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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Homo sapiens

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.1 alcohol dehydrogenase
IUBMB Comments
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adh, alcohol dehydrogenase, aldehyde dehydrogenase, adh1b, short-chain dehydrogenase/reductase, ssadh, adh1c, yeast alcohol dehydrogenase, retinol dehydrogenase, faldh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 kDa allergen
-
-
-
-
ADH-A2
-
-
-
-
ADH-B2
-
-
-
-
ADH-C2
-
-
-
-
ADH-HT
-
-
-
-
ADH1
-
-
ADH1B
-
-
ADH1C
isozyme
ADH1C*1
-
-
ADH1C*2
-
-
ADH2
isozyme
alcohol dehydrogenase (NAD)
-
-
-
-
alcohol dehydrogenase 1
-
-
Alcohol dehydrogenase-B2
-
-
-
-
aldehyde dehydrogenase
-
-
aldehyde reductase
-
-
-
-
ALDH
-
-
aliphatic alcohol dehydrogenase
-
-
-
-
class I ADH
class II ADH
class III ADH
-
-
class IV ADH
dehydrogenase, alcohol
-
-
-
-
ethanol dehydrogenase
-
-
-
-
FALDH
-
-
-
-
FDH
-
-
-
-
Gastric alcohol dehydrogenase
-
-
-
-
Glutathione-dependent formaldehyde dehydrogenase
-
-
-
-
GSH-FDH
-
-
-
-
NAD-dependent alcohol dehydrogenase
-
-
-
-
NAD-specific aromatic alcohol dehydrogenase
-
-
-
-
NADH-alcohol dehydrogenase
-
-
-
-
NADH-aldehyde dehydrogenase
-
-
-
-
Octanol dehydrogenase
-
-
-
-
primary alcohol dehydrogenase
-
-
-
-
Retinol dehydrogenase
-
-
-
-
yeast alcohol dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + NAD+ = an aldehyde + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alcohol:NAD+ oxidoreductase
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-72-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E)-4-hydroxynon-2-enal + NADH + H+
(2E)-non-2-ene-1,4-diol + NAD+
show the reaction diagram
-
substrate of isozyme ADH4
-
-
r
(S)-2-butanol + NAD+
butanone + NADH + H+
show the reaction diagram
-
-
-
-
r
1-butanol + NAD+
butanal + NADH + H+
show the reaction diagram
-
-
-
-
?
1-hydroxymethyl-6-methylpyrene + NAD+
1-formyl-6-methylpyrene + NADH + H+
show the reaction diagram
-
-
-
r
1-hydroxymethyl-8-methylpyrene + NAD+
1-formyl-8-methylpyrene + NADH + H+
show the reaction diagram
-
-
-
r
1-hydroxymethylpyrene + NAD+
1-formylpyrene + NADH + H+
show the reaction diagram
-
-
-
r
1-octanol + NAD+
octanal + NADH + H+
show the reaction diagram
substrate for isozyme ADH3
-
-
r
11-cis-retinol + NAD+
11-cis-retinal + NADH
show the reaction diagram
-
-
-
-
?
12-hydroxydodecanoate + NAD+
12-oxododecanoic acid + NADH
show the reaction diagram
-
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH
show the reaction diagram
-
no activity with isozyme ADH1
-
-
?
16-hydroxyhexadecanoate + NAD+
16-oxohexadecanoic acid + NADH
show the reaction diagram
-
-
-
-
?
17beta-hydroxyetiocholan-3-one + NAD+
ethiocholan-3,17-dione + NADH
show the reaction diagram
-
-
-
-
?
2-deoxy-D-ribose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
2-hydroxymethylpyrene + NAD+
2-formylpyrene + NADH + H+
show the reaction diagram
-
-
-
r
3,4-dihydro-retinol + NAD+
3,4-dihydro-retinal
show the reaction diagram
-
-
-
-
r
3-nitrobenzaldehyde + NADH + H+
3-nitrobenzyl alcohol + NAD+
show the reaction diagram
-
class IV isozyme, reductive activity
-
-
?
