Ligand ethylenediaminetetraacetic acid

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Basic Ligand Information

Molecular Structure
Picture of ethylenediaminetetraacetic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C10H16N2O8
ethylenediaminetetraacetic acid
KCXVZYZYPLLWCC-UHFFFAOYSA-N
Synonyms:
2,2',2'',2'''-(1,2-ethanediyldinitrilo)tetraacetic acid, Chelating agents, EDTA, ethylendiaminetetraacetate, ethylenediaminetetraacetate, ethylene diamine tetraacetic acid, Fe(III)-ethylenediaminetetraacetic complex

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2 = ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
EDTA + O2 + FMNH2 + H+ = ethylenediaminetriacetate + glyoxylate + H2O + FMN
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (4 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
4,7-diphenyl-1,10-phenanthroline-disulfonic acid + Fe(III)-ethylene diamine tetraacetic acid = Fe(II)-tri-4,7-diphenyl-1,10-phenanthroline-disulfonic acid + ethylene diamine tetraacetic acid
show the reaction diagram
-
-
Fe(III)-EDTA + NADPH + H+ = Fe(II) + EDTA + NADP+
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (455 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation, acyldihydroxyacetone phosphate as substrate
-
activates 5% at 5 mM, reduction reaction
-
activtion to 112% activity; up to 112% of initial activity
-
1 mM, 105% of initial activity
-
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
-
0.5 mM, 21% increase
-
increases the apparent HMGR activity in sweet potato extracts
-
10-100 mM, sodium phosphate buffer, pH 8.0
-
stimulation
-
without EDTA the rates are about 60% of the maximal rate
-
110% activity at 1 mM
-
slightly stimulating
-
slight stimulation
-
slight activation for short and long chain oxidases
-
40% activation at 1 mM
-
up to 7fold activation
-
106.8% activity at 2 mM
-
Co QueD: 110% activity remains after 15 min incubation with 1 mM reagent
-
135.07% activity at 1 mM
-
10 mM, 1.1fold activation
-
38% activation at 0.05 mM
-
5 mM or 20 mM, slightly increases activity
-
0.01 mM, stimulates by 67%
-
49% enhancement of activity at 5 mM
-
200-400 mM, activates
-
slight stimulation
-
slightly activating at 1 mM, mitochondrial enzyme
-
the enzyme activity is increased 12% over the control by 1 mM EDTA
-
reversible stimulation of GDP reduction, irreversible inhibition of CDP reduction
-
poor activation
-
1 mM, increase in activity
-
5fold increase in enzyme activity
-
enhances activity 1.3fold
-
activation
-
stimulation of undialyzed enzyme at 30 mM
-
slight activation at 1 mM
-
1 mM, slight activation, effect not consistant
-
stimulates slightly
-
reduction of nitrate and menadione requires EDTA
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
-
activates slightly
-
109.33% activity at 5 mM
-
removal of EDTA leads to 60% loss of activity
-
5 mM, 10% increase inactivity
-
activates
-
presence of 1 mM EDTA results in a slight but significantly higher activity
-
2.5 mM, 1.3fold activation
-
5.0 mM, relative activity 103%
-
slight increase of activity
-
activates
-
47.8% activity in absence of both EDTA and mercaptoethanol
-
activation
-
10 mM, enhances activity, relative activity: 143%
-
activates
-
activates at low concentrations in the presence of a higher concentration of CoCl2, inhibits at 0.1-1.0 mM by 30%
-
required
-
activates
-
required for enzyme activity
-
slight activation
-
2fold activation, lowers the Km-value
-
50 mM, 9% increase of activity
-
activation
-
0.01 mM, 10% activation
-
up to 3fold stimulation
-
stimulation in the presence of high concentrations of methanol and detergents
-
slight stimulation
-
30% activation at 1 mM
-
60% increase of activity at 0.1 mM, probably due to removal of heavy metal ions
-
0.01 mM, activation
-
1-10 mM, activates
