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1,2-dithioglycerol
-
competitive
1,2-Ethanedithiol
-
competitive
1,3-propanedithiol
-
competitive
1,4-Butanedithiol
-
competitive
1,4-dioxane
30%, 530% inactivation of the initial values following 5 h incubation at 50°C
1,4-dithioerythritol
-
competitive
1,4-dithiothreitol
-
competitive
1-butyl-3-methylimidazolium tetrafluoroborate
1-hydroxypyridine-2-thione
-
competitive
1-thio-1-phenylmethane
-
competitive
1-thioacetamide
-
competitive
1-thioacetate
-
competitive
1-thiobutane
-
competitive
1-thioethane
-
competitive
1-thioglycerol
-
competitive
1-thiopropane
-
competitive
1-thiosorbitol
-
competitive
12-hydroxydodecanoate
-
-
1H,1H-heptafluorobutanol
strong inhibitor
2,4-dinitrophenol
-
1 mM, complete inhibition
2-Chloroethanol
-
competitive towards ethanol
2-mercapto-1-methylimidazole
-
competitive
2-mercaptobenzimidazole
-
competitive
2-mercaptobenzothiazole
-
competitive
2-mercaptoimidazole
-
competitive
2-phenylethanethiol
-
competitive
2-propanol
120125% activation after incubation for 25 h in the presence of 17% 2-propanol. High concentration (30%) result in enzyme inactivation to 530% of the initial values following 5 h incubation at 50°C
2-pyridylethanethiol
-
competitive
2-thioacetate
-
competitive
2-thiobutane
-
competitive
2-thiopropane
-
competitive
2-thiopyridine
-
competitive
2-thiopyrimidine
-
competitive
3-butylthiolan 1-oxide
-
dead-end inhibitor to the enzyme-cofactor complex, inhibition of oxidation reaction
3-mercapto-1,2,4-triazole
-
competitive
3-thiopropionate
-
competitive
4-androsten-3,17-dione
-
competitive against substrate cyclohexanone
4-bromobenzyl alcohol-NAD+
-
-
4-methylbenzyl alcohol-NAD+
-
-
5-beta-D-ribofuranosylnicotinamide adenine dinucleotide
-
potent and specific inhibitor
5-hydroxymethylfurfural
-
-
5alpha-androstan-17beta-ol-3-one
-
i.e. 5alpha-dihydrotestosterone, allosteric, competitive against substrate cyclohexanone, noncompetitive against NAD+ nd ethanol
6-thioguanine
-
competitive
6-thioguanosine
-
competitive
8-Amino-6-methoxyquinoline
-
-
8-hydroxyquinoline 5-sulfonic acid
acetaminophen
-
0.5 mM, 16% inhibition of hepatic allotype ADH1B*1/*1 activity, 6.1% inhibition of hepatic allotype ADH1B*2/*2 activity
acetonitrile
120125% activation after incubation for 25 h in the presence of 17% acetonitrile. High concentration (30%) result in enzyme inactivation to 530% of the initial values following 5 h incubation at 50°C
Acetylsalicylate
-
1 mM, 4.4% inhibition of hepatic allotype ADH1B*1/*1 activity, 2.8% inhibition of hepatic allotype ADH1B*2/*2 activity
all-trans-retinal
-
product inhibition
all-trans-retinoic acid
-
weak feedback inhibition
Antimycin
0.0017 mM, 95% inhibition
Biochanin A
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
CaCl2
-
100 mM, 30% inhibition
caffeic acid
-
mixed type of inhibition
CHAPS
10% (w/v), 59% inhibition
Cibacron blue
-
competitive towards NAD+
cimetidine
-
0.2 mM, 2.5% inhibition of hepatic allotype ADH1B*1/*1 activity, 12% inhibition of hepatic allotype ADH1B*2/*2 activity
CoSO4
1 mM, 11% inhibition
cyanide
-
competitive with nicotinamide nucleotides. NADH increases cyanide-resistance of ADH II
cyclobutyl carbinol
-
complete inhibition in vitro at 890 nM, anti-amoebic activity on trophozoites by growth inhibition of recombinant Escherichia coli cells
