Ligand Al3+

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 Al3+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Al
Al3+
REDXJYDRNCIFBQ-UHFFFAOYSA-N

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
GDH is activated at 0.03-0.08 mM in the Tris-HCl buffer solution at pH 6.5 and 7.5
-
SML shows 16% increased activity in the presence of 10 mM Al3+
-
in vivo acceptor activity of tRNALeu is decreased by 23% thereby the leucyl-tRNA synthetase activity is increased by 20%, overview
-

Inhibitor in Enzyme-catalyzed Reactions (282 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 14.7% residual activity; 1 mM, 18.9% residual activity
-
almost complete inhibition of activity at 10 mM
-
83%% inhibition, reduction of 2-dehydropantolactone
-
21.6% residual activity at 1 mM
-
strong inhibition
-
13.5% inhibition at 1 mM
-
1 mM, 89% inhibition
-
10 mM, 7% inhibition
-
95% inhibition at 0.1 mM
-
95% inhibition at 0.1 mM
-
strongly inhibited diphenolase activity at ripening stage 1 and 2
-
1 mM, isozyme A, 26% inhibition
-
inhibits NahF activity by 42%; inhibits NahV activity by 15%
-
strong inhibition of both isoforms at 10 mM
-
2 mM, 47.9% residual activity
-
80% inhibition
-
67.81% residual activity at 5 mM
-
strongly inhibits the native and the recombinant enzyme
-
1 mM, strong
-
strong inhibition
-
inhibits at 0.5-5 mM
-
22.4% residual activity at 1 mM
-
inhibition of phospholipase A1 activity and lysophospholipase activity
-
can replace Ca2+, decreased activity
-
1 mM, slight inhibition
-
strong inhibition
-
inhibited by more than 5 mM Al3+
-
1 mM, less than 20% residual activity, both free and immobilized enzyme
-
1.33 mM, 0.9% relative activity
-
about 3.0% residual activity at 10 mM
-
56% inhibition at 1 mM
-
3% residual activity at 2 mM
-
mild inhibitor
-
35% inhibition at 1 mM
-
1 mM, 93% inhibition
-
20.5% residual activity at 10 mM
-
10 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
-
strong inhibition at 10 mM
-
80% inhibition of xylan-inducible enzyme, 10% of xylose-inducible enzyme, at 1 mM
-
slight inhibition at 10 mM
-
82% inhibition at 5 mM
-
50% inhibition at 20 mM
-
F1 and F2 form 30% inhibition
-
35% inhibition at 10 mM
-
at 55ºC, pH 4.5, 5 mM, 89% inhibition
-
72.3% residual activity at 1 mM
-
complete inhibition at 1 mM
-
10 mM, more than 90% loss of activity
-
slight inhibition at 1 mM
-
slight inhibition
-
linear mixed inhibition
-
inactivates enzyme from smooth muscle at millimolar concentrations of Ca2+, calpain 1 and 2
-
inactivation at millimolar concentration of Ca2+
-
slight inhibition
-
1 mM, 47% residual activity
-
29% residual activity at 5 mM
-
1 mM AlCl3, 30% inhibition
-
46% residual activity at 1 mM
-
no inhibition of isozyme I, 33% inhibition of isozyme II
-
1 mM
-
91.2% residual activity at 2 mM
-
50 mM, 26% loss of activity
-
21.4% inhibition at 1 mM
-
IC50: 0.319 mM, GSH has no protective effect
-
10 mM, 5% residual activity
-
inhibitory
-
5 mM AlCl3, 95% loss of activity
-
complete inhibition at 10 mM
-
1 mM, complete inactivation
-
57% inhibition at 1 mM
-
2 mM, complete loss of activity
-
in vitro the enzyme is inhibited by 40% at 0.04 mM, Al3+ inhibits the enzyme in vivo and in vitro, quantitative analysis, in vivo acceptor activity of tRNALeu is decreased by 23% thereby the leucyl-tRNA synthetase activity is increased by 20%, overview
-
40% residual activity
-

Metals and Ions (73 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
no activity
-
maximum activity at a ratio of 2 mol M3+/mol of enzyme. Inhibitory above a ratio of 4 mol M3+/mol of enzyme
-
108% increased activity at 1 mM; 177% relative activity at 1 mM; 208% relative activity at 1 mM; 77% increased activity at 1 mM
-
the enzyme activity increases in the presence of Al3+
-
activates the free enzyme and enzyme immobilized on calcium alginate
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
-
activates
-
127.3% activity at 1 mM
-
activates by 10% at 10 mM
-
modulation of AGODH activity, exposure of the Al-challenged cells to a control medium results in a dramatic decrease in the activity of AGODH, in contrast, control cells incubated in an Al-enriched medium display an intense activity band, AGODH may be pivotal to the adaptation of Pseudomonas fluorescens to aluminium toxicity
-
enhances increase in GDH activity due to Hg
-
activates
-
activates
-
activation of LjPCS1; activation of LjPCS3
-
best as chloride at lower concentrations around 0.1 mM, inhibitory at higher concentrations
-
increases the enzyme activity at pH 8
-
activates at 1 mM
-
strongly inhibits enzymatic activity
-
at near-physiological ratios of aluminum to magnesium, aluminum can dominate over magnesium in the enzyme-metal fluoride inhibitory TSA complexes, aluminium is the more likely origin of some of the physiological effects of fluoride
-
the enzyme is activated in the presence of Al3+
-
102.62% activity at 1 mM
-
5 mM, 113% of initial activity
-
inhibits activity
-
about 120% activity at 5 mM in acetate buffer
-
2 mM, 1.25fold activation
-
1 mM, 1.4fold activation
-
activates 46.8% at 5 mM
-
10 mM, 125% of initial activity; 125.4% activity at 10 mM
-
millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+
-
5 mM, 16% residual activity
-
required
-
0.125 mM stimulates activity 37%
-
slightly enhances activity to about 110% of the standard activity
-
at 2 mM 112% relative enzyme activity
-
1 mM AlCl3, relative activity 102%
-
exposure of the rye roots to Al3+ results in activation of GTPase, Al-induced secretion is inhibited by pertussis toxin
-
activates
-
activation, no significant influence on the rate-limiting step. Km value 0.850 mM
-
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 68.8% of the maximal activity with 10 mM Mg2+
-
stimulates
-
151% relative activity at 3 mM
-
1 mM, 110% of initial activity, respectively; 1 mM, 115% of initial activity, respectively
-
stimulates at a concentration of 0.1 mM
-
enzyme activity is 28.6 U/mg protein at a metal concentration of 1 mM
-
activity of enzyme towards UDP-xylose is 15.5 U/mg protein at a metal concentration of 1 mM
-
1 mM, activates to 104% of control
-
accelerates reaction
-
results in 8.91tivity compared to Mg2+
-

3D Structure of Enzyme-Ligand-Complex (PDB) (3 results)

Enzyme Kinetic Parameters

Ki Value (1 result)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
2
-
pH 9.0, 37°C

IC50 Value (5 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
1.526
-
at pH 8.0 and 25°C
0.804
-
pH 8.0, 25°C
8
-
at pH 7.5 and 30°C
0.319
-
IC50: 0.319 mM, GSH has no protective effect
100
-
at pH 6.5, temperature not specified in the publication

References & Links

Links to other databases for Al3+

ChEBI
PubChem
ChEBI
PubChem