-
1 mM: slight activation, 10 mM: 36% inhibition
-
25% activation at 1 mM
-
markedly increased activity
-
maximal activity at 50 mM
-
50% activation, 1 mM
-
84% activation at 25 mM
-
100% activity in the presence of 100 mM EDTA
-
10 mM, increases reaction velocity 1.5fold
-
approx. 3.5fold activation at 20 mM
-
maximal activity at 5 mM, inhibition by 20 mM
-
1.0 mM, relative activity 108%
-
stimulates
-
2 mM, marked stimulation, even in presence of 30 mM Mg2+
-
variable degree of activation
-
prevents inhibition by traces of cations
-
stimulates
-
maximum activation at 0.5 mM, in presence of 20 mM Mg2+
-
10 mM, stimulates isozymes A and B
-
stimulatory effect
-
the addition of 0.1 mM EDTA increases product formation by 2.5fold
-
in absence of reducing agents
-
slight activation
-
in small quantities activating: one-tenth the Ca2+-concentration
-
1 mM, 108% of initial activity; 1 mM, 111% of initial activity; 1 mM, 62.7% of initial activity
-
10% activation at 10 mM
-
1 mM, 22% activation, Phedase type 1; 1 mM, 9% activation, Phedase type 2
-
with RNA core as substrate
-
stimulates the activity of the mitochondrial enzyme above 2 mM
-
stimulates the activity of the mitochondrial enzyme above 2 mM
-
with 0.2 mM, at 37°C, pH 7.4, 11% relative activity when compared to Co2+
-
less than 1 mM
-
14 mM, 30°C, pH 7.5, 175% relative activity with histone as substrate
-
increases activity
-
activation
-
35% stimulation at 2 mM
-
reverses Ca2+ inhibition
-
13% activation at 2 mM
-
EDTA at 0.10 mM slightly activates PDE4
-
10 mM, 114% of initial activity
-
activates
-
115.2% activity at 5 mM
-
activating
-
slight stimulatory effect
-
about 115% activity at 1 mM
-
especially EDTA, activate
-
increases activity of wild-type enzyme and of mutant enzyme R26Q/S169N/I333V/A398V/Q411L/P453L
-
0.04 M, 70% activation
-
120% activity at 1 mM
-
1%, 1.25fold activation
-
10 mM, activation to 105.32% of control
-
up to 24% enhanced activity
-
30% stimulation
-
a slight activating influence on isoform RhaB1 is observed for EDTA at 10 mM
-
about 120% activity at 1 mM
-
slight stimulatuion after 30 min of incubation
-
10 mM, about 1.1fold activation
-
146% activity in the presence of 10 mM
-
activation
-
1.0 mM, 8% activation
-
25% increase of activity at 10 mM
-
increase in activity about 40% at 10 mM
-
increase in activation of pro-matrix metalloproteinase-2
-
required for maximal activity
-
enhances activity
-
28% increase of activity at 2 mM
-
stimulation
-
2 mM, 79% increase in activity
-
enhances activity
-
assay with
-
slight activation
-
23.9% activation at 10 mM
-
slight stimulation
-
1-20 mM strongly activates deformylase activity, activity increases up to 70% at 10 mM
-
27% activation at 1 mM
-
1 mM, 110% of initial activity
-
1 mM, more than 200% of initial activity
-
stimulates
-
1 mM, relative activity 104%
-
stimulates
-
stimulates
-
stimulates
-
about 130% activity at 1 mM
-
in a concentration range of 0.02 mM to 1000 mM
-
89% activation at 0.9 mM, complete inhibition at 5 mM
-
able to reverse Zn2+ inhibition
-
119% activity at 1 mM
-
32% activity increase at 1 mM
-
activating below 5 mM
-
10-20 mM, 10% activation
-
2 mM, stimulates
-
stimulates
-
activates
-
enhances activity
-
1 mM, 146% of initial activity
-
increases activity
-
10 mM, 94.2% increase of activity
-
stimulates
-
maximum activity at 2 M
-
1 mM, 123% of initial activity
-
slight stimulation
-
enhances activity
-
1-5 mM, 110-120% activation
-
activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
-
1 mM, 115% of initial activity
-
activation, 5 mM
-
slight stimulation
-
weak activator at 1 mM
-
stimulates
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activation
-
10 mM, 30% increase in activity
