Ligand iodoacetamide

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Basic Ligand Information

Molecular Structure
Picture of iodoacetamide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C2H4INO
iodoacetamide
PGLTVOMIXTUURA-UHFFFAOYSA-N
Synonyms:
2-iodo-acetamide, 2-Iodoacetamide, alpha-Iodoacetamide, iodacetamide, iodoacetamid, iodoacetoamide, Monoiodoacetamide

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
iodoacetamide + reduced thioredoxin = ?
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (32 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM activates up to 25fold
-
at 1 mM 140% of the activity without activator, at 10 mM 220% of the activity without activator
-
1 mM, 1.3fold activation
-
1 mM, relative activity 101%
-
stimulatory on solubilized enzyme from microsomes
-
slightly activating
-
relative activity 105%
-
slight activation
-
10 mM, 20% activation
-
1 mM: slight activation
-
104.3% activity at 10 mM
-
enhances activity
-
stimulates
-
5 mM, 2fold stimulation
-
131% activity at 1 mM
-
stimulates
-
induces expression of heavy subunit
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Inhibitor in Enzyme-catalyzed Reactions (805 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
200 mM, 90% inhibition
-
NADH 0.4 mM protects
-
86% inhibition at 1 mM
-
1 mM, slight inhibition
-
46% inhibition at 1 mM
-
41% inhibition at 1 mM
-
almost complete inhibition at 0.25 mM
-
almost complete inhibition at 0.25 mM
-
slight
-
slight inhibition
-
slight inhibition
-
41% inhibition at 1 mM
-
slight
-
1 mM, 20% inhibition
-
5% inhibition at 1.0 mM, 22% at 10 mM
-
weak inhibition
-
strong inhibition, 10 mM
-
1 mM, 78% inhibition
-
1 mM, complete inhibition
-
effective inhibitor
-
50 mM, 49% residual activity
-
complete inhibition
-
slight
-
inhibition at 50 mM
-
1.0 mM, 30% inhibition
-
0.01 mM, 20% inhibition
-
competitive inhibitor
-
1 mM, catalytic subunit kOLase, 50% residual activity, native enzyme, 80% residual activity
-
at 1 mM less than 5% activity, 2-oxoglutarate and EDTA protects
-
reversed by dithiothreitol
-
inhibition reversed in presence of dithiotreitol
-
14% inhibition at 1 mM, irreversible
-
5 mM, 39% inhibition, 10 mM, 79% inhibition
-
10 mM, 87% residual activity
-
5 mM, 43% inhibition
-
weak
-
85% inhibition at 100 mM
-
1 mM causes 88-96% inhibition
-
at 0.1 mM: 45.4% inactivation in the absence of NADP+, 22% inactivation in the presence of 1 mM NADP+
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate, even in the presence of dithiothreitol
-
equimolar amount reduces benzaldehyde oxidation activity by 44%
-
slight
-
completely inhibits in the presence of 1 mM
-
40% inhibition at 1 mM
-
1 mM, 50% inhibition
-
10 mM causes 96% inhibition
-
0.05 mM, strong inhibition
-
both isoforms
-
0.1 mM, 32% residual activity
-
inactivation at 1 mM, stearoyl-CoA protects, probably due to competition between the two reagents for the active site cysteine
-
0.1 mM concentration 62% inhibition
-
yields di(carboxamidomethyl)molybdopterin cytosine dinucleotide from reaction with the molybdenum cofactor
-
1 mM, about 80% loss of activity after 20 min
-
at 2 mM 19% activity remains
-
2 mM, 73% inhibition
-
1 mM, 11% inhibition
-
1 mM, 50% inhibition
-
at 4 mM, complete inactivation
-
5 mM, in presence of 20 mM, 24% inhibition
-
64% inhibition at 1 mM
-
0.1 mM, 66% inhibition
-
90% inactivation after 15 h, L-glutamine protects from inactivation
-
28% inhibition at 1 mM
-
complete inactivation at 1 mM
-
24% inhibition at 5 mM
-
inhibition reversed by 2-mercaptoethanol
-
inhibition at 1 mM
-
23% inhibition at 10 mM
-
pH 7.5, 40% inhibition at 1 mM
-
