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Ligand ethylenediaminetetraacetic acid

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Basic Ligand Information

Molecular Structure
Picture of ethylenediaminetetraacetic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C10H16N2O8
ethylenediaminetetraacetic acid
KCXVZYZYPLLWCC-UHFFFAOYSA-N
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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)

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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
-

Substrate in Enzyme-catalyzed Reactions (7 results)

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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)

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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 (537 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation, acyldihydroxyacetone phosphate as substrate
-
activates 5% at 5 mM, reduction reaction
-
1 mM, 105% of initial activity
-
1 mM, 109.1% of initial activity
-
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
-
0.5 mM, 21% increase
-
1 mM, 5% activation
-
increases the apparent HMGR activity in sweet potato extracts
-
1 mM, 30% activation
-
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
-
activates
-
up to 7fold activation
-
106.8% activity at 2 mM
-
50 mM EDTA activates isoform mPPO
-
1 mM, 1.05fold activation
-
2 mM, 128% of initial activity
-
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
-
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
-
132.2% activity at 1 mM
-
5fold increase in enzyme activity
-
enhances activity 1.3fold
-
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
-
the enzyme is activated at 0.4 mM EDTA
-
110.57% activity at 20% (v/v)
-
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, 110% of initial 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
-
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
-
isoform Lyso-PAF ATE is activated by 1.4 mM EDTA in assay conditions
-
50 mM, 9% increase of activity
-
activation
-
0.01 mM, 10% activation
-
1 mM EDTA enhances the enzyme activity by 31%
-
up to 3fold stimulation
-
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
-
0.2 mM, activation to 150.26% of control
-
slight activation
-
50% activation, 1 mM
-
84% activation at 25 mM
-
100% activity in the presence of 100 mM EDTA
-
stimulation in the presence of high concentrations of methanol and detergents
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10 mM, increases reaction velocity 1.5fold
-
approx. 3.5fold activation at 20 mM
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maximal activity at 5 mM, inhibition by 20 mM
-
1.0 mM, relative activity 108%
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stimulates
-
2 mM, marked stimulation, even in presence of 30 mM Mg2+
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variable degree of activation
-
prevents inhibition by traces of cations
-
stimulates
-
maximum activation at 0.5 mM, in presence of 20 mM Mg2+
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10 mM, stimulates isozymes A and B
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stimulatory effect
-
the addition of 0.1 mM EDTA increases product formation by 2.5fold
-
in absence of reducing agents
-
about 125% activity at 1 mM
-
1 mM, 133% of initial activity
-
slight activation
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in small quantities activating: one-tenth the Ca2+-concentration
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10% activation at 10 mM
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EDTA together with Zn2+, Mn2+ and Co2+ enhances enzyme activity
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with RNA core as substrate
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stimulates the activity of the mitochondrial enzyme above 2 mM
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stimulates the activity of the mitochondrial enzyme above 2 mM
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with 0.2 mM, at 37°C, pH 7.4, 11% relative activity when compared to Co2+
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less than 1 mM
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14 mM, 30°C, pH 7.5, 175% relative activity with histone as substrate
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increases activity
-
activation
-
reverses Ca2+ inhibition
-
13% activation at 2 mM
-
EDTA at 0.10 mM slightly activates PDE4
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activates
-
activating
-
slight stimulatory effect
-
about 115% activity at 1 mM
-
especially EDTA, activate
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increases activity of wild-type enzyme and of mutant enzyme R26Q/S169N/I333V/A398V/Q411L/P453L
-
10 mM, slightly promotes the enzymatic activity
-
120% activity at 1 mM
-
113.65% activity at 5 mM
-
more than 160% activity at 2 mM
-
1%, 1.25fold activation
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10 mM, activation to 105.32% of control
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up to 24% enhanced activity
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a slight activating influence on isoform RhaB1 is observed for EDTA at 10 mM
-
about 120% activity at 1 mM
-
activity is increased by 25% by 1 mM EDTA but is completely inhibited by 2 mM EDTA
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slight stimulatuion after 30 min of incubation
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10 mM, about 1.1fold activation
