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Ligand N-ethylmaleimide

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Basic Ligand Information

Molecular Structure
Picture of N-ethylmaleimide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C6H7NO2
N-ethylmaleimide
HDFGOPSGAURCEO-UHFFFAOYSA-N
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Synonyms:
1-ethyl-1H-pyrrole-2,5-dione, 1-ethyl-pyrrole-2,5-dione, ethylmaleimide, N-ethyl-maleimide, N-ethyl maleimide, N-ethylmaleimine, N-ethylmaleinimide, N-ethylmalimide, N-etyhlmaleimide, NEM

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
NADPH + H+ + NEM = NADP+ + ?
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (7 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
N-ethylmaleimide + reduced thioredoxin = ?
show the reaction diagram
-
N-ethylmaleimide + NAD(P)H + H+ = N-ethylsuccinimide + NAD(P)+
show the reaction diagram
-
N-ethylmaleimide + NADPH = N-ethylpyrrolidine-2,5-dione + NADP+
show the reaction diagram
-
N-ethyl-maleimide + NADPH + H+ = ? + NAD+
show the reaction diagram
-
N-ethylmaleimide + NADPH + H+ = ?
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (38 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation of enzyme MGR I, inhibition of enzyme MGR II
-
1 mM, 8.9fold increase in oxaloacetate reduction activity
-
blocking the SH group leads to activation of rBmG6PD activity
-
at 0.1 mM 145% of the activity without activator
-
147% activity at 1 mM
-
1 mM: activation
-
activation by alkylation of sulfhydryl groups
-
stimulatory on solubilized enzyme from microsomes
-
stimulation
-
remarkably enhances the lysine oxidase activity (500% activity at 1 mM (pH 7.0))
-
slight stimulation, 117% of activity
-
ASK1 activation at lower concentrations
-
stimulation about 10-20% at both pH 6.2 and 7.7
-
up to 90% inhibition at pH 6.5-7.0, slight increase of activity at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
-
activates
-
1 mM: slight activation
-
0.01 M, 1.4fold activation
-
0.01 M, 1.4fold activation
-
1 mM, 1.4fold activation
-
slight activation at 10 mM
-
1mM solution increase the reaction rates 2-3fold
-
1 mM, 20% activation
-
8% increase of activity at 10 mM
-
0.1 mM, relative activity 117%
-
0.10-0.20 mM, activity 114%
-
2fold increase in activity after modification of GroEL with 2 mM N-ethylmaleimide
-
Ca2+-activated ATPase
-
biphasic effect: at short reaction times ligase activity increases, but further reaction leads to nearly complete inactivation
-
250fold activation of glutaminase activity. Irreversible inactivation of synthetase activity
-

