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Ligand Al3+

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Basic Ligand Information

Molecular Structure
Picture of Al3+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
Al
Al3+
REDXJYDRNCIFBQ-UHFFFAOYSA-N
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Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (6 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
slight activation
-
GDH is activated at 0.03-0.08 mM in the Tris-HCl buffer solution at pH 6.5 and 7.5
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SML shows 16% increased activity in the presence of 10 mM Al3+
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activates by 80% at 1 mM
-
20% activation at 1 mM
-
in vivo acceptor activity of tRNALeu is decreased by 23% thereby the leucyl-tRNA synthetase activity is increased by 20%, overview
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Inhibitor in Enzyme-catalyzed Reactions (373 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 14.7% residual activity; 1 mM, 18.9% residual activity
-
1 mM, 14.7% of initial activity
-
almost complete inhibition of activity at 10 mM
-
1 mM, 13% residual activity
-
83%% inhibition, reduction of 2-dehydropantolactone
-
21.6% residual activity at 1 mM
-
strong inhibition
-
13.5% inhibition at 1 mM
-
8% inhibition at 1 mM, 78% inhibition at 10 mM
-
10 mM, 7% inhibition
-
95% inhibition at 0.1 mM
-
95% inhibition at 0.1 mM
-
1 mM, moderately inhibited
-
1 mM, isozyme A, 26% inhibition
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inhibits NahF activity by 42%; inhibits NahV activity by 15%
-
moderately inhibited by 1 mM
-
strong inhibition of both isoforms at 10 mM
-
2 mM, 47.9% residual activity
-
5 mM, no residual activity
-
moderate inhibition of isoform NhoA1
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the wild type enzyme shows bout 75% residual activity at 10 mM. The C-terminally truncated enzyme shows about 95% residual activity at 10 mM
-
80% inhibition
-
67.81% residual activity at 5 mM
-
1 mM, strong
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80.5% residual activity at 5 mM
-
68% inhibition at 100 mg/kg for male rats, 24% inhibition at 172.5 mg/kg for female rats
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strong inhibition
-
1 mM, slight inhibition; slight inhibition at 1 mM
-
22.4% residual activity at 1 mM
-
inhibition of phospholipase A1 activity and lysophospholipase activity
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can replace Ca2+, decreased activity
-
41% inhibition at 5 mM
-
strong inhibition
-
inhibited by more than 5 mM Al3+
-
less than 10% residual activity at 10 mM
-
1.33 mM, 0.9% relative activity
-
about 3.0% residual activity at 10 mM
-
70% inhibition at 5 mM
-
3% residual activity at 2 mM
-
67% inhibition at 5 mM
-
complete inhibition at 100 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
-
5 mM, complete inhibition
-
90% inhibition at 10 mM
-
10 mM, 91.97% residual activity
-
82% inhibition at 5 mM
-
50% inhibition at 20 mM
-
F1 and F2 form 30% inhibition
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35% inhibition at 10 mM
-
at 55ºC, pH 4.5, 5 mM, 89% inhibition
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72.3% residual activity at 1 mM
-
complete inhibition at 1 mM
-
10 mM, more than 90% loss of activity
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slight inhibition at 1 mM
-
linear mixed inhibition
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inactivates enzyme from smooth muscle at millimolar concentrations of Ca2+, calpain 1 and 2
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inactivation at millimolar concentration of Ca2+
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slight inhibition
-
1 mM, 47% residual activity
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84% residual activity at 1 mM
-
1 mM AlCl3, 30% inhibition
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46% residual activity at 1 mM
-
no inhibition of isozyme I, 33% inhibition of isozyme II
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1 mM
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5 mM, almost complete loss of enzyme activity
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50 mM, 26% loss of activity
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complete inhibition at 1 mM
-
21.4% inhibition at 1 mM
-
IC50: 0.319 mM, GSH has no protective effect
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10 mM, 5% residual activity
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about 83% residual activity at 1 mM
-
0.5-1 mM, inhibition of recombinant enzyme
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inhibitory
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5 mM AlCl3, 95% loss of activity
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1 mM, 2 h, 4°
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90.6% residual activity at 1 mM
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complete inhibition at 10 mM
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1 mM, complete inactivation
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57% inhibition at 1 mM
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2 mM, complete loss of activity
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1 mM
-
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
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40% residual activity
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Metals and Ions (105 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 109% of initial activity
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addition of trivalent aluminium ions (more than 0.1 mM) accelerates enzyme-catalyzed carboxylation of pyruvate with CO2
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no activity
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maximum activity at a ratio of 2 mol M3+/mol of enzyme. Inhibitory above a ratio of 4 mol M3+/mol of enzyme
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129% activity at 10 mM
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activates the free enzyme and enzyme immobilized on calcium alginate
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nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
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activates
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activates by 10% at 10 mM
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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
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5 mM, 25.9% increase in activity
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enhances increase in GDH activity due to Hg
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activates
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1 mM, 113% of initial activity
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activates
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best as chloride at lower concentrations around 0.1 mM, inhibitory at higher concentrations
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increases the enzyme activity at pH 8
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activates
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142.8% activity at 10 mM
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activates 18% at 1 mM
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1 mM, 110% of initial activity
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strongly inhibits enzymatic activity
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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
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the enzyme is activated in the presence of Al3+
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102.62% activity at 1 mM
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5 mM, about 150% of initial activity
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activates by 10% at 1 mM
-
about 193% activity at 1 mM
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5 mM, 113% of initial activity
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inhibits activity
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about 120% activity at 5 mM in acetate buffer
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activates 46.8% at 5 mM
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1 mM, enhances activity
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millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+
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5 mM, 16% residual activity
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117% activity at 3.5 mM
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required
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0.125 mM stimulates activity 37%
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slight activation of Cda2
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slightly enhances activity to about 110% of the standard activity
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at 2 mM 112% relative enzyme activity
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1 mM AlCl3, relative activity 102%
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exposure of the rye roots to Al3+ results in activation of GTPase, Al-induced secretion is inhibited by pertussis toxin
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activates
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activation, no significant influence on the rate-limiting step. Km value 0.850 mM
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can partially substitute for Mg2+ or Zn2+ at 10 mM showing 68.8% of the maximal activity with 10 mM Mg2+
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about 120% activity at 1 mM
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151% relative activity at 3 mM
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stimulates at a concentration of 0.1 mM
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enzyme activity is 28.6 U/mg protein at a metal concentration of 1 mM
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activity of enzyme towards UDP-xylose is 15.5 U/mg protein at a metal concentration of 1 mM
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1 mM, activates to 104% of control
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accelerates reaction
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results in 8.91tivity compared to Mg2+
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3D Structure of Enzyme-Ligand-Complex (PDB) (3 results)

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Enzyme Kinetic Parameters

Ki Value (1 result)

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

IC50 Value (5 results)

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

References & Links

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Links to other databases for Al3+

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EXTERNAL LINKS
ChEBI
PubChem
UniChem