-
146% activity in the presence of 10 mM
-
6.13fold activation at 1.0 mM
-
slight activation at 1.0 mM
-
1.0 mM, 8% activation
-
25% increase of activity at 10 mM
-
increase in activity about 40% at 10 mM
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increase in activation of pro-matrix metalloproteinase-2
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5 mM, about 1.2fold activation
-
slight activation at 10 mM
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5 mM, slight activation
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required for maximal activity
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enhances activity
-
stimulation
-
2 mM, 79% increase in activity
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enhances activity, best activity at 0.5 mM EDTA
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enhances activity
-
assay with
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less than 0.5 mM, slight enhancement of deaminase activity
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the chelators EDTA and EGTA have a positive effect over the antibacterial activity at 1-10 mM. 10 mM of EDTA increases radically the activity by 185%
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23.9% activation at 10 mM
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slight stimulation
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1-20 mM strongly activates deformylase activity, activity increases up to 70% at 10 mM
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27% activation at 1 mM
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103.6% activity at 10 mM, substrate N-(3-oxooctanoyl)-L-homoserine lactone
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1 mM, 110% of initial activity
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1 mM, more than 200% of initial activity
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stimulates
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1 mM, relative activity 104%
-
stimulates
-
stimulates
-
stimulates
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in a concentration range of 0.02 mM to 1000 mM
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89% activation at 0.9 mM, complete inhibition at 5 mM
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able to reverse Zn2+ inhibition
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35% stimulation at 2 mM
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119% activity at 1 mM
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32% activity increase at 1 mM
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about 130% activity at 2 mM
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activating below 5 mM
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10-20 mM, 10% activation
-
2 mM, stimulates
-
stimulates
-
activates
-
enhances activity
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1 mM, 146% of initial activity
-
increases activity
-
10 mM, 94.2% increase of activity
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stimulates
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maximum activity at 2 M
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about 130% activity at 10 mM
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slight stimulation
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enhances activity
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1-5 mM, 110-120% activation
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activation by 2-mercaptoethanol, EDTA, and ascorbic acid. The effects of EDTA and ascorbic acid are additive
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1 mM, 115% of initial activity
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after 3 h and 24 h incubation with EDTA, the observed activity values are 2 and 4.7times higher than those of the reference sample
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activation, 5 mM
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slight stimulation
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weak activator at 1 mM
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stimulates
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activation
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10 mM, 30% increase in activity
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1 mM, slightly enhances the activity (9.6%)
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Inhibitor in Enzyme-catalyzed Reactions (3740 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
weak inhibition
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2 mM
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2 mM
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strong inhibition
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up to 0.3 mM, 70% loss of enzyme activity
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complete inhibition at 50 mM, the enzyme activity can be restored by adding 25 mM Zn2+
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97% inhibition at 0.01 mM
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2 mM
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50% inhibition at 67.7 mM
-
strong inhibition at 10 mM
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40% inhibition at 1 mM
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inhibits 92% at 10 mM
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slight inhibition at 1 mM
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1 mM, 72.9% residual activity