Inhibitor in Enzyme-catalyzed Reactions (1696 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
10 mM, 81% inhibition
-
1 mM
-
about 90% inactivation
-
94% inhibition at 0.1 mM
-
inactivation via sulfhydryl groups of the enzyme in a nonpolar region
-
1 mM, slight inhibition
-
1 mM, 80% inhibition of reduction and oxidation reaction
-
no exact differentiation between organisms in the reference
-
8§% inhibition at 1 mM
-
46% inhibition at 1 mM
-
53% inhibition at 1 mM
-
inhibition at 1 mM, reversal by an excess of L-cysteine
-
100% inhibition at 1 mM
-
almost complete inhibition at 0.25 mM
-
almost complete inhibition at 0.25 mM
-
slight inhibition
-
weak inhibition of aldehyde reduction
-
D-carnitine dehydrogenase, 1 mM, 77% inactivation after 3 min
-
1 mM, 35% inhibition
-
0.97 mM, 81% residual activity
-
1 mM, no residual activity
-
weaker inhibitor than p-chloromercuribenzoate or HgCl2
-
55% inhibition at 1.0 mM, complete inhibition at 10 mM
-
I80 of less than 0.5 mM
-
3 mM, 2 h, 50% inactivation
-
84% residual activity at 1 mM
-
1 mM, complete inhibition
-
10 mM, strong inhibition
-
2.5 mM, 71% loss of activity after 1 h
-
54% residual activity at 1 mM
-
3 mM, room temperature, pH 9.0, 50% inactivation
-
irreversible inhibition; irreversible inhibition of 17beta-HSD1, preincubation with NADPH protects from inhibition
-
1 mM, 82% inhibition
-
1 mM, 18% inactivation
-
complete inhibition
-
2 mM, 5% residual activity
-
49% inhibition at 2 mM
-
1 mM, 30 min at 4°C, 24% inhibition
-
1 mM, 33.8% inhibition
-
less than 10% inhibition at a concentration of 5 mM
-
50% inhibition at 1 mM
-
33% inhibition at 0.05 mM, 28% inhibition at 0.5 mM
-
60% inhibition of isoform Gpx-1 at 1 mM
-
complete inhibition at 18.3 mM
-
18% inhibition at 5 mM
-
2 mM; 60% inhibition
-
isoform LOX2 exhibits 84% residual activity at 2.8 mM; isoform LOX3 exhibits 51% residual activity at 2.8 mM; isoform LOX4 exhibits 11% residual activity at 2.8 mM; isoform LOX6 exhibits 47% residual activity at 2.8 mM
-
45% inhibition at 0.1 mM
-
35% inhibition at 0.1 mM
-
1 mM, 15% inhibition
-
0.01 mM, 75% inhibition
-
5 mM 30 min
-
1 mM, 58% inhibition of cleavage of D-tryptophan, 45% inhibition of cleavage of L-tryptophan
-
83% residual activity at 0.5 mM
-
10 mM, 31% residual activity; 10 mM, 69% inhibition
-
0.1 mM, catalytic subunit kOLase, 1% residual activity, native enzyme, 81% residual activity
-
0.025 mM, complete inhibition
-
slight
-
less effective than p-chloromercuriphenylsulfonate
-
inactivation
-
2 mM, 30% inhibition of ferredoxinNAP reductase
-
100% inhibition at 2 mM
-
1 mM, 38% inhibition
-
1 mM, 69% inhibition
-
preincubation of the enzyme for 15 min at 14°C, pH 7.7, in the presence of 1.0 mM N-ethylmaleimide inhibits the enzymatic activity approximately by 25%
-
0.1 mM, 59% inhibition
-
0.1 mM, 62% residual activity
-
80-90% inhibition at 0.008 mM per g protein, irreversible by dilution, inhibition does not affect enzyme activity, but retards translocation of the substrate into the cytoplasm
-
complete inhibition at 0.1 M, irreversible
-
90% inhibition at 5 mM
-
partial inhibition, dehydrogenase
-
5 mM inhibits activity by 97%
-
1 mM, 35% inhibition
-
42% inhibition at 0.1 mM
-
0.1 mM inhibits by 38%, 1 mM completely inhibits; complete inhibition at 1 mM
-
98% inhibition at 1 mM
-
protection by substrates
-
1 mM, 58% residual activity
-
higher concentrations
-
1 mM, 10% residual activity
-
DELTA12-desaturase system, enzymatic complex
-
conversion of dehydrogenase type D to oxidase type O, prevented by dithioerythritol but no reversible conversion
-
1 mM, 10 min at 35°C, complete loss of activity
-
0.1 mM, 50% inhibition of intact enzyme, 0.05 mM, 50% inhibition of effector-binding subunit, 0.3 mM, 50% inhibition of non-heme iron subunit
-
10 mM, 67% inhibition
-
67% inhibition at 10 mM
-
2.5 mM, 71% loss of activity after 1 h
-
prevents desuccinylation of the 2-oxoglutarate dehydrogenase complex
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0.1 mM
-
inhibition of the reduction of benzoyladenosine 5'-monophosphate
-
1-3 mM
-
0.1 mM, complete loss of activity
-
18% residual activity at 1 mM
-
1.1 mM, 50% inhibition
-
sulfhydryl inhibitors N-ethylmaleimide -and iodoacetate inhibit arsenate reductase activity by 80% in crude cell-free preparations and by 90% with purified ArsC protein
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3.0 mM, 63% inhibition
