
-
inhibitory
-
34% residual activity at 0.5 mM
-
slight inhibition
-
34% residual activity at 0.5 mM
-
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
-
2 mM, 15% loss of activity
-
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
-
slight inhibition
-
53% residual activity at 2 mM
-
20 mM, 14% residual activity
-
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
-
1 mM, 66.3% residual activity
-
5 mM, 9% inhibition
-
5 mM
-
1 mM, 22% inhibition
-
1 mM, 87% inhibition
-
complete inhibition at 20 mM
-
5 mM, 39% inhibition
-
complete inhibition
-
strong inhibition
-
about 20 % residual activity at 5 mM
-
strongly inhibits, relative activity 7% of control
-
1 mM, 20-50% inhibition
-
complete inhibition
-
complete loss of activity
-
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
-
complete inhibition at 1 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+
-
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
-
about 68% residual activity 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+
-
less than 4% activity in the presence of Co2+ions
-
0.25 mM CoCl2, 12.7% inhibition
-
inhibits Mg2+-activation
-
Co2+ reduces activity by more than 60% at 5 mM
-
20 mM, 85% loss of activity
-
1 mM, 96% inhibition
-
10 mM
-
10 mM CoCl2, 44% inhibition
-
strong inhibition at 5 mM
-
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
-
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
-
the enzyme shows clearly reduced activity (11.5%) with Co2+
-
complete inhibition at 20 mM
-
65% residual activity in the presence of 4 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
-
60% inhibitin at 10 mM
-
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
-
can replace Ca2+, decreased activity
-
low inhibition at 1 mM
-
pH 5.3: stimulates, optimal concentration: 80 mM, pH 9.3: inhibition
-
1.0 mM, 68% relative residual activity
-
45% inhibition at 1 mM
-
5 mM, 50% inhibition
5 mM, 23% inhibition
-
significant inhibition of the intracellular enzyme, and slight inhibition of extracellular enzyme at 5 mM
-
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
-
about 60% residual activity at 1 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
-
1 mM, 61% loss of activity
-
29% inhibition at 5 mM
-
F1 and F2 form 47% inhibition
-
about 18% residual activity at 1 mM
-
0.8fold decrease of activity at 10 mM
-
1 mM, strong inhibition
-
90% residual activity at 5 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
-