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83% residual activity at 1 mM
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D-carnitine dehydrogenase, 20 mM, 25-70% inhibition
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inhibition at 1 mM, fully restored by addition of 1 mM Mn2+, Co2+, Mg2+ or Ca2+, partially restored by 1 mM Ni2+ or Zn2+
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59% inhibition at 10 mM
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1 mM, 77% inhibition
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90% inhibition
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inhibition and destabilization of the enzyme at 10 mM
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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
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1 mM, 91% of initial activity with substrate diacetyl, 90% with substrate 2,3-butanediol, respectively
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1 mM, 30% inhibition
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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)
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44% inhibition at 100 mM
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inhibits the subsequent reactions of the mevalonate pathway in Hevea latex
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7 mM EDTA inhibits the enzyme by 96%; 7 mM, 96% inhibition
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about 35% inhibition at 1 mM, about 25% inhibition at 10 mM
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1 mM, 52.2% inhibition
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2.5 mM, 8% inhibition
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5 mM, 73% residual activity; 73.7% residual activity at 5 mM EDTA
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68% inhibition at 1 mM, restored by addition of 2 mM MgCl2
-
slight inhibition at 2 mM
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complete inhibition; complete loss of activity. Activity is recovered up to 85% by addition of Zn2+ and 15% by addition of Fe2+
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severe inhibition
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80.6% residual activity at 1 mM
-
weak inhibition at high concentration, little effect in soluble extract of disintegrated mitochondria
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1 mM, 20% decrease in activity
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inhibits the enzyme activity about 68% and 89% in the concentration of 10 mM and 50 mM,respectively
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1 mM, complete inhibition
-
decreases enzyme thermal stability
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5 mM, 85% of initial activity
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1 mM, 23% inhibition
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24% inhibition at 0.5 mM
-
5 mM, partial inhibition of activity
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partial inhibition
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slight
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inhibits apoenzyme quinate dehydrogenase
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0.1 mM, 96% inhibition
-
8% inhibition at 10 mM
-
59% residual activity at 100 mM
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no activity
-
5.2 mM, 13% inhibition
-
40% inhibition at 5 mM
-
27% inhibition at 10 mM
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1 mM, about 40% residual activity, activity is completely restored upon addition of Se+ cations, followed by Na+
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the removal of Ca+2 by dialysis of isoform PXG2 against EDTA completely abolishes its co-oxidative properties
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10 mM, 10% inhibition
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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
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2 mM, 50% residual activity
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99% inhibition at 5 mM
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1 mM, 31% inhibition
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64.77% residual activity in the presence of 5 mM EDTA
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0.05 mM, 80% of initial activity, 0.1 mM, 61% of initial activity
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complete loss of activity, only presence of Fe(II) restores activity
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1 mM, relative activity remaining 95%
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1 mM, 1% residual activity
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1 mM, 8% inhibition
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little or no effect
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complete inhibition at 1 mM
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complete loss of activity
-
inhibits after a prolonged incubation time
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1 mM, 32% inhibition
-
inhibits 15-20% at 0.5-5 mM
-
9.8% inhibition at 2.5 mM
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0.1 mM, 77% inhibition
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7% inhibition at 1 mM
-
chelation of Fe3+
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68% inhibition at 2 mM
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3% residual activity at 10 mM