-
1 mM, 100% inhibition
-
wild-type and mutant C145S
-
1 mM, 60% inhibition
-
inhibition of 70-80% at concentration of 1 mM
-
protection by FAD
-
tested at 1.0 mM, 94% inhibition
-
5 mM: 53% inhibition, inhibition negligible in the presence of 10 mM glutathione
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1 mM: 79% inhibition
-
0.01 mM, 73% inhibition
-
the modification of the free lipoyl sulfhydryl group renders the intermediate complex inactive
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at 0.8 mM, 44% inhibition
-
5 mM, in presence of 20 mM, 83% inhibition
-
27% inhibition at 0.05 mM
-
87% residual activity at 1 mM
-
1 mM, 90% inhibition
-
90% inhibition at 0.02 mM, inhibition can be prevented by NADH
-
0.13 mM, complete inhibition
-
0.001 M, 26% inhibition
-
0.001 M, 38% inhibition
-
83% inhibition at 5 mM
-
1 mM or 10 mM, complete inhibition
-
0.01 mM, 85% inhibition
-
0.01 mM, 85% inhibition
-
20% residual activity at 2 mM
-
inhibitory to thiolated enzyme, no inhibition of unmodified enzyme
-
inhibition at 1 mM
-
reduction of cytochrome c and formation of superoxide anion
-
1 mM, 86% inhibition
-
1 mM, 77% residual activity
-
both inducible and constitutive enzyme are affected equally at 5 mM
-
47% inhibition at 1 mM
-
treatment with thiol prior to incubation with GSH and substrate: no inhibition, preincubation with GSH and thiol reagent: inhibition
-
1 mM, 54% inhibition
-
0.4 mM, 50% inhibition
-
16% inhibition at 1 mM
-
0.5 mM, 99% inhibition
-
5 mM, 82% inhibition
-
irreversible
-
0.1 mM, 90% inhibition
-
70% inhibition at 4 mM
-
56% inhibition at 0.05 mM
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0.1 mM, 70% inhibition
-
complete loss of activity, second-order kinetics, pH-dependent inactivation, dCMP protects against inactivation, dCMP plus either methotrexate or aminopterin greatly enhances protection, inactivation involves the modification of one thiol group per mol of dimeric enzyme
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74% inhibition at 0.01 mM
-
16 mM, 42% inhibition
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inhibition at 0.5 mM
-
weak
-
1 mM: 100% inhibition
-
weak
-
5 mM, 53% inhibition, 20 min, 20°C
-
5 mM, complete inhibition
-
complete inhibition at 5 mM
-
preincubation with malonyl-CoA or methylmalonyl-CoA protects
-
complete inhibition at 5 mM
-
50% inhibition of ACAT1 at 0.5 mM
-
1 mM N-ethyl-maleimide for 15 min inhibits the enzyme by 56%
-
34.5% residual activity after 1 h at 1 mM
-
preincubation of the acetyl transferase with 0.4 mM N-ethylmaleimide results in large decrease of active citrate lyase formed
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0.1 mM, total inhibition
-
strong
-
inhibition of elongation process and malonyl transfer at 10 mM
-
irreversible, acetyl-CoA protects
-
rapid inactivation at 0.2 mM
-
0.1 mM, 90% inhibition
-
strong
-
inactivation is partially prevented by prior addition of donor or acceptor substrate and by sulfhydryl reducing agents. 0.2 mM inhibits 42%
-
83% inactivation at 3 mM
-
1.25 mM, 30% inhibition
-
10 mM, 35% inhibition
-
92% inhibition at 1 mM
-
binding site is close or at the active site, UDP-N-acetyl-D-glucosamine protects; strong
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at 1 mM, 96% decrease of activity, after addition of dithioerythritol, full activity
-
1 mM, 89% inhibition, 14 mM 2-mercaptoethanol completely restores activity
-
10 mM, 16% activity retains
-
5 mM, pH 7.0, 20°C, 20 min, complete inactivation
-
1 mM, 16.4% residual activity
-
concentration-dependent inactivation
-
20.53% residual activity at 1 mM
-
weak
-
26% remaining activity at 10 mM
-
1 mM, 67% inhibition
-
attacks Cys207
-
90% inhibition at 1 mM
-
1 mM, 10% inhibition
-
slight inhibition of mutant, not wild-type
-
5 mM, 86% inhibition
-
5'-methylthioadenosine partly protects
-
0.5 mM
-
inhibition of RT6.1, no affect on Rt6.2 and Glu207 mutant of RR6.1
-
0.014 mM, 50% non-competitive inhibition, almost complete protection with 0.05 mM CMP-N-acetylneuraminate
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8 mM, 54% inhibition
-
in the absence of sulfhydryl compounds
-
5 mM, 15% activity
-
67% inhibition at 1 mM
-
non-competitive
-
inhibition of gamma-elimination
-
time-dependent inactivation of both MAT activities
-
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
-