loss of 30.6% activity at 10% v/v
-
progressive inhibition, 2 mM GMP protect
-
low inhibition
-
inhibition only of the enzyme with reduced cysteine residues in the catalytic center by alkylation
-
treatment with thiol prior to incubation with GSH and substrate: no inhibition, preincubation with GSH and thiol reagent: inhibition
-
0.3 mM, complete inhibition
-
0.1 mM, 50% inhibition
-
1 mM, 60% inhibition
-
1 mM, 40% residual activity
-
weak
-
slight
-
55% inhibition at 10 mM
-
55% inhibition at 0.5 mM
-
5 mM, 70% inhibition
-
16.7 mM, 53% decrease of activity
-
0.5 mM: 95% inhibition
-
prior incubation of the enzymes with fatty acyl thioesters prevents inhibition
-
complete inactivation
-
15% inhibition at 1 mM, DTT protects
-
0.5 mM, total inhibition
-
70% inactivation after 1 min at 5 mM
-
inactivation in a biphasic manner, half of the activity is lost rapidly and the other half more slowly, tobramycin but not acetyl-CoA protects
-
slight inhibition
-
reacts slowly, relative insenstitive to iodoacetamide. This property distinguishes E2230K from other E2 proteins
-
effective inhibitor, complete inhibition at 1 mM
-
1 mM, 82% inhibition
-
1 mM, 18% residual activity
-
strong inhibition
-
weak
-
strong and irreversible inhibition by thiol directed reagents like 4-chloromercuribenzoate, N-methylmaleimide and iodoacetamide suggest the requirement of free-SH groups for the catalytic activity
-
60% inhibition at 1 mM
-
5 mM, weak
-
10 mM, about 50% inhibition
-
weak
-
1 mM, 65% inhibition
-
49% inhibition at 1 mM
-
1 mM, 10% inhibition
-
slight inhibition of mutant, not wild-type
-
approx. 60% inactivation of amidotransferase activity after 30 min, very weak inactivation of NH3-dependent activity
-
at 1 mM causes an inhibition of 55%, reversed by cysteine
-
1 mM, 44% inhibition
-
IC50: 40 mM for homodimeric enzyme, 8.7 mM for heterodimeric enzyme
-
preincubation, 1 mM, 30 min prior to assay causes 50% inhibition
-
1 mM, 48% loss of activity
-
alkylation, abolishes the dependence on reducing agents
-
inhibition by alkylation of the active site Cys155, pH-dependent, no alkylation below pH 7.0, maximum alkylation at pH 9.0
-
results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue
-
10 mM, completely inhibits 4HB geranyltransferase activity
-
strong inhibition, dithiothreitol partially protects
-
substrates partially protect against inactivation
-
0.05 mM, complete inactivation
-
0.125 mM, 60% inhibition. Preincubation with 0.25 mM dithiothreitol for 5 min partially protects
-
weak
-
20 mM; 49% inhibition
-
wild-type: loss of 56% activity after 30 min at 0.1 mM, mutant C123S is not affected
-
; 1 mM, 6% remaining activity
-
complete inhibition at 20 mM
-
preincubation dramatically inhibits enzyme activity
-
pH 7.5, 30°C, inhibition prevented by presence of 3'-phosphate 5'-sulfatophosphate but not by L-tyrosine methyl ester
-
2.5fold increase at 2 mM
-
modest inactivation
-
no effect at a concentration of 3.3 mM
-
50 mM, 45% inhibition
-
slight inhibition at 10 mM
-
100% inhibition at 5 mM
-
0.5 mM, 30-40% inhibition
-
0.5 mM, strong inhibition
-
slight inhibitory
-
iodoacetamide, but not iodoacetate, reacts with these His residues at pH 8.0, but not at pH 5.5
-
50 mM, 30% inhibition after 1 h at 30°C
-
weak
-
1.0 mM, 16% inhibition
-
2 mM: 50% inhibition
-
weak inhibition
-
1 mM, 20% inhibition
-
slight inhibition at 1 mM
-
5 mM, about 20% inhibition of isozyme IT I, 44% inhibition of isozyme IT II
-
100 mM required for inhibition of more than 50%
-
78% inhibition at 10 mM, 40% inhibition at 1 mM
-
highly inhibitory
-
slight inhibition
-
30% inhibition at 1 mM
-
very slight inhibition
