Ligand nickel(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 nickel(2+) (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Ni
nickel(2+)
VEQPNABPJHWNSG-UHFFFAOYSA-N
Synonyms:
Ni, Ni(2+), Ni2+, Ni2+[side 2], Nickel

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
sirohydrochlorin + Ni2+ = Ni-sirohydrochlorin + 2 H+
show the reaction diagram
-
ATP + H2O + Ni2+/out = ADP + phosphate + Ni2+/in
show the reaction diagram
ATP + H2O + Ni2+/in = ADP + phosphate + Ni2+/out
show the reaction diagram
-
ATP + H2O + Ni2+/out = ADP + phosphate + Ni2+/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
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide = pyridinium-3,5-bisthiocarboxylate mononucleotide + Ni2+
show the reaction diagram
-
ATP + H2O + Ni2+/in = ADP + phosphate + Ni2+/out
show the reaction diagram
-
-
ATP + H2O + Ni2+/out = ADP + phosphate + Ni2+/in
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (8 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
sirohydrochlorin + Ni2+ = Ni-sirohydrochlorin + 2 H+
show the reaction diagram
-
coproporphyrin III + Ni2+ = Ni-coproporphyrin III + 2 H+
show the reaction diagram
-
ATP + H2O + Ni2+/out = ADP + phosphate + Ni2+/in
show the reaction diagram
ATP + H2O + Ni2+/in = ADP + phosphate + Ni2+/out
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide = pyridinium-3,5-bisthiocarboxylate mononucleotide + Ni2+
show the reaction diagram
-
ATP + H2O + Ni2+/in = ADP + phosphate + Ni2+/out
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (121 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
stimulates
-
1 mM, activation to 144% of control
-
10 mM, activation to 113% of control
-
may replace Mg2+/Mn2+ but with lower catalytic efficiencies
-
39% of the activity with Co2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
-
less efficient activation than Mg2+
-

Inhibitor in Enzyme-catalyzed Reactions (1540 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
strong inhibition
-
2 mM, 75% inhibition, complete reversion with 5 mM EDTA
-
84% inhibition at 2 mM
-
1 mM, 18.2% residual activity; 1 mM, 72.7% residual activity
-
29% inhibition at 1 mM
-
0-15% inactivation at 1 mM
-
0.5 mM, 54% inhibition
-
slight inhibition
-
slight inhibition at 1 mM
-
0.5 mM, strong inhibition
-
enzyme MGR I
-
strong inhibition at 0.5 mM
-
1 mM, about 60% inhibition
-
about 50% activity at 0.5 mM
-
about 95% residual activity at 2 mM
-
10-20% inhibition
-
inhibits the enzyme at high concentrations
-
14% residual activity at 1 mM
-
50% inhibition at 31.66 mM; 50% inhibition at 31.7 mM
-
11.3% residual activity at 1 mM
-
inhibits 39% at 1 mM and 63% at 10 mM
-
28.6% inhibition
-
slight
-
1 mM, 50% inhibition
-
complete inhibition at 1 mM
-
15% inhibition at 1 mM
-
some authors found inhibition, others not
-
0.5-1 mM, strong inhibition of artificial electron acceptor reduction
-
inhibits at 1 mM
-
10 mM, 28% inhibition
-
1 mM, strong inhibition
-
strong
-
1 mM, strong inhibition
-
incubation with Fe2+ plus Ni2+ in equimolar concentrations inhibits
-
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, 87.5% inhibition
-
2 mM abolishes enzyme activity completely
-
1 mM, 49% of initial activity
-
inhibits the light emission by dinoflagellate luciferase
-
0.5 mM, strong
-
IC50: 0.00071 mM, in the presence of Fe2+; IC50: 0.032 mM
-
competitive versus Fe2+
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
-
more than 50% inhibition at 1 mM
-
95% inhibition at 0.25 mM
-
20% residual activity at 1 mM
-
atalytic activity is affected by Ni2+. A significant reduction of activity is observed when the protein is purified using Ni-NTA column. The activity can be restored by dialysis of the protein in a buffer solution containing 0.1 mM EDTA, followed by the addition of 0.2 mM of Fe2+ to the protein solution
-
binding structure with truncated enzyme mutant
-
substitutes Fe2+ and inhibits the hydroxylation reaction
-
25% inhibition compared to the activity without any metal
-
0.1 mM, 21% residual activity
-
slight effect, crude enzyme extract
-
4% residual activity at 1 mM
-
ionic or uncomplexed Ni2+ (2 mM) is inhibitory to the enzyme
-
0.1 mM inhibits by 79%, 1 mM completely inhibits; complete inhibition at 1 mM
-
severely inhibits enzyme activity
-
inhibition in decreasing order, Zn2+, Co2+, Ni2+
-
completely abolishes activity of WelO5 toward 12-epi-fischerindole U