3-phenyl-1-propanol + NAD+
3-phenyl-1-propanone + NADH
show the reaction diagram
-
-
-
-
?
3-pyridylcarbinol + NAD+
pyridine-3-carbaldehyde + NADH
show the reaction diagram
-
-
-
-
?
4-hydroxy-retinol + NAD+
4-oxo-retinal + NADH
show the reaction diagram
-
-
-
-
r
4-hydroxymethylpyrene + NAD+
4-formylpyrene + NADH + H+
show the reaction diagram
-
-
-
r
4-methoxy-1-naphthaldehyde + NAD+
4-methoxy-1-naphthol + NADH + H+
show the reaction diagram
-
fluorogenic substrate of class I and II isozymes
-
-
?
4-methoxy-1-naphthaldehyde + NAD+
4-methoxy-1-naphthyl alcohol + NADH + H+
show the reaction diagram
-
substrate for class I ADH
-
-
?
4-methoxy-1-naphthaldehyde + NADH + H+
4-methoxynaphthalene-1-carbaldehyde + NAD+
show the reaction diagram
-
substrate for class I ADH
-
-
r
4-nitrosodimethylaniline + NAD+
? + NADH + H+
show the reaction diagram
-
photometric assay substrate
-
-
?
5alpha-androstan-17beta-ol-3-one + NADH + H+
3beta,17beta-dihydroxy-5alpha-androstan + NAD+
show the reaction diagram
-
-
-
-
?
5alpha-pregnan-3beta-ol-20-one + NAD+
5alpha-pregnan-3,20-dione + NADH
show the reaction diagram
-
low activity
-
-
?
5beta-androstan-17beta-ol-3-one + NAD+
5beta-androstan-3,17-dione + NADH
show the reaction diagram
-
low activity
-
-
?
5beta-androstan-3beta-ol-17-one + NAD+
5beta-androstan-3,17-dione + NADH
show the reaction diagram
-
-
-
-
?
5beta-cholanic acid-3-one + NADH
5beta-cholanic acid-3-ol + NAD+
show the reaction diagram
-
low activity
-
-
?
5beta-pregnan-3,20-dione + NADH
?
show the reaction diagram
-
-
-
-
?
5beta-pregnan-3beta-ol-20-one + NAD+
5beta-pregnan-3,20-dione + NADH
show the reaction diagram
-
-
-
-
?
6-methoxy-2-naphthaldehyde + NADH + H+
(6-methoxynaphthalen-2-yl)methanol + NAD+
show the reaction diagram
7-cis-retinol + NAD+
7-cis-retinal + NADH
show the reaction diagram
-
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH
show the reaction diagram
-
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
show the reaction diagram
benzyl alcohol + NAD+
benzaldehyde + NADH
show the reaction diagram
-
-
-
-
?
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
show the reaction diagram
-
-
-
-
?
butan-2-ol + NAD+
butan-2-one + NADH
show the reaction diagram
-
-
-
-
?
butanol + NAD+
butyraldehyde + NADH
show the reaction diagram
-
-
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH
show the reaction diagram
-
-
-
-
?
cyclohexanone + NADH + H+
cyclohexanol + NAD+
show the reaction diagram
-
-
-
-
?
digitose + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
ethanol + NAD+
acetaldehyde + NADH + H+
show the reaction diagram
ethylene glycol + NAD+
? + NADH
show the reaction diagram
furfuryl alcohol + NAD+
furfural + NADH
show the reaction diagram
-
-
-
-
?
hexanol + NAD+
hexanal + NADH
show the reaction diagram
-
-
-
-
?
hexanol + NAD+
n-hexanal + NADH
show the reaction diagram
-
-
-
-
?
isobutyl alcohol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
isobutyramide + NAD+
?
show the reaction diagram
-
-
-
-
r
isopentenyl alcohol + NAD+
isopentanone + NADH
show the reaction diagram
-
-
-
-
?
m-nitrobenzaldehyde + NAD+
m-nitrobenzyl alcohol + NADH + H+
show the reaction diagram
-
substrate of class IV ADH
-
-
?