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Inhibitor in Enzyme-catalyzed Reactions (3195 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
weak inhibition
-
2 mM
-
5% residual activity at 50 mM, addition of Mg2+ in excess restored the initial activity
-
2 mM
-
up to 0.3 mM, 70% loss of enzyme activity
-
complete inhibition at 50 mM, the enzyme activity can be restored by adding 25 mM Zn2+
-
97% inhibition at 0.01 mM
-
2 mM
-
50% inhibition at 67.7 mM
-
30% inhibition at 1 mM
-
strong inhibition at 10 mM
-
40% inhibition at 1 mM
-
inhibits 92% at 10 mM
-
slight inhibition at 1 mM
-
83% residual activity at 1 mM
-
; D-carnitine dehydrogenase, 20 mM, 25-70% inhibition
-
inhibition at 1 mM, fully restored by addition of 1 mM Mn2+, Co2+, Mg2+ or Ca2+, partially restored by 1 mM Ni2+ or Zn2+
-
59% inhibition at 10 mM
-
1 mM, 77% inhibition
-
90% inhibition
-
inhibition and destabilization of the enzyme at 10 mM
-
xylulose 5-phosphate does not protect the enzyme from EDTA inactivation. Addition of Mn2+ at concentrations of up to 2 mM results in complete reactivation of APDH
-
inhibition, (R)-2,3-butanediol dehydrogenase activity
-
1 mM, 91% of initial activity with substrate diacetyl, 90% with substrate 2,3-butanediol, respectively
-
1 mM, 30% inhibition
-
approximately 0.02-0.025 mM PhpC is incubated with 20-25 mM EDTA at 4°C until the activity is completely abolished (usually 1-2 h)
-
44% inhibition at 100 mM
-
inhibits the subsequent reactions of the mevalonate pathway in Hevea latex
-
7 mM, 96% inhibition; 7 mM EDTA inhibits the enzyme by 96%
-
about 35% inhibition at 1 mM, about 25% inhibition at 10 mM
-
1 mM, 52.2% inhibition
-
2.5 mM, 8% inhibition
-
5 mM, 73% residual activity; 73.7% residual activity at 5 mM EDTA
-
68% inhibition at 1 mM, restored by addition of 2 mM MgCl2
-
severe inhibition
-
80.6% residual activity at 1 mM
-
weak inhibition at high concentration, little effect in soluble extract of disintegrated mitochondria
-
1 mM, 20% decrease in activity
-
inhibits the enzyme activity about 68% and 89% in the concentration of 10 mM and 50 mM,respectively
-
1 mM, complete inhibition
-
decreases enzyme thermal stability
-
1 mM, 23% inhibition
-
24% inhibition at 0.5 mM
-
inhibits apoenzyme quinate dehydrogenase
-
0.1 mM, 96% inhibition
-
slight
-
8% inhibition at 10 mM
-
59% residual activity at 100 mM
-
no activity
-
5.2 mM, 13% inhibition
-
40% inhibition at 5 mM
-
27% inhibition at 10 mM
-
10 mM, 10% inhibition
-
at 0.2 M 35% inhibition of hydrogen production and 27% inhibition of hydrogen oxidation
-
destabilizes the enzyme
-
1 mM, 40% inhibition
-
slight inhibition
-
largely irreversible losses
-
1 mM, 99% inhibition
-
inhibits by 10% at 5 mM
-
2 mM, 50% residual activity
-
99% inhibition at 5 mM
-
1 mM, 31% inhibition
-
1 mM, 30% inhibition
-
1 mM, relative activity remaining 95%
-
1 mM, 1% residual activity
-
1 mM, 8% inhibition
-
little or no effect
-
complete inhibition at 1 mM
-
inhibits after a prolonged incubation time
-
1 mM, 32% inhibition
-
inhibits 15-20% at 0.5-5 mM
-
9.8% inhibition at 2.5 mM
-
0.1 mM, 77% inhibition
-
7% inhibition at 1 mM
-
chelation of Fe3+
-
68% inhibition at 2 mM
-
3% residual activity at 10 mM
-
68% inhibition at 1 mM
-
inhibits non-purified enzyme, ammonium sulfate precipitate
-
1 mM, 18% loss of activity
-
significantly inhibits enzyme activity
-
10 mM
-
64.6% inhibition
-
0.5 mM, 64% inhibition
-
no inhibition EDTA
-
18.1% residual activity at 1.5 mM
-
DELTA12-desaturase system, enzymatic complex
-
2 mM, 7% koss of activity
-
5 mM, 94% inhibition
-
1 mM, 1% residual activity
-
weak
-
2 mM, complete loss of activity
-
2.36% residual activity at 1.0 mM
-
19.8% inhibition of hypoxanthine oxidation at 10 mM
-
50 mM, slight inhibition
-
slight inhibition
-
10 mM, complete inhibition, reactivated by Mn2+ to a level of 25%