-
68% inhibition at 1 mM
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inhibits non-purified enzyme, ammonium sulfate precipitate
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1 mM, 18% loss of activity
-
significantly inhibits enzyme activity
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10 mM
-
strong inhibition
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0.5 mM, 64% inhibition
-
no inhibition EDTA
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DELTA12-desaturase system, enzymatic complex
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2 mM, 7% koss of activity
-
1 mM, 1% residual activity
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EDTA-treated enzyme is inactive, activity is restored upon addition of Fe(II) but not Mn(II)
-
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
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10 mM, complete inhibition, reactivated by Mn2+ to a level of 25%
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causes a 2fold decrease in activity at 2 mM
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60% inhibition at 5 mM, 87% inhibition at 10 mM
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18% inhibition in the presence of 1 mM
-
2 mM, 63% residual activity; 63% relative activity
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50 mM, 22% inhibition
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5 mM, 83.2% activity compared to untreated control
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50% inhibition at 50 mM
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40% inhibition by 1 mM and 45% inhibition at 5 mM
-
10 mM, 55% inhibition
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0.5 mM, 85% inhibition
-
10 mM, 28% inhibition
-
partial inhibition at 2 mM
-
5 mM, 75% inhibition
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potent inhibitor, other metal chelators ineffective
-
11% inhibition at 10 mM
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0.036 mM, 40% inhibition, 0.36 mM, complete inhibition, reversed by addition of excess Mg2+ and Ca2+
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80°C, complete loss of activity
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presence of EDTA induces monomerization
-
slightly inhibitory
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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
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3.3 mM, 32% inhibition
-
strong inhibition
-
1 mM, 23% inhibition
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reactivation by Ca2+ and Mn2+
-
1 mM, 5.3% residual activity
-
1 mM, 92% 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
-
1 mM, slight inhibition
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incubation for 1 h completely inhibits enzymatic activity
-
2 mM, 33% inhibition
-
2 mM, 33% inhibition
-
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
-
0.1 mM, 89% residual activity
-
56.7% residual activity at 10 mM
-
0.25 mM, 71.8% loss of activity
-
20 mM, 50% inhibition
-
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
-
about 70-85% residual activity at 1 mM
-
the recombinant enzyme is inactivated by 10 mM EDTA
-
above 10 mM
-
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+
-
23% inhibition by 5 mM
-
relative activity 77% of control
-
slight inhibition
-
in absence of Mg2+
-
complete inhibition
-
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%
-
treatment leads to inactivation
-
slight inhibition at 5 mM
-
5 mM, 60% inhibition
-
2 mM, 59% residual activity
-
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
-
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
-
at 10 mM, partially
-
complete inhibition
-
1 mM, 25% inhibition of hydrolysis reaction, transfer reaction increases to 388%
-
EDTA inhibits transferase activity completely, but hydrolysis remains almost unaffected (89% residual activity at 1 mM)
-
1 mM, inhibition to 98.7% of control
-
10 mM, 82% inhibition
-
slight inhibition
-
5 mM, 95% loss of activity
-
5 mM, 15% loss of activity
-
inhibits probably due to complex binding to Mn2+
-
complete inhibition
-
10 mM, slight inhibition
-
4.7% inhibition at 1 mM
-
2 mM, complete inhibition
-
56.5% residual activity at 5 mM
-
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
-
strong inhibition
-
activity is restored by addition of Mn2+ and Mg2
-
reversible by 2-mercaptoethanol and excess 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
-
5 mM, complete loss of activity
-
10 mM, 100% inhibition
-
50 mM, complete inhibition; complete loss of activity; completely abolishes activity
-
40 mM
-
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
-
complete inhibition at 1.3 mM
-
5 mM, almost complete inhibition
-
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
-
the inhibition is rescued by addition of of Mg2+ or Mn2+ but not Ca2+ or Zn2+
-
1 mM, complete loss of activity
-
complete inhibition at 2 mM
-
10 mM, complete inhibition
-
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
-
1 mM, 33% inhibition
-
10 mM, 30°C, 20 min, about 15% loss of activity; 15% inhibition at 10 mM
-
inhibition after prolonged incubation
-
50% residual activity at 1 mM
-
a metal chelator, complete inhibition
-
inhibitory above 1 mM
-
10 mM, 16% inhibition
-
activity 88% reduced in the presence of Mg2+
-
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
-
comple inhibition
-
complete inhibition at 0.02 mM
-
chelates Mg2+, increasing Mg2+ concentrations can restore the activity of the enzyme