m-nitrobenzaldehyde + NADH + H+
m-nitrobenzyl alcohol + NAD+
show the reaction diagram
-
substrate of class IV ADH isozyme
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
show the reaction diagram
n-butanol + NAD+
butylaldehyde + NADH + H+
show the reaction diagram
n-butanol + NAD+
n-butanal + NADH
show the reaction diagram
-
-
-
-
?
octan-1-ol + NAD+
n-octanal + NADH
show the reaction diagram
-
-
-
-
?
octan-2-ol + NAD+
octan-2-one + NADH
show the reaction diagram
-
-
-
-
?
octanal + NADH + H+
octanol + NAD+
show the reaction diagram
-
-
-
-
?
octanol + NAD+
octanal + NADH
show the reaction diagram
-
-
-
-
?
p-nitrobenzaldehyde + NADH + H+
p-nitrobenzyl alcohol + NAD+
show the reaction diagram
-
substrate of isozyme ADH4
-
-
r
pentanal + NAD+
pentanone + NADH
show the reaction diagram
-
-
-
-
?
pentanol + NAD+
n-pentanal + NADH
show the reaction diagram
-
-
-
-
?
phenylalaninol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
propan-2-ol + NAD+
acetone + NADH
show the reaction diagram
-
-
-
-
?
propanol + NAD+
propionaldehyde + NADH + H+
show the reaction diagram
-
-
-
-
?
retinal + NADH + H+
retinol + NAD+
show the reaction diagram
-
substrate of isozyme ADH4
-
-
r
retinol + NAD+
retinal + NADH
show the reaction diagram
-
-
-
-
?
trans-4-(N,N-dimethylamino)-cinnamaldehyde + NADH
trans-4-(N,N-dimethylamino)-cinnamyl alcohol + NAD+
show the reaction diagram
-
-
-
-
?
tryptophol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
vanillyl alcohol + NAD+
vanillin + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-butanol + NAD+
butanal + NADH + H+
show the reaction diagram
-
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
show the reaction diagram
-
ADH4 might be involved in biosynthesis of retinoic acid
-
-
r
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
isobutyramide + NAD+
?
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
differences in the activities of total ADH and class I ADH isoenzyme between cancer liver tissues and healthy hepatocytes may be a factor in ethanol metabolism disorders, which can intensify carcinogenesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
catalytic zinc
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2,2'-bipyridine
-
-
3-butylthiolan 1-oxide
-
dead-end inhibitor to the enzyme-cofactor complex, inhibition of oxidation reaction
4-androsten-3,17-dione
-
competitive against substrate cyclohexanone
4-bromopyrazole
-
-
4-cyanopyrazole
-
-
4-iodopyrazole
-
-
4-methoxypyrazole
4-Methylpyrazole
4-nitropyrazole
-
-
4-octylpyrazole
-
-
4-pentylpyrazole
-
-
4-propylpyrazole
-
-
5alpha-androstan-17beta-ol-3-one
-
i.e. 5alpha-dihydrotestosterone, allosteric, competitive against substrate cyclohexanone, noncompetitive against NAD+ nd ethanol
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
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
cimetidine
-
0.2 mM, 2.5% inhibition of hepatic allotype ADH1B*1/*1 activity, 12% inhibition of hepatic allotype ADH1B*2/*2 activity
dipicolinic acid
-
-
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
EDTA
-
-
ethanol
ethanol competitively inhibits the oxidation of 1-hydroxymethylpyrene by ADH1C and ADH3; ethanol competitively inhibits the oxidation of 1-hydroxymethylpyrene by ADH4
Isobutyramide
-
substrate inhibition, competitive against retinol, noncompetitive against NADH
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-heptylformamide
-
inhibits isozyme beta(1)beta(1)
NADP+
-
-
pyrazole
salicylate
-