-
60% inhibition at 5 mM, 87% inhibition at 10 mM
-
18% inhibition in the presence of 1 mM
-
2 mM, 63% residual activity; 63% relative activity
-
50 mM, 22% inhibition
-
5 mM, 83.2% activity compared to untreated control
-
50% inhibition at 50 mM
-
40% inhibition by 1 mM and 45% inhibition at 5 mM
-
10 mM, 55% inhibition
-
0.5 mM, 85% inhibition
-
10 mM, 28% inhibition
-
5 mM, 75% inhibition
-
potent inhibitor, other metal chelators ineffective
-
11% inhibition at 10 mM
-
0.036 mM, 40% inhibition, 0.36 mM, complete inhibition, reversed by addition of excess Mg2+ and Ca2+
-
80°C, complete loss of activity
-
presence of EDTA induces monomerization
-
slightly inhibitory
-
16.7 mM, 17% inhibition
-
enzyme preincubated with the inhibitor, 0.00333 mM, for 60 min at room temperature before the addition of the substrate, 11% inhibition
-
3.3 mM, 32% inhibition
-
strong inhibition
-
1 mM, 23% inhibition
-
reactivation by Ca2+ and Mn2+
-
1 mM, 5.3% residual activity
-
64% inhibition at 7.1 mM
-
treatment with EDTA reduces the activity of wild type enzyme
-
13% inhibition at 1 mM
-
NAD+ dependent enzyme from Ehrlich ascites tumor cells
-
2 mM, 45% inhibition, complete inhibition after preincubation with 1 mM EDTA for 30 min, almost the total activity can be restored with 2 mM Co2+, Ni2+ and Mn2+
-
1 mM, slight inhibition
-
incubation for 1 h completely inhibits enzymatic activity
-
; 72.6% residual activity at 2 mM
-
reduction of cytochrome c and formation of superoxide anion
-
0.15 mM, 80% inhibition
-
10 mM, 11% inhibition
-
10 mM, 21% inhibition
-
0.1 mM, 89% residual activity
-
20 mM, 50% inhibition
-
inhibits the enzymatic reducing activity slightly, addition of Mo2+ and Zn2+ to the reaction mixture eliminates the EDTA inhibitory effect
-
not EGTA
-
1 mM, 5% inhibition
-
5 mM, 32% inhibition, production of methyl iodide
-
2 mM, markedly reduces the level of methylation
-
10 mM, complete inhibition
-
10 mM, 31% inhibition
-
significantly lowers the activity of MycE even in the presence of 10 mM Mg2+
-
1 mM, strong inhibition
-
75% inhibition at 1 mM, complete inhibition at 2 mM, reversible by Zn2+ addition, competitive versus Zn2+, kinetics, overview
-
13% inhibition at 5 mM
-
above 10 mM
-
23% inhibition by 5 mM
-
relative activity 77% of control
-
slight inhibition
-
in absence of Mg2+
-
complete inhibition at 1 mM, reversible by Mn2+ or, to a lesser extent, by Co2+ to 90% and 68% of maximal activity, respectively, no protection by Mg2+
-
weak
-
weak inhibition
-
inhibits 30% fraction P3D, does not inhibit subcellular fraction P3A
-
at 1 mM, 15% inhibition
-
1 mM, 79% inhibition
-
2 mM, 34% inhibition
-
weak
-
activates at low concentrations in the presence of a higher concentration of CoCl2, inhibits at 0.1-1.0 mM by 30%
-
0.1 mM, 24% inhibition
-
1 mM EDTA inhibits enzyme by 20%
-
1.0 mM, complete inhibition
-
63% inhibition at 1 mM, complete inhibition at 10 mM
-
slightly inhibitory
-
above 0.5 mM
-
relative activity: 90%
-
slight inhibition at 5 mM
-
5 mM, 60% inhibition
-
0.05 mM, no residual activity. Activtity can be completely restored by addition of Co2+, or Mn2+
-
1.0 mM, 30% inhibition
-
1 mM, 25% inhibition
-
slight inhibition
-
0.001 mM: 30% inhibition, 0.01 mM: complete inactivation
-
83% inhibition at 10 mM
-
10% of maximal activity in absence of any cation and in presence in EDTA
-
complete inhibition
-
1 mM, 43% inhibition
-
negative influence on activity at 10 mM, but reversible
-
strong
-
16% decrease of activity
-
1 mM, complete inactivation
-
strong inhibition at 5 mM
-
complete inhibition at 5 mM
-
1 mM, 86% residual acitvity
-
5 mM, 17% inhibition
-
completely inhibited by addition of EDTA
-
about 20% residual activity in the presence of 10 mM
-
32% inhibition at 2 mM