Cyclohexanol
-
competitive
cyclohexylformamide
dead-end inhibition pattern
cyclopropyl carbinol
-
complete inhibition in vitro at 1820 nM, anti-amoebic activity on trophozoites by growth inhibition of recombinant Escherichia coli cells
D-glucose
-
enzyme activity decreases to half of its original activity at 4 mg/ml of D-glucose. The thiol groups of alcohol dehydrogenase are involved in binding
daidzein
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
diethyldithiocarbamate
-
competitive
dodecanoic acid
-
inhibits ADH3 irrespective of substrate
ellagic acid
-
mixed type of inhibition
FeCl2
1 mM, 57% inhibition
genistein
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
Glutaraldehyde
-
71% relative activity in the presence of 10 mM glutaraldehyde
glycolaldehyde
slight inhibition
guanidine hydrochloride
-
-
heptane
50% (v/v), 99% loss of activity
hexadecane
50% (v/v), 71% loss of activity
hexadecyltrimethyl-ammonium bromide
1 mM, 79% inhibition
Hg(CH3COO)2
1 mM, 37% inhibition
Hydroxylamine hydrochloride
1 mM, 34% inhibition
isoburyramide
-
competitive towards ethanol and butan-2-ol
isooctane
50% (v/v), 98% loss of activity
Isopropanol
50% (v/v), 88% loss of activity
KCN
-
1 mM, 41% inhibition
methanol
50% (v/v), 30% loss of activity
MgSO4
-
19% inhibition at 1 mM
MnCl2
-
24% inhibition at 1 mM
N-1-methylheptylformamide
-
inhibits isozyme gamma(2)gamma(2)
N-benzylformamide
-
inhibits isozyme beta(1)beta(1)
N-cyclopentyl-N-cyclobutylformamide
-
inhibits isozyme alphaalpha, complex structure
N-ethylmaleimide
-
1 mM, 11% inhibition
N-heptylformamide
-
inhibits isozyme beta(1)beta(1)
Na+
10 mM, 13% loss of activity
NAD+
-
substrate inhibition above 5 mM
NO
-
Cys residues contained within the zinc/thiolate active center may be primary sites of NO interaction
o-phenanthroline
-
loses 30% of its activity immediately on addition of o-phenanthroline
p-chloromercuribenzene sulfonate
Megalodesulfovibrio gigas
-
-
p-hydroxymercuribenzoate
-
-
p-nitrophenol
-
noncompetitive inhibition of the hydrolysis of p-nitrophenyl octanoate
Pectin
-
enzyme activity decreases to half of its original activity at 2 mg/ml of pectin. The thiol groups of alcohol dehydrogenase are involved in binding
pefabloc
10 mM, 32% inhibition
Penicillamine
-
competitive
polyoxyethylene octylphenyl ether
1 mM, 43% inhibition
-
propan-2-ol
-
competitive
pyridoxal 5'-phosphate
-
inactivates by modifying its epsilon-amino group, NAD+ protects
quercetin
-
22% inhibition at 0.01 mM
S-2-Chloro-3-(imidazol-5-yl)propionate
-
inactivation at pH 8.2, R-2-chloro-3-(imidazol-5-yl)propionate has no effect
salicylate
-
1.5 mM, 12% inhibition of hepatic allotype ADH1B*1/*1 activity, 31% inhibition of hepatic allotype ADH1B*2/*2 activity
Sodium dodecyl sulfate
5 mM, complete loss of activity
sodium iodoacetate
-
increasing concentrations od sodium iodoacetate produce a slight decrease in activity
starch
-
enzyme activity decreases to half of its original activity at 10 mg/ml of starch. The thiol groups of alcohol dehydrogenase are involved in binding
syringaldehyde
-
mixed type of inhibition
tert-butanol
50% (v/v), 92% loss of activity
tert-butyl hydroperoxide
-
irreversible, inactivation is associated with -SH group oxidation
testosterone