1.5 mM, 12% inhibition of hepatic allotype ADH1B*1/*1 activity, 31% inhibition of hepatic allotype ADH1B*2/*2 activity
sulfonic acid
-
-
trifluoroethanol
-
competitive against retinol, noncompetitive against NAD+
Tween 80
-
competitive, stabilizes the retinoid compounds, elevates the Km values of the substrates, most effective at 0.1% w/v
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
120
(S)-2-butanol
-
-
0.000036 - 0.0038
1-formyl-6-methylpyrene
0.000035 - 0.00149
1-formyl-8-methylpyrene
0.0005 - 0.012
1-formylpyrene
0.00028 - 0.0064
1-hydroxymethyl-6-methylpyrene
0.00031 - 0.059
1-hydroxymethyl-8-methylpyrene
0.00059 - 0.076
1-hydroxymethylpyrene
0.39 - 0.55
1-Octanol
27
1-Pentanol
-
-
0.018 - 0.035
11-cis-retinol
0.047 - 0.23
12-hydroxydodecanoate
0.056
12-Hydroxydodecanoic acid
-
-
0.06
16-hydroxyhexadecanoate
-
0.1 M glycine-NaOH buffer, pH 10.0, 25°C
310
2-deoxy-D-ribose
-
0.1 M glycine-NaOH buffer, pH 10.0, 25°C
0.0021 - 0.009
2-formylpyrene
0.00048 - 0.106
2-hydroxymethylpyrene
560
2-propanol
-
0.1 M glycine-NaOH buffer, pH 10.0, 25°C
0.025 - 0.026
3,4-dihydro-retinal
0.024 - 0.028
3,4-dihydro-retinol
0.032
3-Phenyl-1-propanol
-
0.1 M glycine-NaOH buffer, pH 10.0, 25°C
0.00048 - 0.0038
4-formylpyrene
0.004 - 0.015
4-hydroxy-retinol
0.00037 - 0.04
4-hydroxymethylpyrene
0.017 - 0.027
4-oxo-retinal
0.0036
5alpha-androstan-17beta-ol-3-one
-
pH 7.3, 37°C, ADH1C*2 (gamma2gamma2)
0.046
5beta-androstan-17beta-ol-3-one
-
pH 7.3, 37°C, ADH1C*2 (gamma2gamma2)
0.058
5beta-androstan-3beta-ol-17-one
-
pH 7.3, 37°C, ADH1C*2 (gamma2gamma2)
0.25
5beta-cholanic acid-3-one
-
pH 7.3, 37°C, ADH1C*2 (gamma2gamma2)
0.0036
5beta-pregnan-3,20-dione
-
pH 7.3, 37°C, ADH1C*2 (gamma2gamma2)
0.027
5beta-Pregnan-3beta-ol-20-one
-
pH 7.3, 37°C, ADH1C*2 (gamma2gamma2)
0.011 - 0.023
9-cis-retinol
0.085 - 26
acetaldehyde
0.011 - 0.034
all-trans-retinal
0.009 - 0.033
all-trans-retinol
0.007 - 0.15
benzyl alcohol
0.24 - 0.79
butanol
0.008 - 210
Cyclohexanol
0.022 - 120
ethanol
50 - 290
ethylene glycol
0.13 - 17
Hexanol
10.4 - 150
methanol
0.0074 - 710
NAD+
0.0025 - 260
NADH
2.4 - 9.6
octanal
0.007 - 1.2
Octanol
0.044 - 0.28
Pentanol
0.91 - 1.39
Propanol
0.011 - 0.012
retinol
0.2
tryptophol
-
0.1 M glycine-NaOH buffer, pH 10.0, 25°C
0.034 - 11
Vanillyl alcohol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.17
(S)-2-butanol
-
-
2.83
1-Octanol
-
-
0.183
1-Pentanol
-
-
2.95 - 4
12-hydroxydodecanoate
0.333
12-Hydroxydodecanoic acid
-
-
6.17
16-hydroxyhexadecanoate
-
-
2.83
2-deoxy-D-ribose
-
-
0.75
2-propanol
-
-
0.22 - 1.22
3,4-dihydro-retinal
0.088 - 2.5
3,4-dihydro-retinol
7.5
3-Phenyl-1-propanol
-
-
0.683
3-Pyridylcarbinol
-
pH 7.5, anodic enzyme form
0.092 - 34.2
4-hydroxy-retinol
0.167 - 20
4-oxo-retinal
0.018 - 1.83
all-trans-retinal
0.028 - 0.9
all-trans-retinol
4.67 - 9.17
benzyl alcohol
0.7 - 34.8
butanol
0.583
Cyclohexanol
-
-
0.167 - 30.7
ethanol
0.75
ethylene glycol
-
-
19.5
Hexanol
-
-
0.102
methanol
-
-
0.717
NAD+
-
pH 7.5, anodic enzyme form
3.33
octanal
-
-
0.038 - 8.33
Octanol
0.245 - 16
Pentanol
17.2
Propanol
-
-
0.087 - 0.11
retinol
1.83
tryptophol
-
-
0.467 - 8.67
Vanillyl alcohol
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0047
4-androsten-3,17-dione
-
pH 7.3, 37°C, versus cyclohexanone
0.0047 - 0.028
5alpha-androstan-17beta-ol-3-one
1.7 - 1470
ethanol
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.65
-
-
1.47
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 10.5
-
and a second optimum at pH 10.0-10.5, ADH Indianapolis form 2 and 3