-
10 mM, complete inhibition
-
dialysis of IgGs from rabbits immunized with DNase II against a buffer containing EDTA or addition of EDTA to the reaction mixture leads to a complete disappearance of DNase activity
-
90% inhibition at 0.001 M
-
inhibits Py-Py correndonuclease II at concentrations above 20 mM
-
10 mM
-
disrupts the oligomer
-
presence of 2 mM EDTA results in total inhibition, under 0.2 mM: no effect
-
higher concentrations
-
does not inhibit all reductase phosphatase isoenzymes
-
51% inhibition at 5 mM
-
complete inhibition
-
complete inhibition at 20 mM
-
no activity is found in the presence of 0.2 mM EDTA without added Mg2+, native enzyme
-
complete inhibition at 1 mM, the activity can be restored by addition of 2 mM Co2+
-
2 mM, complete loss of activity
-
less than 20% activity in the presence of 1 mM EDTA
-
10% inhibition at 1 mM
-
25.8% residual activity at 10 mM
-
10 mM, no residual activity
-
complete loss of activity
-
5 mM, complete inhibition
-
inhibits the nuclease activity by chelating Mg2+
-
metal ions reverse inhibition
-
complete loss of activity, presence of Zn2+ restores the activity
-
1 mM, 30-50% inhibition
-
70% inhibition, 90% of original activity restored with 10 mM Ca2+
-
0.5 mM: 35% inhibition
-
partial inhibition
-
complete inhibition at 1 mM
-
48.5% residual activity at 50 mM
-
about 80% residual activity at 5 mM
-
63% residual activity at 2 mM
-
about 80% residual activity at 1% (w/v)
-
2 mM, 47% residual activity
-
68.3% residual activity at 50 mM
-
65% residual activity at 1 mg/ml, complete inhibition at 5 mg/ml
-
80.92% residual activity at 1 mM
-
49.5% residual activity at 10 mM
-
1 mM EDTA decreases the enzymatic activity to 1.4%
-
about 85% residual activity at 5 mM
-
15% loss of activity at 20 mM
-
0.02 M, 22% loss of activity
-
1 mM, 82% inhibition
-
activity is increased by 25% by 1 mM EDTA but is completely inhibited by 2 mM EDTA
-
competitive, equal inhibition of enzyme from healthy individuals and mucopolysaccharidosis type I patients
-
almost complete inhibition
-
10%, inhibition to 24% of control
-
inhibits 10% at 5 mM
-
1 mM inhibits NMN hydrolysis by 30%
-
90 inhibition at 1 mM
-
2 mM, 70% of initial activity
-
at 1 mM: inhibits uridine hydrolysis by 50%
-
66% cleavage efficiency in presence of EDTA
-
CdpNPT and FtmPT1 are completely inhibited by 5 mM EDTA, 7-DMATS and FgaPT1 show 11.6% and 43.1% relative activity at 5 mM EDTA
-
reversible by divalent cations
-
complete inhibition; complete loss of activity
-
1 mM, complete inhibition
-
0.5 mM, complete inhibition
-
less than 80% residual activity at 1 mM
-
moderate
-
4 mM, complete loss of activity. Ativity may be restored in presence of 8 mM Zn2+
-
isoform LcdB is inactive in the presence of EDTA
-
1 mM, complete inactivation
-
1 mM, complete inhibition. Inhibition is fully reversible upon 50fold dilution and re-activation by Co2+
-
1 mM, 10% inhibition
-
reactivation by zinc, cobalt and manganese ions
-
8% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
-
inhibition at 5 mM
-
0.05 mM, 90% inhibition
-
complete inhibition at 20 mM
-
68% residual activity at 2 mM
-
0.2 mM, 46% inhibition. 0.5 mM, 95% inhibition
-
slight inhibition
-
inhibits interaction between C4b and C2b
-
45% inhibition at 0.01 mM, 64% inhibition at 0.1 mM, 84% inhibition at 0.5 mM
-
5 mM, complete inhibition
-
inhibits binding of integrin alphanybeta3 to the enzyme
-
at 2 mM completely inhibits coagulant and protease activities of RVBCMP
-
10 mM inhibits at pH 3.5
-
1.3 mM, 98% remaining activity, 20 mM, 57% remaining activity
-
mitochondrial Imp1p
-
zinc-selective chelator, inhibits NS2/3 auto-cleavage and NS3 protease activity
-
1 mM, 45% of initial activity
-
41% inhibition at 5 mM
-
complete inhibition at 1-10 mM
-
95% inhibition at 10 mM
-
weak inhibition at high concentration
-
10 mM, 27% inhibition
-
5 mM, 67% inhibition
-
1 mM, 30% inhibition
-
reduces enzyme activity by 30%
-
slight inhibition
-
inhibits binding of MASP-1 to immobilized mannan-binding lectin and L-ficolin/P35, when substituted for Ca2+
-
89% remaining activity at 1 mM, 80% remaining activity at 2 mM
-
low inhibition
-
slight inhibition at 10 mM
-
3.72% inhibition at 0.1 mM
-
6.52% inhibition at 0.1 mM
-
about 60% inhibition at 1-10 mM
-
above 20 mM
-
inhibition of nsp2pro at or above 2 mM EDTA
-
87.3% residual activity at 5 mM
-
2 mM, 12.31% inhibition
-
7% residual activity at 10 mM
-
71.1% residual activity at 50 mM
-
10 mM EDTA causes inhibition of 73.8% of the milk-clotting activity
-
1 mM, 16% loss of activity
-
inhibits the hemorrhagic and proteolytic activity of HR1A
-
Ki is about 50 mM
-
1 mM
-
10 mM, non-specific inhibitor
-
10 mM
-
1 mM, complete inhibition
-
strong
-
moderate inhibitory effect
-
5 mM, complete inhibition
-
1 mM, complete loss of activity
-
alpha-fibrinogenolytic activity is completely inhibited
-
pre-incubation of the enzyme with EDTA blocks the fibrinogenolytic activity
-
eliminates the proteolytic as well as the hemorrhagic activity
-
5 mM, inhibits azocaseinolytic activity
-
10 mM, 1% residual activity
-
complete inhibition
-
about 80% residual activity at 5 mM
-
inhibits 80.4% at 10 mM
-
the Fe-containing compound inhibits the enzyme activity
-
slight inhibitory effect
-
10 mM, 27% inhibition
-
10 mM, 45% inhibition
-
50% inhibition at 1 mM
-
2 mM, 65-80% inhibition
-
40% inhibition at 10 mM
-
slight inhibition at 8 mM
-
26% inhibition at 62 mM
-
1 mM: complete inhibition
-
10 mM: 30% inhibition
-
10 mM: 61% inhibition
-
10 mM, 27% loss of activity
-
