Ligand EGTA

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Basic Ligand Information

Molecular Structure
Picture of EGTA (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C14H24N2O10
EGTA
DEFVIWRASFVYLL-UHFFFAOYSA-N
Synonyms:
ethylenedioxybis(ethylamine)-N,N,N',N'-tetraacetic acid, ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid, ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetracetic acid, ethyleneglycol-bis-(2-aminoethylether)-N,N,N',N'-tetraacetic acid, ethylene glycol bis(beta-amino-ethylether)-N,N,N',N'-tetraacetic acid, ethylene glycol bis(beta-aminoethyl ether)-N,N'-tetraacetic acid, ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid, ethylene glycol tetraacetic acid, glycoletherdiamine tetraacetic acid, O,O'-bis(2-aminoethyl)ethylenglycol-N,N,N',N'-tetraacetic acid, [ethylenebis(oxyethylenenitrilo)]tetraacetic acid

Show all pahtways known for Show all pathways known for EGTA

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (36 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
EGTA causes an increase in levels of enzyme observed on immunoplots
-
1.4fold stimulation at 0.2 mM, equimolar with Fe2+, and 2.8fold stimulation at 1 mM
-
2.5 mM, 1.3fold activation
-
50% of inhibition at 13 mM
-
stimulation at 0.4-0.9 mM, inhibition at 1.8 mM
-
0.5 mM
-
stimulates
-
activates
-
activates
-
14 mM, 30C, pH 7.5, 127% relative activity with histone as substrate
-
0.01 - 0.10 mM
-
activation, optimum at 1.5-3 mM
-
Cu2+ not inhibitory when EGTA added prior
-
increases activity about 2.3fold, relative activity 236.3%
-
activation
-
increase in activity about 40% at 10 mM
-
activates
-
2 mM, 79% increase in activity
-
1 mM, about 200% of initial activity
-
significantly increases cumulus cell cAMP concentrations
-
activation
-

Inhibitor in Enzyme-catalyzed Reactions (312 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
5 mM, 72% residual activity; 72.9% residual activity at 5 mM EGTA
-
strain DSM 4025, 5 mM, 89% inhibition
-
weak
-
slight inhibition
-
trivial name EGTA
-
7.5% inhibition at 1 mM
-
60% inhibition at 50 mM
-
10 mM, 35% inhibition
-
10 mM, 14% inhibition
-
the enzyme activity is abolished in the presence of 10 mM EGTA
-
71.57% residual activity at 1 mM
-
almost complete inhibition at 0.5 mM
-
10 mM, slightly increases activity
-
95% residual activity at 5 mM
-
38% inhibition at 10 mM
-
36% at 0.5 mM after 30 min
-
1 mM, 28% inhibition
-
i.e. ethylene glycol bis(beta-aminoethylether)-N,N'-tetraacetic acid, 1 mM, 53% inhibition
-
10 mM, 50% inhibition
-
strong
-
weak, 30 mM, 20% inhibition
-
10 mM, 96% inhibition
-
strong inhibition at pH 6.8 and Ca2+ concentrations below 0.5 mM
-
Ca2+/calmodulin-activated enzyme
-
1 mM, about 50% loss of activity
-
5 mM, 20% inhibition of the 410000 Da isoform, 85% inhibition of the 63000 Da isoform
-
stimulation at 0.4-0.9 mM, inhibition at 1.8 mM
-
negative regulation of COT
-
EGTA treatment reduces PME activity, but the addition of Ca2+ with EGTA reinstates the activity in response to heat shock
-
highly sensisitve to EGTA, the lost activity can be restored to the original level by the addition of divalent cations of the order Ca2+ = Mg2+ > Zn2+ > Fe2+ = Co2+, Mn2+, Ni2+, Cu2+ > Mo2+
-
10 mM, 15% inhibition at pH 7.0, LPL1
-
strong inhibition
-
inhibits enzyme activity in histone 2A-treated or alamethicin-treated microsomes, but has little effect on enzyme activity in intact microsomes
-
1 mM, slight inhibition
-
enzyme activity against 1-myristoyl-lysophosphatidylcholine, glycerophosphorylcholine, and p-nitrophenyl phosphorylcholine are readily inhibited by EGTA. Indicates that a divalent cation is essential for catalytic activity
-
20 mM, 55% residual activity
-
1-10 mM, 65-70% inhibition
-
95% inhibition at 20 mM
-
10% of enzyme inhibition at 20 mM, at 37C, pH 6.5
-
the inhibition by 1 mM EGTA is almost completely recovered by the addition of Co2+ at a concentration of 0.2 mM
-
99.9% inhibition at 1 mM
-
slightly inhibitory from 2 mM to 5 mM
-
complete inhibition, activity can be completely restored by addition of 1 mM CaCl2
-
96% inhibition in the presence of 1 mM EGTA, but 110% activity in the presence of the two inhibitors 1 mM EGTA and 1 mM Zn2+
-
0.05 mM, 94% inhibition
-
Ca2+ does not restore
-
17% inhibition at 0.01 mM, 44% inhibition at 0.1 mM, 44% inhibition at 0.5 mM
-
at 37C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 34%
-
strong inhibition at 1 mM
-
1.6 mM, 50% inhibition
-
complete inhibition at 1-10 mM
-
1 mM, 40% inhibition
-
40.55% inhibition at 0.1 mM
-
completely reversed by addition of excess Ca2+
-
4.72% inhibition at 0.1 mM
-
inhibition to a lesser extent than with EDTA
-
59% inhibition at 1 mM, 98% at 5 mM
-
strong, Zn2+ reverses, bovine serum albumin as substrate
-
35% inhibition at 5 mM
-
1 mM, complete inhibition
-
less effective than EDTA, Ca2+ at a 3:1 ratio of Ca2+/EDTA protects and reverses partially, Zn2+ at a 1:10 ratio of Zn2+/EGTA protects and reverses
-
5 mM
-
10 mM
-
5 mM, complete inhibition
-
1 mM, treatment of cells dramatically inhibits shedding of shedding of FcalphaR, i.e. Fc receptor for immunoglobulin A
-
moderate inhibitory effect
-
1 mM, 96% inhibition
-
hemorrhagic as well as the proteinase activity is inhibited
-
0.2 mM EGTA
-
1 mM causes 74% inhibition
-
strong inhibition at 1 mM, partially reversed by Mg2+, complete reactivation at 10 mM Ca2+
-
inhibits demembranated sperm motility at 30C, reversible by Ca2+, is less effective at 40C
-
enzyme activity is reduced to 24% after dialysis in buffer containing EGTA. Activity is completely recovered in the presence of 10 mM MgCl2 and recovered to 39% and 62% in the presence of MnCl2 and CoCl2, respectively
-
complete inhibition
-
1 mM, complete inhibition
-
10 mM, complete loss of activity
-
addition of 0.5-1 M reduces activity to 50%, Ca2+, Mn2+, Co2+ or Ni2+ restore activity
-
93% residual activity at 3 mM
-
-
-

Metals and Ions (3 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
relative activity: 14%
-

Enzyme Kinetic Parameters

Ki Value (2 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.012
-
-
1.6
-
-

IC50 Value (2 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.05
-
pH 7.2, 23C
0.0025
-
IC50 is 0.0025 mM

References & Links

Links to other databases for EGTA

ChEBI
PubChem
ChEBI
PubChem