10.4
-
-
10.8
-
-
5.9
-
acetaldehyde reduction, isoenzyme beta1,beta1
7 - 7.5
-
and a second optimum at pH 10.0-10.5, ADH Indianapolis form 2 and 3
7.3
-
assay at
7.4
-
acetaldehyde reduction of isoenzyme beta2,beta2
7.6
-
assay at, class II enzyme, reduction reaction
8
-
assay at, class III enzyme, reduction reaction
8.5 - 8.8
-
ethanol oxidation, isoenzyme beta2,beta2, beta2,beta1, alpha,beta2 and beta2gamma1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10.5
-
pH 8.0: about 40% of maximal activity, pH 10.5: about 85% of maximal activity
8 - 12
-
about 30% of maximal activity at pH 8.0 and at pH 12.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the activity of the class I ADH isoenzyme is significantly lower in the wall of aortic aneurysm than in healthy aorta
Manually annotated by BRENDA team
-
the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy colorectum
Manually annotated by BRENDA team
-
isozyme ADH4
Manually annotated by BRENDA team
-
isozyme ADH4, the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy esophagus
Manually annotated by BRENDA team
-
the activities of total alcohol dehydrogenase, aldehyde dehydrogenase and class I alcohol dehydrogenase isoenzyme between cancer liver tissues and healthy hepatocytes might be a factor in ethanol metabolism disorders which can intensify carcinogenesis
Manually annotated by BRENDA team
-
isozyme ADH1
Manually annotated by BRENDA team
-
isozyme ADH1
Manually annotated by BRENDA team
-
total activity of alcohol dehydrogenase is not significantly different in cancer and normal cells. The differences between enzymes of drinkers and nondrinkers in both cancer and healthy tissue are not significant
Manually annotated by BRENDA team
-
isozyme ADH4
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
the class III enzyme contributes by far the bulk of the total alcohol dehydrogenase activity
Manually annotated by BRENDA team
additional information
-
activity of ADH isoenzymes and ALDH in cervical carcinoma and healthy tissues., overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
ADH1 molecular modeling and molecular dynamics simulations, and comparison to rat ADH5 enzyme, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADH7_HUMAN
386
0
41481
Swiss-Prot
other Location (Reliability: 1)
ADHX_HUMAN
374
0
39724
Swiss-Prot
other Location (Reliability: 2)
ADH6_HUMAN
368
0
39073
Swiss-Prot
other Location (Reliability: 3)
ADH1A_HUMAN
375
0
39859
Swiss-Prot
other Location (Reliability: 3)
ADH1G_HUMAN
375
0
39868
Swiss-Prot
other Location (Reliability: 3)
Q9H1A0_HUMAN
51
0
5831
TrEMBL
other Location (Reliability: 2)
ADH4_HUMAN
380
0
40222
Swiss-Prot
-
ADH1B_HUMAN
375
0
39835
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39500
isozyme ADH3, apparent molecular weight deduced from electrophoretic mobility
39720
isozyme ADH3, calculated from amino acid sequence
39870
isozyme ADH1C, calculated from amino acid sequence
40000
40220
isozyme ADH2, calculated from amino acid sequence
40500
41000
-
2 * 41000, class III isoenzyme chi ADH, SDS-PAGE
42000
78000
-
ultracentrifugation under non-denaturing conditions
78000 - 85000
-
amino acid analysis, ultracentrifugation
79000 - 84000
-
ultracentrifugal analysis
82700
-
equilibrium sedimentation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
-
structure modelling