-
5 mM, 5% residual activtiy
-
at 10 mM, partially
-
complete inhibition
-
10 mM, 82% inhibition
-
slight inhibition
-
5 mM, 95% loss of activity
-
inhibits probably due to complex binding to Mn2+
-
complete inhibition
-
10 mM, slight inhibition
-
1 mM, 25% inhibition of hydrolysis reaction, transfer reaction increases to 388%
-
2 mM, complete inhibition
-
5 mM, 41% inhibition in presence of Mg2+, 2% inhibition in absence of Mg2+
-
10 mM, strong
-
weak
-
complete inhibition at 1 mM
-
38% inhibition at 0.2 mM
-
reversible by 2-mercaptoethanol and excess Mg2+
-
activity is restored by addition of Mn2+ and Mg2
-
0.1 mM, 71% inhibition of purified sialyltransferase-1
-
5 mM, 12% inhibition
-
the enzyme is active in the absence of exogenously added divalent cations but lost all activity when incubated before assay with 5 mM EDTA. The lost enzyme activity is restored to 2.4–3 times higher levels of the original one by the addition of 1 mM MnCl2, CoCl2, or NiCl2 and to one-third the original activity by 1 mM MgCl2. The other cations (Ca2+, Fe2+, Cu2+, and Zn2+) do not restore enzyme activity
-
10 mM, complete inhibition
-
1 mM, 16% inhibition
-
complete inhibition at 10 mM
-
maximal activity at 5 mM, inhibition by 20 mM. Mg2+ reactivates
-
complete inhibition
-
5 mM, complete inhibition
-
1 mM, 21% residual activity
-
complete inhibition at 10 mM
-
89% activity retained at 1 mM, 36% activity retained at 10 mM
-
1 mM, 92% remaining activity
-
complete inhibition at 1.3 mM
-
10 mM, 100% inhibition
-
50 mM, complete inhibition; complete loss of activity; completely abolishes activity
-
50 mM, complete inhibition; complete loss of activity; completely abolishes activity
-
inhibition of reaction by molar exess of EDTA over Mg2+
-
weak
-
reversed by Mg2+
-
complete incactivation at 2.5 mM
-
1 mM, about 50% loss of activity
-
about 10% residual activity at 5 mM
-
2 mM: 3% inhibition
-
10 mM: 50% inhibition
-
a 3fold excess of EDTA compared to the Mg2+ concentration strongly represses the MurK activity. Addition of 2 mM MgCl2 to the reaction mixture partially restores MurK activity
-
slight inhibition between 0.5-5 mM
-
strong inhibition
-
inpresence of phosphate
-
10 mM, complete loss of activity
-
4 mM, 80% loss of activity
-
5 mM, 98.5% inhibition
-
100% inhibition at 0.5 mM
-
complete inhibition
-
complete inhibition
-
above 0.5 mM
-
1 mM, complete loss of activity
-
complete inhibition at 2 mM
-
10 mM, complete inhibition
-
10 mM, in presence of 20 mM Mg2+
-
at 0.1 mM, for 1 h at 0ºC, activity is reduced to 40% of the control value. The activity is fully restored by addition of 0.5 mM MnCl2
-
enzyme is inactive in presence of EDTA, but inhibition is completely relieved by addition of 1 mM MnSO4 or MgSO4
-
20 mM, loss of activity
-
complete inhibition at 50 mM
-
80 mM, 30% inhibition
-
in absence of added metal ion
-
inactivation reversed by addition of metal ions
-
15% inhibition at 10 mM
-
50 mM, 89% inhibition
-
inhibition after prolonged incubation
-
50% residual activity at 1 mM
-
slight inhibition
-
a metal chelator, complete inhibition
-
10 mM, 42% residual acivity
-
inhibitory above 1 mM
-
10 mM, 16% inhibition
-
10 mM, 30°C, 20 min, about 15% loss of activity
-
activity 88% reduced in the presence of Mg2+
-
activity is completely lost when the ions are removed from the wild-type enzyme by incubation with 10mM
-
inhibition can be reversed by Mg2+
-
recoverage by either Mg2+, Cl-, or CaCl2
-
slight inhibition at 0.1 M
-
enhances the inactivation of the enzyme in the presence of iron and L-ascorbic acid
-
0.01 M, 40% inhibition
-
inhibits the activity of the mitochondrial enzyme at concentrations of 0.5 mM
-
inhibits the activity of the mitochondrial enzyme at concentrations of 0.5 mM
-
reversible inhibition
-