alkylation of cysteine residues
-
complete inactivation at 0.1 and 1 mM after 20 min
-
1 mM, 50% inhibition
-
50% inhibition at 5 mM
-
thiol modifiying agent stops CerK acitivity, demonstrating that CerK contains exposed cysteine residues important for enzymatic activity
-
1 mM, 92% inhibition of the 63000 Da isoform, 34% inhibition of the 410000 Da isoform
-
0.02 mM, 50% inhibition
-
0.1 mM, 66% inhibition, 1 mM, 94% inhibition
-
1 mM, 26% inhibition
-
considerable protection
-
5 mM, 77% inhibition, NADH protects, ATP not
-
DTT prevents inhibition
-
0.5 mM, 47% residual activity
-
complete inhibition at 2 mM
-
MEKK1 inhibition through Cys1238 alkylation, Cys1238 is located in the ATP binding domain, no inhibition of MEKK1 mutant C1238V
-
0.125 mM, complete inhibition. Preincubation with 0.25 mM dithiothreitol for 5 min partially protects
-
1.67 mM, 44% inhibition
-
irreversible inactivation
-
weak
-
10 mM, 64% inhibition
-
0.1 mM, reduces the transcription activity down to 10%
-
protected to the extent of about 50% when all of the substrates, UDP-GlcNAc, dolichyl phosphate and Mn2+ are added before addition of the sulfhydryl reagent
-
0.2 mM, 25% remaining activity
-
2-mercaptoethanol protects
-
20% inhibition at 1 mM
-
succinate or acetoacetate protects
-
leads to 24fold reduced enzyme activity at 0.2 mM
-
20% inhibition at 30 mM, 39% inhibition at 60 mM
-
slight
-
inhibits all-trans retinyl-palmitate hydrolase and 11-cis-retinyl-palmitate hydrolase activity of the liver enzyme, inhibits all-trans-retinyl-palmitate hydrolase activity of the pigment epithelium, 1-cis-retinyl-palmitate hydrolase activity of the pigment epithelium is unaffected
-
inhibits all-trans retinyl-palmitate hydrolase and 11-cis-retinyl-palmitate hydrolase activity of the liver enzyme, inhibits all-trans-retinyl-palmitate hydrolase activity of the pigment epithelium, 11-cis-retinyl-palmitate hydrolase activity of the pigment epithelium is unaffected
-
inactivation
-
1 mM, complete inhibition
-
10 mM, 29% inhibition
-
1 mM, 11% inhibition, Phedase type 1
-
the recombinant enzyme shows about 75% residual activity at 1 mM
-
47% inhibition in absence of mercaptoethanol
-
the enzyme is relatively insensitive to sulfhydryl reagents
-
5 mM, complete inhibition
-
little effect on activity at 10 mM
-
slight
-
10 mM, 57% inhibition
-
2.5 mM, 50% inhibition
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
-
1 mM, complete inhibition, 79% inhibition at 0.1 mM
-
slight inhibition
-
pre-treatment of the membrane fraction with 5 mM for 15 min causes 30% inhibition
-
NEM inactivation of Sac1 wild-type completely prevents its inhibitory activity in two-stage fusion reactions compared to mock treated Sac1 wild-type
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with 5 mM 67% reduction of hydrolysis of polydeoxythymidylic acid
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5 mM, 34% inhibition
-
5.8% inhibition at 25 mM
-
no inhibition at pH 5.5, but at pH 5.0
-
complete inhibition at 0.1 mM
-
70% inactivation by 3.3 mM at room temperature after 10 min
-
2 mM: 50% inhibition
-
66% residual activity at 1 mM
-
2 mM, complete inhibition
-
2 mM, 8.4% inhibition
-
IC50: 0.09 mM
-
80% inhibition at 1 mM
-
strong inhibition
-
slight inhibition at 1 mM
-
1.8 mM, 60% of original activity
-
30% inhibition at 1 mM
-
N-acetylglucosaminidase
-
0.1 mM, 24% inhibition
-
30% inhibition at 10 mM
-
50% inhibition at 80 mM
-
after incubation with dithiothreitol at 30°C the thiol-sensitive and the thiol-resistant hydrolase are inactivated by NEM at 4°C , exposure to dithiothreitol at 4°C is sufficient to permit subsequent inactivation of the thiol-sensitive but not the thiol-resistant form by NEM
-
1 mM, 43% inhibition
-
1 mM, 90% inhibition. Inhibition is through covalent modifiction of residue C105
-
22% inhibition at 1 mM
-
30°C, 10 min, 1 mM, 80% loss of activity
-
inhibition of wild-type but not of S120C mutant
-
3 mM, 30% inhibition
-
1 mM, complete inhibition
-
1 mM, 71% inhibition
-
weak
-
inhibits at a molar ratio of inhibitor to enzyme of 20:1
-
10 mM, 22% inhibition
-
weak
-
25% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
-
1 mM, partial inhibition
-
at 37°C and pH of 7.5, 0.1 mM inhibits prosubtilisin JB1 by 15%
-
11.2% inhibition at 5 mM
-
moderately
-
1 mM, enzyme retains 87% of its activity
-
1 mM, complete inhibition
-
44.59% inhibition at 0.1 mM
-