complete inhibition at 10 mM, the enzyme irreversibly loses activity upon incubation with a metal chelator
-
0.1 mM, complete inactivation
-
5 mM, 27% inhibition
-
1 mM, 30 min, complete loss of activity. Zn2+, Mg2+, Mn2+ may restore activity
-
21% inhibition at 1 mM
-
2 mM, 30% inhibition
-
5 mM, 43.6% residual activity
-
49% residual activity at 1 mM for IsoI and 40% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII, Fe2+ and Mn2+ restore the enzyme activity partially, while Ca2+ restores it completely
-
reactivation by Mn2+
-
complete loss of activity, fully restored with Mn2+
-
2 mM, 10% inhibition
-
no activity of GCYH-IB is observed in the presence of EDTA
-
reversible inhibition
-
1 mM, 9% inhibition
-
inhibits 99% at 1 mM
-
10 mM, complete inhibition
-
87% inhibition, reactivation by Mn2+ or Co2+
-
complete inhibition at 2 or 0.2 mM
-
weak inhibition
-
strong inhibition at 2 mM
-
2 mM, negative effect on activity
-
0.1 mM, no residual activity
-
0.5 mM, 5.6% inhibition
-
5 mM, 80% of initial activity
-
10 mM, 6% inhibition; 10 mM, at 70°C, weak inhibition
-
weak
-
0.5 mM, 86% inhibition
-
2 mM Mn2+ restores 82% of the activity, 2 mM Zn2+ restores 69% of the initial activity
-
1 mM, 4.3% residual activity
-
1 mM, 15% inhibition
-
complete inhibition at 1 mM
-
10 mM: 66% of maximal activity
-
5% inhibition at 0.24 mM, 45% inhibition at 9.68 mM
-
1 mM, complete inhibition
-
84.4% residual activity after 2h at 30°C in the presence of 100 mM EDTA
-
slight inhibition
-
slight inhibition
-
82% inhibition at 1 mM
-
activity is completely restored by the addition of excess Mn2+
-
complete loss of activity, addition of Fe2+, Fe3+, Co2+, Mn2+, Ni2+, Cu2+, or Zn2+ leads to varying degrees of recovery
-
loses all activity during treatment with EDTA, activity is most efficiently restored by Mn2+
-
complete loss of activity
-
5 mM EDTA results in only weak inhibition (25% reduction in rate)
-
an extensive dialysis of Hsp31 with 10 mM EDTA does not significantly decrease the glyoxalase III activity of more than 30%
-
5 mM, complete loss of activity
-
inhibits 20% at 2.5 mM
-
80% inhibition at 1 mM
-
1 mM, 99% inhibition in absence of GSH, 74% inhibition in presence of 0.5 mM GSH
-
inhibition can be alleviated by either Mn2+ or Co2+
-
10 mM, 100% inhibition
-
1-5 mM: 70% loss of activity
-
10 mM, 17% inhibition
-
enzyme form IM1634 is inhibited to about 10% residual activity by 5 mM EDTA
-
completely abolishes activity against potato pectic galactan
-
10 mM, complete loss of activity
-
2 mM, 14% inhibition
-
1 mM, complete inactivation
-
complete inhibition
-
2.5 mM, complete loss of activity
-
2.5 mM, complete loss of activity
-
2.5 mM, complete loss of activity
-
up to 95% loss of activity, isoenzyme QH1, full reactivation by 10 mM Mg2+
-
complete inhibition
-
1 mM, activity is fully restored by the addition of Mg2+ to a saturating concentration of 1 mM. Mn2+ is about half as effective as Mg2+ at 1 mM
-
1 mM, complete loss of activity
-
complete inhibition at 50 mM
-
5 or 10 mM, inhibits beta-pol dRP lyase activity, in contrast to the 8-kDa domain dRP lyase activity that is slightly stimulated. Higher concentrations, 20 and 40 mM restore the beta-pol activity to a level similar to that in the absence of EDTA. The inhibitory effect of EDTA on the beta-pol ectivity is reversed by 25-100 mM NaCl. The same concentration has no effect on the activity of the 8-kDa domain
-
5 mM, complete loss of activity
-
the enzyme is modestly inhibited by EDTA (27% inhibition at 1 mM)
-
above 15 mM
-
2 mM, 13% inhibition
-
70% inhibition at 1 mM
-
7.1 mM, 70% inhibition
-
5 mM. Activity can be restored by the addition of Mg2+ to a concentration of 10 mM
-
only intracellular RNase
-
45% inhibition at 0.1 mM in the absence of Na2S
-
about 50-60% decrease in nitrile formation
-
inhibition of both activities
-
7% inhibition at 1 mM
-
complete inhibition by metal-chelating agents in 50 mM Tris-HCl buffer (pH 8.0) at 30°C
-
complete inhibition
-
1 mM, complete loss of activity
-
reactivated by addition of divalent metal ion in decreasing order: Mn2+, Co2+, Ni2+, Ca2+, Zn2+, Mg2+
-
activity of D-psicose 3-epimerase is 20% after the removal of metal ions by treatment with EDTA
-
complete inhibitory at 10 mM
-
0.25 mM, 50% inhibition
-
reactivation by Co2+, Fe2+, Mo5+
-
inhibits more than 75% at 1 mM
-
EDTA, slight inhibition
-
Zn2+ restores activity
-
addditon of 5mM EDTA results in almost complete loss of activity
-
84% residual activity at 1 mM
-
abolishes autophosphorylation and catalytic activity
-
31% residual activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)
-
5 mM, complete inhibition; 5 mM, complete inhibition
-
the complex Pus1/tRNAVal is sensitive to the presence of EDTA
-
1.3 mM
-
inhibits activity in cell free extract containing the enzyme
-
the enzyme is partially sensitive to EDTA
-
about 40% residual activity at 1 mM
-
compete inhibition at 1 mM, addition of M2+ to the apoenzyme results in a complete restoration of the original activity
-
10 mM, 25% inactivation
-
10 mM, weak
-
-
-
isoform Facl1 shows 12% residual activity and isoform Facl2 shows 26% residual activity at 1 mM
-
-
-
0.5 mM, reduces the enzyme activity to 1.4% of the maximal activity
-
-
-
-
-
10 mM
-
10 mM, complete inhibition
-
the enzyme is almost completely inhibited by 5 mM EDTA
-
causes maximal inhibition of either the isolated enzyme, or the activity of the crude membrane extract by 63% with a half-maximal effect at 21 mM
-
complete inhibition at 10 mM
-
complete inhibition, addition of excess Mg2+ to EDTA-containing samples restores labeling
-
complete inhibition at 2 mM
-