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
Toluene
50% (v/v), 97% loss of activity
trichloroethanol
-
weak inhibition
Triton X-100
10% (w/v), 78% inhibition
Tween 20
10% (w/v), 82% inhibition
Vanillin
-
mixed type of inhibition
1,10-phenanthroline
-
-
1,10-phenanthroline
-
1 mM, 6% inhibition
1,10-phenanthroline
1 mM, 38% inhibition
1,10-phenanthroline
-
1 mM, complete inhibition
1,10-phenanthroline
-
mixed type inhibition
1,10-phenanthroline
-
inhibition of isoenzyme A2 and C2, no inhibition of isoenzyme B2
1,10-phenanthroline
-
0.2 mM, strong inhibition
1-butyl-3-methylimidazolium tetrafluoroborate
5%, 50% inhibition, presumably due to a competition of the BF4- ion with the coenzyme phosphate moiety for the anion-binding site of the enzyme
1-butyl-3-methylimidazolium tetrafluoroborate
-
2 mM, 35% of initial activity; 2 mM, 65% inhibition
2,2'-bipyridine
-
-
2,2'-bipyridyl
-
1 mM, 11% inhibition
2,2'-bipyridyl
-
1 mM, 78% inhibition
2,2'-bipyridyl
91% relative activity at 10 mM
2,2'-dipyridyl
Megalodesulfovibrio gigas
-
-
2,2,2-Trifluoroethanol
-
-
2,2,2-Trifluoroethanol
-
competitive towards ethanol
2,2,2-Trifluoroethanol
95 mM, 74% inhibition
2-mercaptoethanol
-
1 mM, 19% inhibition
2-mercaptoethanol
-
competitive
2-mercaptoethanol
60% inhibition at 10 mM
4-iodopyrazole
-
-
4-iodopyrazole
-
competitive inhibitor
4-methoxypyrazole
-
1 mM, 28% inhibition
4-methoxypyrazole
-
competitive
4-methoxypyrazole
-
class I ADHs migrate towards cathode on starch gel and are very sensitive to 4-methylpyrazole inhibition, class II ADH migrates slowly towards anode and is less sensitive to 4-methylpyrazole, class II ADH migrates rapidly towards anode and is insensitive to 4-methylpyrazole
4-methoxypyrazole
-
0.1-10 mM, ADH-2 is practically insensitive, ADH-3 is very sensitive
4-methoxypyrazole
-
competitive inhibitor of all four isoenzymes
4-Methylpyrazole
-
-
4-Methylpyrazole
-
class III enzyme is completely insensitive to inhibition
4-Methylpyrazole
-
poor inhibitor, class II isoenzyme
4-Methylpyrazole
-
class III enzyme is completely insensitive to inhibition
4-Methylpyrazole
-
no inhibition by 12 mM
4-Methylpyrazole
-
1 mM, 31% inhibition
4-Methylpyrazole
-
competitive against ethanol
4-Methylpyrazole
-
isoenzyme AA-ADH, BB-ADH and TT-ADH
4-Methylpyrazole
-
inhibits cell protein carbonylation following exposure to crotyl alcohol
4-Methylpyrazole
-
competitive inhibitor
8-hydroxyquinoline 5-sulfonic acid
-
-
8-hydroxyquinoline 5-sulfonic acid
-
-
acetaldehyde
-
product inhibition, 50% inhibition at 16 mM
acetaldehyde
-
linear noncompetitive inhibition
acetaldehyde
slight inhibition
acetaldehyde
-
strong product inhibition
acetone
-
product inhibition
acetone
50% (v/v), 82% loss of activity
Ag+
-
-
Ag+
80% inhibition at 1 mM
Ag+
1 mM, no residual activity
AgNO3
-
1 mM, 37% inhibition
AgNO3
-
0.1 mM, 66% inhibition
Al3+
1 mM, 18.9% of initial activity
Al3+
10 mM, 30% loss of activity
Al3+
slight inhibition at 0.5 mM
Ba2+
-
5 mM, 95% inhibition
Ba2+
-
5 mM, 94% inhibition
BaCl2
-
1 mM, 95% inhibition
BaCl2
-
1 mM, complete inhibition
Ca2+
1 mM, 98.4% of initial activity
Ca2+
49.0% inhibition at 2.0 mM
Ca2+
-
100 mM, 70% of initial activity
Co2+
1 mM, 51.9% of initial activity
Co2+
Megalodesulfovibrio gigas
-
-
Co2+
32.0% inhibition at 1.0 mM
Co2+
