Ligand iodoacetic acid

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Basic Ligand Information

Molecular Structure
Picture of iodoacetic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C2H3IO2
iodoacetic acid
JDNTWHVOXJZDSN-UHFFFAOYSA-N
Synonyms:
2-Iodoacetate, 2-iodoacetic acid, CH2ICOOH, ICH2COOH, iodacetic acid, iodoacatate, iodoacetate, monoiodoacetate, mono iodoacetate, Monoiodoacetic acid, monoiodo acetic acid

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
monoiodoacetate + H2O = glycolate + HI
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
monoiodoacetate + H2O = glycolate + HI
show the reaction diagram
-
monoiodoacetate + H2O = glycolate + HI
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (4 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ethyl iodoacetate + H2O = ethanol + iodoacetate
show the reaction diagram
-
-
N6-iodoacetyl-L-lysine + H2O = L-lysine + iodoacetate
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (28 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 1.1fold activation
-
activation of enzyme MGR I, inhibition of enzyme MGR II
-
activity 102.5%
-
stimulation
-
112% activity at 10 mM
-
activation
-
activation
-
10% activation at 5 mM
-
0.1 mM, 28% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
0.1 mM, 28% acti1vation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
rapid induction of isoform PLDbeta1
-
induction in green seedling; induction in green seedling; induction in green seedling
-
5 mM, 105% of initial activity
-
1 mM, relative activity 102.7%
-
activation of isozymes Ic and IIB
-
11% activation at 1 mM
-
1mM, relative activity 103%
-
0.10 mM, activity 105%
-
10 mM, stimulates
-
0.1 mM, 53% increase in activity
-
0.05 mM
-
activates
-
activates up to 80% by low concentrations, in a 1:1 molar ratio with the 40000 MW species of the enzyme
-
in roots in low-phosphorus nutrient solution, iodoacetic acid stimulates the activity of plasma membrane H+-ATPase and phosphorus uptake. The effect is blocked by naphthylphthalamic acid
-