does not completely inhibit NIa activity
-
almost complete inhibition
-
strong inhibition
-
NEM, blocks SENP activity by acting as a general alkylating agent that modifies the active site cysteine in parasite lysates
-
blocks calpain-5 processing
-
5 mM, 95% inhibition
-
88.8% residual activity at 5 mM
-
1 mM, 95% inhibition
-
slow and weak inhibition
-
5 mM, 64% inhibition
-
0.1 mM, about 10% inhibition
-
1 mM, incubation at 30°C for 10 min, complete inhibition
-
1 mM, 24% inhibition
-
1 mM, complete inhibition
-
50% inhibition at 0.25 mM
-
1 mM, complete inhibition
-
with 20 micromol NEM the activity is 0% after 10 min
-
inhibition at 10 mM, C-amidase
-
Ki: 0.86 mM
-
allophanate protects
-
0.25 mM: 50% inhibition of mitochondrial enzyme, 0.5 mM: 50% inhibition of microsomal enzyme
-
1 mM
-
1 mM: 100% inhibition
-
0.1 mM: 3.5% inhibition, 1 mM: 27.4% inhibition, 10 mM: 90.8% inhibition
-
more than 90% loss of activity at 0.05 mM; more than 90% loss of activity at 0.5 mM
-
1 mM, 15 min, no residual activity in absence of substrate S-pantetheine-3-pyruvate, 54% residual activity in presence of the substrate S-pantetheine-3-pyruvate
-
2 mM, about 15% residual activity
-
2 mM, complete inhibition
-
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess N-ethylmaleimide
-
slight inhibition
-
15% inhibition at 5 mM
-
10 mM, complete inhibition
-
2-mercaptoethanol partially protects
-
0.1 mM, 48% residual activity
-
1 mM, 73.8% residual activity
-
12 mM, 14% loss of activity
-
1 mM, 62.6% residual activity; 1 mM, 73.8% residual activity
-
1 mM, 16% inhibition
-
in the presence of N-ethylmaleimide, ATPase activity of the peroxisomal AAA-complex is drastically decreased and the complex dissociates; in the presence of N-ethylmaleimide, ATPase activity of the peroxisomal AAA-complex is drastically decreased and the complex dissociates
-
inhibits GTP hydrolysis, but not the assembly reaction
-
68% inhibition at 1 mM
-
1 mM
-
1 mM
-
0.1 mM, 88% residual activity
-
10 mM, 40% inhibition
-
less than 10% inhibition
-
weak
-
1 mM, 28% loss of carboxylation activity, 6% loss of decarboxylation activity
-
1 mM, 97% inhibition
-
1 mM, 15% inhibition
-
10 mM: 77% of maximal activity
-
1 mM, 30 min, 25°C, 35% inhibition of fHBP HA B, more than 85% of the initial activity of fHBP HA A remains
-
64% inhibition at 10 mM
-
1 mM, 10% inhibition
-
reaction of component I with NH4+ as substrate
-
10% inhibition at 2.5 mM
-
strong inhibition at 5 mM
-
1.0 mM, 71% inhibition
-
60% inhibition by 5 mM, 96% inhibition by 10 mM NEM
-
10 mM, 19% inhibition. 5 mM, 13% inhibition
-
apoenzyme completely inactivated
-
1.0 mM blocks enzymatic reaction
-
0.01 M, 23% inhibition
-
1 mM, 81% inhibition
-
68% inhibition at 0.05 mM
-
1 mM: 93% inhibition
-
slight
-
5 mM, slight inhibition
-
2 mM, 96% inhibition
-
IC50: 0.08 mM
-
reversible by cysteine treatment
-
activity is inhibited by 50%
-
2 mM, complete inhibition
-
5 mM, DsdSC activity with pyridoxal 5'-phosphate 19.5%, without 8.7%
-
1 mM, partial
-
1 mM, complete inactivation within 3 h
-
kinetics, in vivo; pretreatment of reticulocyte lysates with N-ethylmaleimide results in nearly complete inactivation
-
0.42 mM, half-life: 8 min
-
5 mM
-
weak inhibition
-
2 mM, 99% inactivation after incubation for 2 h. Protoporphyrin IX or Zn2+ at concentrations of 0.8 mM and 20 mM, respectively, does not protect
-
1 mM, 22% inhibition
-
weak noncompetitive inhibitor
-
weak
-
weak
-
65% inhibition at 5 mM, 20% inhibition at 1 mM
-
5 mM, approx. 85% inhibition
-
0.1 mM, 32% inhibition
-
in the absence of divalent cations and in the presence of K+ ions
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
acyl-carrier protein or ATP protects
-
10 mM, 87% inhibition
-
-
-
biphasic effect: at short reaction times ligase activity increases, but further reaction leads to nearly complete inactivation
-
complete inhibition in Tris-HCl at 0.1 mM
-
-
-
-
-
0.1 mM and above
-
slight effect
-
irreversible inactivation of synthetase activity. Increase of glutaminase activity
-
50% inhibition at 0.005 mM
-
inhibition of phosphorylation, Cd2+ protects
-
inhibits the formation of the phosphoenzyme, effect can be supressed in presence of Cd2+
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
-
10 mM, 12% residual activity; 10 mM, 14% residual activity
-
1.5% inhibition at 1 mM
-
inhibits ATPase activity of Pot A
-
noncompetitive inhibition
-