-
0.76% residual activity at 1.0 mM
-
1 mM, 30% inhibition
-
inhibitory
-
complete inhibition at 1 mM
-
30-40% inhibition at 1.0 mM
-
slight
-
12% inhibition in the presence of 1 mM
-
100% inhibition at 0.1 mM
-
25% residual activity at 2 mM
-
inhibits NahF activity by 60%; inhibits NahV activity by 70%
-
both isoforms
-
1 mM, 12 h, 4°C, 58% loss of activity
-
moderate inhibition
-
only after preincubation with cation
-
10 mM, 60% inhibition of reductive amination
-
2% residual activity at 0.5 mM
-
1 mM, moderate inhibition of isozymes 1-3
-
93.3% residual activity at 1 mM
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
-
0.5 mM, 92% inhibition
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
-
5 mM, 73% inhibition
-
0.13 mM, complete inhibition
-
strong inhibition at 1 mM
-
; 7.4% residual activity at 2 mM
-
0.1 mM, 73% inhibition
-
up to 0.1 mM, not inhibitory, 1 mM, 20% residual activity
-
50% inhibition at 0.1 mM
-
1 mM, 32% inhibition
-
stronger inhibition at pH 7.0 than at pH 3.0
-
slight
-
slight inhibition
-
inhibits activity by 72%, inhibition prevented by inclusion of 10 mM EDTA; inhibits TNMT activity by 72%, can be prevented by the inclusion of EDTA
-
5 mM
-
1 mM, complete inhibition
-
5 mM, complete inhibition
-
strong inhibition
-
strong inhibition, Dnmt3a; strong inhibition, Dnmt3b
-
71% inhibition by 5 mM
-
purified protein is not very sensitive to this metal but the loss of AGT could contribute to the well-known carcinogenicity of nickel
-
84% inhibition at 2 mM
-
5 mM, 83% inhibition
-
83% inhibition at 5 mM
-
83% inhibition at 5 mM
-
2 mM, 28% residual activity
-
strong inhibition
-
1 mM, 68% inhibition
-
21% inhibition at 2 mM
-
5 mM, strong
-
10 mM, 21% inhibition; 21% inhibition at 10 mM
-
inhibits CEFT-4
-
15% of maximal activity
-
strongly inhibits the sterol glucosyltransferase activity, IC50 (mM): 1.2
-
1 mM, 58% of initial activity
-
strong inhibition at 1 mM and 10 mM
-
over 90% inhibition
-
about 38% residual activity at 10 mM; about 5% residual activity at 10 mM
-
2 mM
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
-
1 mM, 95.4% inhibition
-
about 80% residual activity in the presence of 2 mM
-
1 mM, 88% inhibition
-
inhibits Mn2+-activated enzyme
-
destabilization, 30.2% activity at 1 mM
-
in the presence of Mn2+
-
10 mM
-
99% inhibition at 10 mM
-
20 mM, 90% loss of activity
-
10 mM NiCl2, 75% inhibition
-
strong
-
5 mM, 50-80% inhibition
-
3.15% of activity remaining at 10 mM
-
weak
-
1 mM, 24% decrease of activity
-
about 1% residual activity at 10 mM
-
strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
-
AST II
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
-
inhibition of ADT and GDT, not PDT
-
reduced activity
-
competitive versus ATP via replacement of Mg2+, noncompetitive versus D-glucose via a cysteine residue proximal to the D-glucose binding site, enzyme-nickel interactions with positive cooperativity via histidine residues, no saturation is reached, nickel binding induces conformational changes in the secondary structure of the enzyme modifying the monomer/dimer equilibrium and decreasing the activity, overview
-
1.6 mM, 43% inhibition; 1.6 mM, 60% inhibition
-
68% activity in the presence of 10 mM Ni2+ compared to Mg2+
-
ATP-dependent activity is reduced to 60% or 7% in the presence of 5 or 20 mM Ni2+
-
3 mM, 50% inhibition in the presence of 3 mM Mg2+
-
53% residual activity at 3 mM
-
inhibits in combination with MgCl2, stimulates without MgCl2
-
inhibits activating effect of Mg2+
-
inhibits sperm protein phosphorylation by the enzyme
-
high inhibition at 1 mM
-
2 mM
-
20 mM in presence of 10 mM Mg2+, more than 90% inhibition
-
inhibits uridylyl removing activity
-
moderate inhibition
-
2 mM, 75% inhibition
-
more than 70% inhibition at 0.1 mM
-
inhibits the synthesis of s4U
-
slight inhibition at 1 mM
-
30% inhibition at 1 mM
-
strong inhibition
-
sensitive to metal ions, almost complete inhibition at 6.0 mM
-
55.4% residual activity at 1 mM
-
57% inhibition at 2 mM
-
1 mM, 15.1% of initial activity; 1 mM, 44.5% of initial activity; 1 mM, 63% of initial activity
-
AChEA and AChEB are completely inhibited by 1 mM of Ni2+
-
1.0 mM, 67% relative residual activity
-
10 mM, 28% inhibition
-
10 mM, 50% loss of activity
-
0.5 mM, strong inhibition
-
1 mM, slight inhibition
-
effective competitive inhibitor