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme alphaalpha in complex with inhibitor N-cyclopentyl-N-cyclobutylformamide, isozyme beta(1)beta(1) in complex with inhibitors N-benzylformamide and N-heptylformamide, and isozyme gamma(2)gamma(2) in complex with inhibitor N-1-methylheptylformamide, X-ray diffraction structure determination and analysis at 1.45-2.5 A resolution, structure modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A93F
-
isozyme alphaalpha, altered active site structure and inhibitor binding
S48T
-
isozyme gamma(2)gamma(2), altered active site structure and inhibitor binding
V141L
-
isozyme gamma(2)gamma(2), altered active site structure and inhibitor binding
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10.6
-
stable
285567
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
unstable at room temperature and above
additional information
-
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
100fold purified enzyme is destroyed by freezing
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DMSO
DMSO is not an ideal substrate-delivering solvent for ADH-catalysed reactions
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM HEPES buffer, 1 mM dithioerythritol, pH 7.5, stable for 2 weeks
-
4°C, 5 mM Na phosphate, pH 7.5, the half-life is 24 h. 0.01 mM ethanol effectively stabilizes for several weeks
-
4°C, 5 mM Na-phosphate, pH 7.5, 50% loss of activity after 1 day. Enzyme can be stabilized for up to 2 weeks by storage in buffer containing 10 mM ethanol
-
4°C, pH 7.5, stable for 2-3 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anodic enzyme form
-
class I isoenzymes
-
class II isoenzyme: pi-ADH
-
class III isoenzyme chi-ADH
-
isoenzyme beta3,beta3
-
recombinant ADH2 alloenzymes from Escherichia coli by DEAE and AMP or blue Sepharose chromatography, and ultrafiltration
-
recombinant enzyme from Escherichia coli by DEAE ion exchange, 5'-AMP-resin affinity, and Mono Q ion exchange chromatography
-
recombinant isozymes from Escherichia coli strain BL21
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
5-7 genes encoding ADH, DNA and amino acid sequence determination and analysis, polymorphism and allelic frequencies analysis, gene ADH2 possesses 2 allelic forms with Ile308 or Val308, expression of ADH2 alloenzymes in Escherichia coli
-
class IV enzyme, expression in Escherichia coli
-
expression of ADH1C*2 in Escherichia coli
-
expression of ADH4 in Escherichia coli
-
expression of human ADH1 in an in vitro transcription/translation system, N-terminally GST-tagged ADH1 in COS cells and in Escherichia coli
-
expression of isozymes in Escherichia coli strain BL21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
organ simulations indicate that higher therapeutic acetaminophen (0.5 mM) inhibits 16% of allotype ADH1B*1/*1 hepatic ADH activity at 2-20 mM ethanol and that therapeutic salicylate (1.5 mM) inhibits 30-31% of the allotype ADH1B*2/*2 activity, suggesting potential significant inhibitions of ethanol first-pass metabolism in these allelotypes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Herrera, E.; Zorzano, A.; Fresneda, V.
Comparative kinetics of human and rat liver alcohol dehydrogenase
Biochem. Soc. Trans.
11
729-730
1983
Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Dafeldecker, W.P.; Vallee, B.L.
Organ-specific human alcohol dehydrogenase: isolation and characterization of isozymes from testis
Biochem. Biophys. Res. Commun.
134
1056-1063
1986
Homo sapiens
Manually annotated by BRENDA team
Woronick, C.L.
Alcohol dehydrogenase from human liver
Methods Enzymol.