Metals and Ions (1 result)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
12% activation at 1 mM
-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (5 results)

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

KM Value (7 results)

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EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.044
-
commentary

Ki Value (22 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.9
-
about
0.25
-
enzyme form FTA and FTB
0.0125
-
-
0.2
-
pH 6.5, 25°C
1.43
-
pH 6.8, 37 C
0.001
-
-
0.001
-
-
0.2
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.5
-
-
0.053
-
pH 6.5, 37°C, versus 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid
80
-
-
3
-
pH 7.8, 37°C
0.03
-
pH 7.8, 37°C
25
-
mitochondrial enzyme
0.209
-
pH and temperature not specified in the publication
0.124
-
pH 6.3, 38°C
0.2
-
-
0.8
-
at 37°C, pH not specified in the publication

IC50 Value (23 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
1
-
at 25°C and pH 9
0.2
-
rapid inactivation, IC50: 0.2 mM
0.5
-
in 50 mM potassium phosphate buffer pH 7.0, at 37°C
0.28
-
at pH 7.5 and 30°C
33
-
IC50: 33 mM
0.1
-
pH 7.5, 30°C
0.01
-
at pH 8.5 and 25°C
0.17
-
IC50: 0.23 mM, reaction with phosphatidic acid. IC50: 0.12 mM, reaction with diacylglycerol diphosphate. IC50: 0.17 mM, reaction with lysophosphatidic acid
2.2
-
in 10 mM sodium phosphate buffer pH 7.0 and at 37°C
2.2
-
-
0.09
-
IC50: 0.09 mM
0.2
-
at pH 8.0 and 37°C
0.1
-
pH and temperature not specified in the publication
0.00014
-
pH 8.9, 23°C
0.05
-
pH 6.5, 31°C
0.08
-
IC50: 0.08 mM
9
-
IC50: 9 mM, almost complete inhibition at 20 mM
0.02
-
potent, IC50 of 0.02 mM

References & Links

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Links to other databases for N-ethylmaleimide

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EXTERNAL LINKS
ChEBI
PubChem
UniChem