Inhibitor in Enzyme-catalyzed Reactions (924 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 50% inhibition after 14 min, half-inactivation time increases to 29.0 min in the presence of 20 mM D-pantoate, 70% inhibition within 50 min at pH 7.2, 20 mM pantoate decreases inactivation from 70 to 30%
-
10% inhibition at 1 mM
-
85% inhibition at 1 mM
-
10 mM, 95% inhibition, prevented by 10 mM glutathione
-
70% remaining activity at concentration 1 mM
-
complete inhibition at 2 mM
-
sulfhydryl reagents, slightly inhibitory
-
62% inhibition at 10 mM
-
1 mM, 56% residual activity
-
42% inhibition of oxidation and 19% inhibition of reduction at 10 mM
-
complete inhibition at 0.05 mM
-
50% inhibition at 0.1 mM
-
to some extent
-
slight inhibition
-
complete inhibition at 10 mM
-
weak inhibition of aldehyde reduction
-
27% inhibition at 1 mM
-
1 mM, 16.4% residual activity
-
weaker inhibitor than p-chloromercuribenzoate or HgCl2
-
weak inhibition
-
1 mM, 49% inhibition
-
weak
-
1 mM, 29% inhibition with NAD+ as cofactor, 80% with NADP+ as cofactor
-
more inhibitory in intact cells than in cell free extracts
-
isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% inhibition
-
94.5% residual activity at 10 mM
-
5% inhibition at 1 mM
-
10% inhibition at 1 mM
-
33% inhibition at 1 mM
-
1 mM, less than 20% inhibition
-
44% inhibition at 2 mM
-
1 mM, 30 min at 4°C, 15% inhibition
-
63% residual activity at 1 mM
-
1 mM, 17.4% inhibition
-
4.2 mM, 34% inhibition
-
less than 10% inhibition at a concentration of 5 mM
-
1 mM; 1 mM: 46%, 39% and 31% inhibition of isoenzymes Ia, Ib, and II, respectively
-
0.0005 mM, 19% inhibition
-
weak
-
preincubation with substrate protects against inactivation
-
55% inhibition at 0.1 mM
-
55% inhibition at 0.1 mM
-
1 mM, 5% inhibition
-
5 mM 30 min
-
1 mM, 12% inhibition of cleavage of D-tryptophan, 7% inhibition of cleavage of L-tryptophan
-
cysteine-directed reagent, 1 mM, 42% inhibition
-
40% residual activity at 0.5 mM
-
; 1 mM, complete inhibition
-
less effective than p-chloromercuriphenylsulfonate
-
10 mM, 50% inhibition of ferredoxinNAP reductase
-
55% inhibition at 2 mM
-
2 mM, complete loss of activity
-
0.01 mM, 77% inhibition
-
partial inhibition
-
at 1 mM 100% inhibition of 17alpha-hydroxylation and 50% inhibition of lyase activity
-
46% inhibition at 1 mM
-
5 mM, 23% inhibition
-
57% inhibition at 0.5 mM
-
weak
-
DELTA12-desaturase system, enzymatic complex
-
inhibition reversed by addition of GSH or cysteine
-
23.5% inhibition at 1 mM
-
21% inhibition at 1 mM
-
10 mM, 50% inhibition
-
50% inhibition at 10 mM
-
preincubation with glyceraldehyde-phosphate, 10fold molar excess over iodoacetate, prevents inactivation
-
slowly
-
1 mM, isozymes A, 83% inhibition, isozyme C, 100% inhibition
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
-
31% inhibtion at 1 mM; 69% remaining activity at an inhibitor concentration of 1 mM
-
18% inhibition in the presence of 1 mM
-
15% inhibition at 1 mM
-
69% residual activity at 1 mM
-
31% inhibition at 1 mM
-
23°C, in a concentration-dependent manner
-
5 mM, 50% inhibition after min
-
5 mM, complete inhibition
-
inactivates wild type enzyme and mutant enzyme C106S, in presence of substrate, arsenate, or the competitive inhibitors phosphate or sulfate, the rate of the alkylation is reduced
-
sulfhydryl inhibitors N-ethylmaleimide -and iodoacetate inhibit arsenate reductase activity by 80% in crude cell-free preparations and by 90% with purified ArsC protein
-
the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited, but protein C is protected from inactivation by treatment acetyl phosphate
-
recombinant and native isozyme type III
-
3.3 mM, 29% inhibition
-
1.0 mM, 9% inhibition
-
inhibition of 70-80% at concentration of 1 mM
-
1 mM, 34% inhibition
-
slight inhibition
-
slight inhibition
-
50% inhibition of apoenzyme at 2 mM, not inhibitory for the holo form
-
1 mM, 8% inhibition
-
50 mM, partial
-
weak
-
1 mM, 30°C, 15% loss of aminating activity
-
81.6% residual activity at 1 mM
-
68% inhibition at 0.1 mM
-
0.1 mM, 62% inhibition
-
15% inhibition at 1 mM
-
10% inactivation at 1 mM
-
1.0 mM, 9% inhibition
-
complete inhibition at 1 mM
-
3 mM
-
64% inhibition
-
progressive inhibition, 2 mM GMP protect
-
partial
-
low effect
-
in presence of NADH or dihydrolipoamide
-
0.054 mM, 57% inhibition
-
1 mM, 19% inhibition
-
1 mM, 51% residual activity
-
0.5 mM, 70% inhibition
-
complete inhibition at 10 mM
-
complete inhibition at 100 mM, 79% inhibition at 10 mM
-
complete inhibition at 100 mM, 89% inhibition at 10 mM
-
5 mM, 28% inhibition, production of methyl iodide
-
slight inhibition
-
weak
-
83% inhibition at 3.3 mM
-
inhibition at 0.5 mM
-
76% inactivation after 4 min at 5 mM
-
5 mM, complete inhibition
-
0.01 mM, 71% inhibition