41B
369-374
1975
Homo sapiens
Manually annotated by BRENDA team
Wagner, F.W.; Burger, A.R.; Vallee, B.L.
Kinetic properties of human liver alcohol dehydrogenase: oxidation of alcohols by class I isoenzymes
Biochemistry
22
1857-1863
1983
Homo sapiens
Manually annotated by BRENDA team
Ditlow, C.C.; Holmquist, B.; Morelock, M.M.; Vallee, B.L.
Physical and enzymatic properties of a class II alcohol dehydrogenase isozyme of human liver: pi-ADH
Biochemistry
23
6363-6368
1984
Homo sapiens
Manually annotated by BRENDA team
Yin, S.J.; Bosron, W.F.; Magnes, L.J.; Li, T.K.
Human liver alcohol dehydrogenase: purification and kinetic characterization of the beta 2 beta 2, beta 2 beta 1, alpha beta 2, and beta 2 gamma 1 Oriental isoenzymes
Biochemistry
23
5847-5853
1984
Homo sapiens
Manually annotated by BRENDA team
Wagner, F.W.; Pares, X.; Holmquist, B.; Vallee, B.L.
Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: chi-ADH
Biochemistry
23
2193-2199
1984
Homo sapiens
Manually annotated by BRENDA team
Bosron, W.F.; Magnes, L.J.; Li, T.K.
Kinetic and electrophoretic properties of native and recombined isoenzymes of human liver alcohol dehydrogenase
Biochemistry
22
1852-1857
1983
Homo sapiens
Manually annotated by BRENDA team
Bosron, W.F.; Li, T.K.
Isolation and characterization of an anodic form of human liver alcohol dehydrogenase
Biochem. Biophys. Res. Commun.
74
85-91
1977
Homo sapiens
Manually annotated by BRENDA team
Schneider-Bernloehr, H.; Formicka-Kozlowska, G.; Buehler, R.; Wartburg, J.P.; Zeppezauer, M.
Active-site-specific zinc-depleted and reconstituted cobalt(II) human-liver alcohol dehydrogenase. Preparation, characterization and complexation with NADH and trans-4-(N,N-dimethylamino)-cinnamaldehyde
Eur. J. Biochem.
173
275-280
1988
Homo sapiens
Manually annotated by BRENDA team
Burnell, J.C.; Li, T.K.; Bosron, W.F.
Purification and steady-state kinetic characterization of human liver beta 3 beta 3 alcohol dehydrogenase
Biochemistry
28
6810-6815
1989
Homo sapiens
Manually annotated by BRENDA team
Pares, X.; Vallee, B.L.
New human liver alcohol dehydrogenase forms with unique kinetic characteristics
Biochem. Biophys. Res. Commun.
98
122-130
1981
Homo sapiens
Manually annotated by BRENDA team
Bosron, W.F.; Li, T.K.; Vallee, B.L.
New molecular forms of human liver alcohol dehydrogenase: isolation and characterization of ADHIndianapolis
Proc. Natl. Acad. Sci. USA
77
5784-5788
1980
Homo sapiens
Manually annotated by BRENDA team
Bosron, W.F.; Li, T.K.; Dafeldecker, W.P.; Vallee, B.L.
Human liver pig-alcohol dehydrogenase: kinetic and molecular properties
Biochemistry
18
1101-1105
1979
Homo sapiens
Manually annotated by BRENDA team
Kedishvili, N.Y.; Bosron, W.F.; Stone, C.L.; Hurley, T.D.; Peggs, C.F.; Thomasson, H.R.; Popov, K.M.; Carr, L.G.; Edenberg, H.J.; Li, T.K.
Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity copared with liver isozymes
J. Biol. Chem.
270
3625-3630
1995
Homo sapiens
Manually annotated by BRENDA team
Yin, S.J.; Wang, M.F.; Liao, C.S.; Chen, C.M.; Wu, C.W.
Identification of a human stomach alcohol dehydrogenase with distinctive kinetic properties
Biochem. Int.