-
weak
-
1 mM, 57% inhibition
-
strongly inhibits the peptidase activity, confirming that Cys100 is a nucleophilic residue
-
0.01 mM, 19% inhibition
-
1 mM, 20% inhibition
-
slight
-
90% inhibition at a concentration of 5 mM
-
10 mM, 27% inhibition
-
0.26 mM, 50% inhibition
-
slight inhibition
-
1 mM, 64% inhibition
-
active site Cys184 of sortase A can be alkylated by iodoacetamide resulting in irreversible modified enzyme. The selenol and thiol of mutant Sec-sortase and mutant Hcy-sortase are sensitive to alkylation as well
-
exceptionally low rat constant for inhibition
-
inhibits desumoylation
-
strong inhibition; strongly inhibits the peptidase activity, confirming that Cys100 is a nucleophilic residue
-
82.1 residual activity at 0.05 mM
-
4 mM iodoacetamide causes inhibition of 7.2% of the milk-clotting activity
-
10 mM, 96% residual activity
-
49.9% residual activity at 4 mM
-
reversible, competitive inhibitor
-
with 20 micromol iodoacetamide the activity is 20% after 10 min
-
slight inhibition
-
slight inhibition at 1 mM
-
complete inhibition at concentrations above 15 mM
-
phosphate protects wild-type enzyme from inactivation, does not affect inactivation of C319S urease
-
weak
-
1 mM, complete inhibition, completely prevented by addition of substrate, the sensitive thiol group is located at the active site
-
very slight inhibition, 1 mM: 2% inhibition
-
7.5 mM: 100% inhibition
-
slight inhibition at 1 mM for both formamidases I and II
-
pH dependent DDAH inactivation, addition of 2.5 mM NG-methyl-L-arginine at pH 8.5 can prevent inactivation by idoacetamide, inactivation may be due to modification at the active site of DDAH, inactivation increases at higher pH values
-
2-mercaptoethanol partially protects
-
less than 10% inhibition
-
1 mM, 16% inhibition
-
76% residual activity at 10 mM
-
pre-incubation results in 25% loss of activity in both cofactor systems
-
1 mM, 56% inhibition
-
in the absence of dithiothreitol, the addition of iodoacetamide (4 mM) results in complete loss of activity
-
partial
-
50 mM, 56% inhibition
-
binds to cysteine residues
-
10 mM, 20 min, 20% inhibition
-
inhibition after prolonged incubation
-
0.01 M, 30% inhibition
-
150 mM, in about 5 min all activity is lost
-
5 mM, 16% inhibition
-
weak
-
1 mM, 70% loss of activity
-
crotonyl-CoA protects
-
22% residual activity at 2.5 mM
-
1 mM, complete inactivation within 3 h
-
0.42 mM, half-life: 12 min. 17 mM, preincubation completely abolishes activity
-
slight
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
-
complete inhibition
-
weak noncompetitive inhibitor
-
60% inhibition, protection by 2,3-diphosphoglycerate; protection by 2,3-diphosphoglycerate, or 3-phosphoglycerate, or 2-phosphoglycerate
-
mutant enzyme Cys119Ala, is less sensitive than wild type enzyme
-
10 mM, weak
-
more than 90% protection by 10 mM ATP or 10 mM ATP + 10 mM Pro
-
-
-
-
-
-
-
inhibits isozyme MtGS1a
-
2 mM, 30 to 85% loss of activity in 5 min, depending on the enzyme concentration
-
inhibition of Gln-dependent activity, no inhibition of NH4+-dependent activity
-
3-methylcrotonoyl-CoA protects against inactivation
-
inactivation
-

Enzyme Kinetic Parameters

Ki Value (12 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
5.7
-
pseudo-first-order kinetics, pH-independent
0.000075
-
-
12.6
-
pH 7.5, room temperature
0.1
-
-
0.26
-
-
0.311
-
pH 6.3, 38°C

IC50 Value (9 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.04
-
pH 7.8, 65°C
40
-
IC50: 40 mM for homodimeric enzyme, 8.7 mM for heterodimeric enzyme
0.098
-
IC50: 0.098 mM, kidney enzyme
0.003
-
pH 7.4, 37°C
0.003
-
at pH 7.8 and 37°C

References & Links