1 mM, 19% residual activity
CoCl2
-
1 mM, 37% inhibition
CoCl2
-
15% inhibition at 1 mM
Cr3+
-
5 mM, 88% loss of activity
Cr3+
-
5 mM, 84% loss of activity
Cu2+
1 mM, 99% loss of activity
Cu2+
1 mM, 44.2% of initial activity
Cu2+
over 90% inhibition at 0.25 mM
Cu2+
1 mM, 89% of initial activity
Cu2+
-
100 mM, 76% of initial activity
Cu2+
1 mM, no% residual activity
CuCl2
-
1 mM, complete inhibition
CuCl2
1 mM, 68% inhibition
CuCl2
-
1 mM, complete inhibition
CuCl2
-
1 mM, 24% inhibition
dipicolinic acid
-
-
dipicolinic acid
Zn2+ chelator and inhibitor of ADH
dithiothreitol
-
1 mM, 6% inhibition
dithiothreitol
14% relative activity at 10 mM
DMSO
DMSO inhibits isozyme ADH2-catalysed oxidation in an uncompetitive mode and reduction in a mixed mode; DMSO inhibits isozymes ADH1C-catalysed oxidation in an uncompetitive mode and reduction in a mixed mode, no inhibition is detected with isozyme ADH3; DMSO inhibits isozymes ADH4-catalysed oxidation in an uncompetitive mode and reduction in a mixed mode
DMSO
50% (v/v), 29% loss of activity
EDTA
-
67% inhibition of ADH II at 5 mM, 45% inhibition of ADH I at 1 mM, irreversible inhibition, addition of Mg2+ and Zn2+ increase the inhibitory effect
EDTA
-
significant inhibition at 10 mM
EDTA
-
1 mM, 31% inhibition
EDTA
-
25% inhibition at 10.5 mM, 44% inhibition at 21 mM
EDTA
Megalodesulfovibrio gigas
-
-
EDTA
-
31% inhibition at 10.5 mM, 92% inhibition at 21 mM
EDTA
-
15 mM, 85% inhibition
EDTA
-
loses 30% of its activity immediately on addition of EDTA
EDTA
1 mM, 93% of initial activity
EDTA
2.3% relative activity at 10 mM
ethanol
-
substrate inhibition above 0.5 M
ethanol
ethanol competitively inhibits the oxidation of 1-hydroxymethylpyrene by ADH1C and ADH3; ethanol competitively inhibits the oxidation of 1-hydroxymethylpyrene by ADH4
ethanol
50% (v/v), 59% loss of activity
Fe2+
-
5 mM, 61% inhibition
Fe2+
-
5 mM, 48% inhibition
Fe2+
34.3% inhibition at 1.0 mM
Fe2+
1 mM, 60% residual activity
FeCl3
-
1 mM, 34% inhibition
FeCl3
-
0.1 mM, 13% inhibition
FeSO4
-
1 mM, complete inhibition
FeSO4
1 mM, 20% inhibition
glutathione
-
competitive
H2O2
fomation of a disulfide bridge between residues Cys47 and Cys243. Cys residues responsible for ADH inhibition by H2O2 are oxidized to irreversible forms. ADH inhibition by H2O2 is not reversible by DTT
H2O2
-
inactivation is caused by oxidation of its functional Cys residues, coenzyme protects from inactivation
Hg2+
-
-
Hg2+
1 mM, 63% of initial activity
Hg2+
-
100 mM, 33% of initial activity
HgCl2
-
1 mM, complete inhibition
HgCl2
-
1 mM, complete inhibition
HgCl2
1 mM, complete inhibition
HgCl2
-
0.1 mM, 85% inhibition
HgCl2
-
1 mM, complete inhibition
HgCl2
-
1 mM, 67% inhibition
HgCl2
-
complete inhibition at 1 mM
imidazole
-
-
imidazole
-
pure competitive inhibition towards ethanol and (R)-(+)-phenylethanol
imidazole
-
weak inhibition
iodoacetamide
-
-
iodoacetate
1 mM, 12% inhibition
iodoacetate
-
20% inhibition at 1 mM
iodoacetic acid
1 mM, 96% inhibition
iodoacetic acid
-
1 mM, 10% inhibition
Isobutyramide
-
Isobutyramide
-
substrate inhibition, competitive against retinol, noncompetitive against NADH
K+
1 mM, 70.3% of initial activity
K+
10 mM, 29% loss of activity
Li+
-
5 mM, 32% inhibition
Li+
-
5 mM, 28% inhibition
Mg2+
1 mM, 74.35% of initial activity
Mg2+