Metals and Ions (55 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates at 2.0 mM, Zn2+ treatment leads to the formation of a bigger oligomer of CAD which is catalytically inactive. EDTA treatment prevents the formation of the bigger CAD oligomer and hence increases the CAD activity
-
1 mM, 85.7% residual activity
-
enhances activity
-
activates to 127% activity compared to the control activity at 1 mM and to 163% at 10 mM
-
activates to 127% activity compared to the control activity at 1 mM and to 163% at 10 mM
-
activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM
-
1 mM, about 155% of initial activity
-
112.93% activity compared to no addition 100%
-
1 mM, 86% residual activity
-
slight activating at low buffer concentrations
-
5 mM, 27% increase of activity at pH 7.5
-
activates slightly
-
assay with 25 mM
-
115.43 activity at 1 mM
-
10 mM, 75% activity retains
-
1 mM, 25% inhibition of hydrolysis reaction, transfer reaction increases to 388%
-
slight stimulation
-
1 mM relative activity: 106.4%
-
activation
-
assay with 0.25 mM EDTA
-
229% activity at 1 mM
-
EDTA does not affect the enzyme activity
-
18% activation at 1 mM, 9% at 10 mM
-
relative activity in presence of EDTA 10mM 104%
-
slightly enhances activity
-
2 mM, 139% of initial activity
-
slightly activating
-
reduces the activity in the range of 10-50%
-
activates at 1 mM
-
5 mM, 10% increase in activity
-
5 mM, 86% residual activity
-
64% residual activity
-
the enzyme activity is significantly promoted at 1 mM EDTA
-
inhibits enzyme, 1, 3, and 10 mM tested
-
results in unfolding and loss of catalytic activity at 10 mM
-
slight activation
-
relative activity: 14%
-
1 mM in enzyme assay
-
the enzyme activity is increased 2.1fold at 0.1 mM EDTA in the presence of Na2S
-
complete inhibition, provokes a profound conformational change
-
119% relative activity at 5 mM
-