-
complete inhibition at 1 mM
-
1 mM
-
competitive towards Mg2+
-
slight inhibition
-
in absence of free Zn2+ in solution
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
-
5 mM, complete loss of activity
-
35% activity at 1 mM
-
35% activity at 1 mM
-
24% inhibition at 1 mM
-
94% inhibition by 2 mM NiCl2
-
0.2 mM, 29% inhibition
-
2 mM, 47% of initial activtiy
-
1 mM, NiCl2, 30% inhibition
-
28% residual activity at 2 mM
-
10 mM, 36% loss of activity
-
1 mM, 25% of initial activity
-
47% inhibition at 50 mM for beta-D-.fucosidase I, 25% inhibition at 50 mM for beta-D-fucosidase II
-
complete inhibition at 5 mM
-
strong inhibition at 5 mM
-
5 mM, strong inhibition
-
83.5% inhibition at 5 mM
-
64% residual activity at 1 mM
-
F1 form 62%, F2 form 67% inhibition
-
about 5% residual activity at 1 mM
-
1.0fold decrease of activity at 10 mM
-
inhibits the enzyme activity at 4 mM by 11.5%
-
54.7% residual activity at 1 mM
-
90.26% residual activity at 10 mM
-
70.55% residual activity at 5 mM
-
1 mM, 59.7% loss of activity
-
1% residual activity at 10 mM
-
1 mM, 19% inhibition
-
10 mM, about 35% loss of activity
-
0.001 mM
-
complete inhibition at 5 mM
-
30% inhibition at 1 mM
-
1 mM, 90% inhibition
-
25% inhibition at 1 mM
-
89% inhibition at 1 mM
-
0.5 mM
-
3.3 mM, no residual activity
-
partial
-
at 0.01 mM 44.6% activity relative to control
-
0.2 mM, about 75% loss of activity, the inhibitory effect is not overcome by the presence of Co2+
-
inhibits S102H/G131H mutant at 0.76 mM, inhibition can be restored by addition of EDTA
-
50% inhibition at 0.011 mM
-
0.06 mM, 30% inhibition
-
inhibition of amidolytic activity
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+
-
26.7% residual activity at 1 mM
-
complete inhibition at 1 mM
-
residual activity in the presence of 20 mM: 0% free papain, 16% immobilized papain
-
strong inhibition
-
inhibits 85% at 0.2 mM and precipitates the enzyme at 1 mM
-
inhibitory below 5 mM
-
weak
-
39% inhibition at 1 mM, 87% at 5 mM
-
at pH 10, not at pH 7
-
1 mM
-
2 mM, 60% decrease of activity of enzyme produced with pET vector system and 20% decrease of activity of enzyme produced with pBAD vector system
-
ADAMTS13 activity is markedly decreased in the presence of 0.9 mM Ni2+
-
low concentrations of Ni2+ inhibit ADAM12-S drastically
-
41% inhibition at 1 mM
-
inhibits the caseinolytic and elastinolytic activities
-
0.087 mM, 48% inhibition
-
slight
-
partial inhibition at 0.050 mM
-
33% inhibition at 1 mM
-
85% inhibition at 10 mM
-
1 mM: 66.8% inhibition
-
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
-
1 mM: 60% inhibition
-
2 mM, 80% inhibition
-
1 mM, plus 0.1 mM Mn2+ complete inhibition
-
at pH 6.5
-
48% residual activity at 1 mM
-
weak
-
2 mM, complete inhibition
-
0.01 mM 73% inhibition
-
2.5 mM, 18% residual activity
-
complete inhibition at 1 mM
-
0.1 mM
-
5 mM
-
complete inhibition, not due to displacement of the native active site metal ion Fe2+
-
2 mM inhibitor in presence of 1 mM Mn2+, 40% inhibition
-
10 mM, over 90% inhibition
-
0.1 mM, 15% decrease of activity
-
1 mM, 64.3% residual activity
-
1 mM, complete loss of activity
-
weak
-
cells stressed by 8 microM Ni(II) for 20 min lose 75% of their FbaA activity. In presence of 8 microM Ni(II), purified FbaA loses 80% of its activity within 2 min. Inhibition is due to Ni(II) binding to a secondary zinc binding site
-
64% inhibition at 1 mM
-
about 10% residual activity in the presence of Ni2+
-
6% specific activity at 10 mM
-
2.6% activity at 0.1 mM and 17.5% activity at 1 mM chloride salt
-
95.0% inhibition at 1 mM
-
inhibits slightly
-
0.5 mM, 8% inhibition
-
90% inhibition
-
0.1 mM, 83% inhibition
5 mM
-
complete inhibition
-
1 mM, 60% inhibition
-
weak
-
1 mM, 80% inhibition
-
10 mM, 40-100% inhibition
about 80% residual activity at 1 mM
-
no activity when Zn2+, Ni2+ or Cu2+ is used as divalent metal ion
-
2 mM, 98% inhibition
-
strong
-
0.1 mM, weak
-
1 mM, 23% of initial activity, respectively; 1 mM, 7.8% of initial activity, respectively
-
5 mM, complete inhibition
-
5 mM, complete inhibition
-
severe inhibition of wild-type PI-PLC
-
substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components
-
slight inhibition of both activities
-
almost complete inhibition at 0.1 mM
-
almost complete inhibition at 1 mM
-
slight inhibition
-
1 mM, 14% residual activity
-