38.2% inhibition at 2.0 mM
Mg2+
-
100 mM, 67% of initial activity
MgCl2
-
1 mM, 10% inhibition
MgCl2
-
100 mM, 33% inhibition
Mn2+
1 mM, 14.3% of initial activity
Mn2+
Megalodesulfovibrio gigas
-
-
Mn2+
94.8% inhibition at 2.0 mM
NaCl
strong inhibition
NaCl
1 mM, 12% inhibition
NADH
-
-
NADH
-
competitive towards NAD+
NADH
inhibitory effects of NADH on the HLADH-catalyzed oxidation
NADH
-
linear competitive inhibition
NADH
-
competitive towards NAD+
NEM
1 mM, complete inhibition
NEM
Megalodesulfovibrio gigas
-
-
NEM
-
17% inhibition at 1 mM
Ni2+
1 mM, 72.7% of initial activity
Ni2+
Megalodesulfovibrio gigas
-
-
Ni2+
10 mM, 46% loss of activity
Ni2+
55.8% inhibition at 2.0 mM
NiCl2
-
1 mM, 93% inhibition
NiCl2
1 mM, 79% inhibition
NiCl2
-
1 mM, complete inhibition
octanoic acid
interacts with the catalytic zinc ion, binding structure
octanoic acid
-
competitive inhibition of the hydrolysis of p-nitrophenyl octanoate
octanoic acid
dead-end inhibition pattern
Pb2+
-
5 mM, 96% inhibition
Pb2+
-
5 mM, 98% inhibition
PbCl2
-
1 mM, 24% inhibition
PbCl2
-
1 mM, complete inhibition
PbCl2
-
1 mM, 63% inhibition
PCMB
-
1 mM, complete inhibition
PCMB
1 mM, complete inhibition
PCMB
-
0.1 mM, complete inhibition
PCMB
Megalodesulfovibrio gigas
-
-
pyrazole
-
pyrazole-sensitive enzyme forms ADH-1, ADH-2, ADH-3 and the pyrazole-insensitive form ADH-An
pyrazole
-
0.05 mM, 50% inhibition
pyrazole
-
no inhibition at 1.0 mM
pyrazole
-
organism has a pyrazole-sensitive isoenzyme and a pyrazole-insensitive enzyme
pyrazole
-
inhibition of isoenzyme A2 and C2. Isoenzyme B2 is insensitive to pyrazole inhibition with trans-2-hexen-1-ol as substrate
pyrazole
-
0.05 mM, complete inhibition
pyrazole
-
0.1-10 mM, ADH-2 is practically insensitive, ADH-3 is very sensitive
pyrazole
-
competitive inhibitor
pyrazole
potent inhibitor, binding to the enzyme-NAD+ complex. The enzyme made with NADH and pyrazole has the closed conformation with NADH bound in the active site and the classical coordination of the zinc with a water
pyrazole
-
organism has a pyrazole-sensitive isoenzyme and a pyrazole-insensitive enzyme
pyrazole
-
competitive towards ethanol
pyrazole
-
strong inhibition
Pyridine
-
-
SDS
1 mM, 91% inhibition
SDS
1 mM, 2.9% of initial activity
SDS
10% (w/v), 95% inhibition
SDS
-
in the presence of the surfactant the initial reaction rates are consistently lower than in pure buffer at all the surfactant concentrations considered (0.5-50 mM). This effect is mainly due to an increase in the dissociation constant of beta-NAD+ which reaches its maximum value (7.1 mM) at the critical micelle concentration. Above the critical micelle concentration the effect of the surfactant is mainly due to an increase in the Michaels constants of the alcohol, with values of 41 mM for 15 mM SDS and 50 mM for 50 mM SDS
SDS
0.4% relative activity at 10% (v/v)
trifluoroethanol
-
competitive against retinol, noncompetitive against NAD+
trifluoroethanol
potent inhibitor, binding to the enzyme-NAD+ complex
Tween 80
-
competitive, stabilizes the retinoid compounds, elevates the Km values of the substrates, most effective at 0.1% w/v
Tween 80
10% (w/v), 89% inhibition
Tween 80
13% relative activity at 10% (v/v)
Urea
5 M, 41% inhibition
Urea
1% relative activity at 5 M
Zn2+
-
0.1 mM, 20% decrease of activity
Zn2+
-