3D Structure of Enzyme-Ligand-Complex (PDB) (52 results)

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Enzyme Kinetic Parameters

kcat Value (Turnover Number) (10 results)

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EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (10 results)

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EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE

Ki Value (34 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.276
-
pH 5.0, temperature not specified in the publication
0.027
-
-
0.015
-
pH 7.5, 22°C
10
-
malE-malF mRNA transcripts incubated at 37°C
0.2
-
-
0.7
-
pH 7.8, 37°C, in presence of 1,10-phenanthroline
0.007
-
-
50
-
-
0.815
-
-
0.2
-
-
0.001
-
-

IC50 Value (37 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
46.75
-
isoform sPPO, at pH 6.8 and 25°C
0.5
-
at pH 7.0 and 30°C
2
-
in 10 mM sodium phosphate buffer, at pH 8.0 and 22°C
26.4
-
-
0.0003
-
IC50 0.0003 mM
2.4
-
-
29
-
at pH 7.5 and 37°C
0.01
-
at pH 9.0 and 30°C
0.005
-
pH 7.2, 23°C
0.01
-
at pH 8.0 and 32°C
0.212
-
IC50: 0.212 mM
1
-
in 50 mM phosphate buffer (pH 7.4), at 30°C
2.26
-
IC50: 2.26 mM
4.4
-
at 30°C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2
20
-
in 50 mM Tris (pH 7.5) containing 0.3% (v/v) Triton X-100, at 37°C
0.33
-
pH 7.8, 37°C

References & Links

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