-
1 mM, 18% residual activity
-
5 mM, 6% residual activity
-
weak inhibition
-
0.2 mM inhibits the enzyme 70%
-
0.001-0.01 mM: 50-70% inhibition
-
30% inhibition at 1 mM
-
1 mM, 47% inhibition
-
10 mM, 84% activity retains
-
slight inhibition
-
98.9% inhibition at 25 mM
-
10 mM, 35% inhibition
-
1 mM, 91% inhibition
-
1 mM, complete inactivation
-
0.5 mM, 24% inhibition
-
1 mM, 75% inhibition
-
0.004 M, 95% inhibition
-
60% inhibition at 10 mM
-
1 mM, 56% inhibition of the 63000 Da isoform, no inhibition of the 410000 Da isoform
-
0.1 mM, complete loss of activity
-
1 mM, 41% inhibition
-
5 mM, 87% inhibition, NADH protects
-
1.67 mM, 12% inhibition
-
0.05 mM, 50% inhibition
-
DNA polymerase beta
-
1 mM, 42% remaining activity
-
weak inhibition
-
slight inhibition
-
plasmalogen-specific PLA2
-
1 mM inhibits 5% of the activity
-
69% inhibition of D-glucose 1-phosphate hydrolysis by 10 mM
-
50 mM, 30% inhibition after 1 h at 30°C
-
30% inhibition at 10 mM
-
70% inhibition at 1 mM
-
95% inhibition at 1 mM
-
77% inhibition by 1 mM
-
still 60.1% relative activity
-
weak inhibition
-
1 mM, about 80% inhibition
-
93% residual activity at 1 mM
-
30.33% residual activity at 10 mM
-
inhibition of beta-xylosidase A
-
strong inhibition
-
34% inhibition at 5 mM
-
1 M, 10% loss of activity
-
complete inhibition at 2.5 mM
-
with 1 mM 73% of activity remains
-
5 mM, 34% inhibition
-
79.7% residual activity at 5 mM
-
5 mM, 17% inhibition
-
5 mM, 3% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, no inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
-
0.01 M, 25% inhibition. 0.02 M 36.1% inhibition
-
12 mM, 17% inhibition
-
weak
-
1 mM, 11% inhibition
-
25% inhibition at 1 mM
-
0.1 mM, complete inactivation
-
inhibition of wild-type but not of S120C mutant
-
1.0 mM inhibitor, 25% inhibition, 5.0 mM inhibitor, 48% inhibition
-
90% inhibition
-
1 mM, 38% inhibition
-
25% inhibition at 1 mM
-
16.5% inhibition at 1 mM; 1 mM, 16.5% inhibition
-
3 mM inhibits at pH 7.5 with casein as a substrate and at pH 3.5 with bovine serum albumin as a substrate
-
1 mM, 10% inhibition
-
5 mM, 17% inhibition
-
1 mM, 92% inhibition
-
0.4 mM, complete inhibition
-
5% residual activity at 2 mM
-
1 mM, 76% inhibition
-
0.05 mM, 80% inhibition
-
0.25 mM, complete
-
exceptionally low rat constant for inhibition
-
weak inhibitor
-
1 mM, 22% inhibition
-
83% inhibition
-
affects specifically MPP, less effective than NEM or PCMB, dithioerythritol protects
-
1.0 mM, 54.04 mM inhibition
-
1 mM, 40% inhibition
-
55% inhibition at 0.25 mM
-
50 mM, strongly inhibited, 80% inhibition, especially more strongly with a progress of purification steps
-
1 mM, 73% inhibition
-
with 20 micromol iodoacetate the activity is 33% after 10 min
-
2.5 mM, 55% inhibition
-
weak
-
weak
-
1 mM: strong inhibition
-
2 mM: strong inhibition, protected partially, about 30%, by preincubation, 15 min, with 20 mM 2-mercaptoethanol
-
4 mM: 100% inhibition
-
1 mM, 28% loss of activity
-
0.1 mM: 40% inhibition
-
weak
-
16% residual activity at 5 mM for IsoI and 13% residual activity at 5 mM for IsoII
-
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess iodoacetic acid
-
slight
-
10 mM, complete inhibition
-
slight inhibition at 1 mM
-
weak
-
0.01 mM: 5% of maximal activity
-
5 mM, complete inhibition
-
0.01 mM 42% inhibition
-
10 mM, 58.8% residual activity
-
inhibitory above 10 mM
-
10 mM, 58.8% residual activity
-
0.5 mM
-
pyridoxal phosphate protects
-
10 mM, 15% inhibition
-
1 mM, 64% remaining activity
-
poor inhibitor
-
68% inhibition at 16 mM, complete inhibition at 35 mM
-
1 mM, 11% inhibition
-
10% inhibition at 10 mM
-
46% inhibition at 5 mM; 50 mM, almost complete inhibition
-
1 mM, 97% inhibition
-
50 mM, 43% inhibition
-
inhibition after prolonged incubation
-
0.01 M, 12% inhibition
-
2.5 mM, 90% inhibition
-
slight
-
weak
-
1 mM, 45% loss of activity
-
1 mM, 94% inhibition
-
1 mM, 86% loss of activity
-
1 mM, complete inactivation within 3 h
-
inhibition to a minor degree, completely reversible
-
weak inhibition
-
12% inhibition at 1 mM
-
weak
-
10 mM, more than 95% inhibition
-
0.7 mM, 100% inhibition
-
1 mM, 80% inhibition
-
irreversibly inactivates
-
75 mM, 100% inhibition
-
1 mM and above
-
specific reaction with subunit acyl carrier protein
-

Metals and Ions (2 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
5 mM, 43% residual activity
-
10 mM, activates 1.3fold
-

Enzyme Kinetic Parameters

KM Value (1 result)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
1.1
-
-

Ki Value (2 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.145
-
30°C, pH 7.2
0.179
-
pH 6.3, 38°C

IC50 Value (3 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
10
-
pH and temperature not specified in the publication

References & Links