5 mM, 17% loss of activity
Zn2+
1 mM, 30.5% of initial activity
Zn2+
Megalodesulfovibrio gigas
-
-
Zn2+
-
5 mM, 29% loss of activity
Zn2+
-
complete inhibition
Zn2+
65.2% inhibition at 0.5 mM
Zn2+
1 mM, 91% of initial activity
Zn2+
91% relative activity at 10 mM
Zn2+
1 mM, 0.5% residual activity
ZnSO4
-
1 mM, complete inhibition
ZnSO4
1 mM, 9% inhibition
ZnSO4
-
26% inhibition at 1 mM
Zr2+
-
5 mM, 72% inhibition
Zr2+
-
5 mM, 78% inhibition
additional information
ADH activity is not significantly affected by diamide + GSH treatment. NAD+ and NADH binding to ADH reduce enzyme sensitivity to H2O2 and diethylamine NONOate
-
additional information
-
ADH activity is not significantly affected by diamide + GSH treatment. NAD+ and NADH binding to ADH reduce enzyme sensitivity to H2O2 and diethylamine NONOate
-
additional information
-
inactivator from rice seedlings
-
additional information
-
inactivator from rice seedlings
-
additional information
-
design of inhibitors
-
additional information
-
thiols and dithiols have their main effect, at the enzyme-NAD+-thiol complex level, by competition with alcohol for the catalytic zinc
-
additional information
high concentrations of alcohols can bind to the enzyme-NADH complex and activate or inhibit the enzyme
-
additional information
no inhibitory: Triton X-100 at 1%, guanidinium hydrochloride at 0.2 M
-
additional information
-
no inhibitory: Triton X-100 at 1%, guanidinium hydrochloride at 0.2 M
-
additional information
-
inactivator from rice seedlings
-
additional information
-
no inhibition by 4-methylpyrazole
-
additional information
-
inactivator from rice seedlings
-
additional information
-
inactivator from rice seedlings
-
additional information
presence of EDTA is not significantly inhibitory. Incubation with 100 mM EDTA at 70°C for 2 h results in loss of half of the enzyme activity. The enzyme is highly stable in the presence of up to 8 M urea or up to 6 M guanidine hydrochloride
-
additional information
-
presence of EDTA is not significantly inhibitory. Incubation with 100 mM EDTA at 70°C for 2 h results in loss of half of the enzyme activity. The enzyme is highly stable in the presence of up to 8 M urea or up to 6 M guanidine hydrochloride
-
additional information
-
not affected by Cu2+
-
additional information
-
use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase
-
additional information
the chlorides of Li+, Na+, K+, Ca2+, Mg2+, and Mn2+ do not affect the activity of the enzyme, whereas the sulfate of heavy metal ions such as Fe2+, Co2+, and Cu2+ cause a slight inactivation
-
additional information
the chlorides of Li+, Na+, K+, Ca2+, Mg2+, and Mn2+ do not affect the activity of the enzyme, whereas the sulfate of heavy metal ions such as Fe2+, Co2+, and Cu2+ cause a slight inactivation
-
additional information
-
the chlorides of Li+, Na+, K+, Ca2+, Mg2+, and Mn2+ do not affect the activity of the enzyme, whereas the sulfate of heavy metal ions such as Fe2+, Co2+, and Cu2+ cause a slight inactivation
-
additional information
-
inactivator from rice seedlings
-
additional information
-
inactivator from rice seedlings
-
additional information
-
no inhibition by 4-chloromercuribenzoate at 0.1 mM and by CuSO4 at 1 mM, poor effects by EDTA, 1,20-phenanthroline, 2-mercaptoethanol, and DTT
-