22
829-835
1990
Homo sapiens
Manually annotated by BRENDA team
Martras, S.; Alvarez, R.; Gallego, O.; Dominguez, M.; de Lera, A.R.; Farres, J.; Pares, X.
Kinetics of human alcohol dehydrogenase with ring-oxidized retinoids: effect of Tween 80
Arch. Biochem. Biophys.
430
210-217
2004
Homo sapiens
Manually annotated by BRENDA team
Gibbons, B.J.; Hurley, T.D.
Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors
Biochemistry
43
12555-12562
2004
Homo sapiens
Manually annotated by BRENDA team
Stroemberg, P.; Svensson, S.; Hedberg, J.J.; Nordling, E.; Hoog, J.O.
Identification and characterisation of two allelic forms of human alcohol dehydrogenase 2
Cell. Mol. Life Sci.
59
552-559
2002
Homo sapiens
Manually annotated by BRENDA team
Plapp, B.V.; Berst, K.B.
Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the uncompetitive inhibition of ethanol metabolism
Chem. Biol. Interact.
143-144
183-193
2003
Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Martras, S.; Alvarez, R.; Martinez, S.E.; Torres, D.; Gallego, O.; Duester, G.; Farres, J.; de Lera, A.R.; Pares, X.
The specificity of alcohol dehydrogenase with cis-retinoids. Activity with 11-cis-retinol and localization in retina
Eur. J. Biochem.
271
1660-1670
2004
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chou, C.F.; Lai, C.L.; Chang, Y.C.; Duester, G.; Yin, S.J.
Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase
J. Biol. Chem.
277
25209-25216
2002
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Chrostek, L.; Markiewicz, W.; Szmitkowski, M.
Activity of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in the sera of patients with breast cancer
J. Clin. Lab. Anal.
20
105-108
2006
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Zalewski, B.; Szmitkowski, M.
The activity of class I, II, III, and IV alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in liver cancer
Digest. Dis. Sci.
53
2550-2555
2008
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Zalewski, B.; Szmitkowski, M.
Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the sera of patients with liver cancer
J. Clin. Lab. Anal.
22
204-209
2008
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Chrostek, L.; Szmitkowski, M.
The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer
Pancreas
35
142-146
2007
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Szmitkowski, M.
Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in the cancer diseases
Clin. Chim. Acta
395
1-5
2008
Homo sapiens
Manually annotated by BRENDA team
Jelski, W.; Orywal, K.; Panek, B.; Gacko, M.; Mroczko, B.; Szmitkowski, M.
The activity of class I, II, III and IV of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in the wall of abdominal aortic aneurysms
Exp. Mol. Pathol.
87
59-62
2009
Homo sapiens
Manually annotated by BRENDA team
Kollock, R.; Frank, H.; Seidel, A.; Meinl, W.; Glatt, H.
Oxidation of alcohols and reduction of aldehydes derived from methyl- and dimethylpyrenes by cDNA-expressed human alcohol dehydrogenases
Toxicology
245
65-75
2008
Homo sapiens (P00326), Homo sapiens (P08319), Homo sapiens
Manually annotated by BRENDA team
Ostberg, L.J.; Stroemberg, P.; Hedberg, J.J.; Persson, B.; Hoeoeg, J.O.
Analysis of mammalian alcohol dehydrogenase 5 (ADH5): Characterisation of rat ADH5 with comparisons to the corresponding human variant
Chem. Biol. Interact.
202
97-103
2013
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Orywal, K.; Jelski, W.; Zdrodowski, M.; Szmitkowski, M.
The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in cervical cancer
Clin. Biochem.
44
1231-1234
2011
Homo sapiens
Manually annotated by BRENDA team
Chi, Y.C.; Lee, S.L.; Lai, C.L.; Lee, Y.P.; Lee, S.P.; Chiang, C.P.; Yin, S.J.
Ethanol oxidation and the inhibition by drugs in human liver, stomach and small intestine: Quantitative assessment with numerical organ modeling of alcohol dehydrogenase isozymes
Chem. Biol. Interact.
258
134-141
2016
Homo sapiens
Manually annotated by BRENDA team