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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Mus musculus
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1.1.1.1 alcohol dehydrogenaseIUBMB 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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Word Map
- 1.1.1.1
- dehydrogenases
- isozymes
- drosophila
- disulfiram
- catalase
- melanogaster
- nicotinamide
- hepatocytes
- horse
-
retinoic
- methanol
-
ethanol-induced
- stomach
- nadp+
- retinal
- semialdehyde
- pyrazole
- intoxication
- aldh1a1
- cyp2e1
-
alcohol-related
-
alcohol-induced
-
self-renewal
-
drinker
-
abuse
-
nadp+-dependent
- benzaldehyde
-
hydride
-
flush
-
stem-like
-
poison
- acrolein
-
chaperone-like
- diethyldithiocarbamate
- isopropanol
-
ethanol-treated
-
tumor-initiating
-
allozymes
- etoh
-
first-pass
- cyclophosphamide
- butanol
-
aldo-keto
- medicine
- synthesis
- sls
- pharmacology
- s-nitrosoglutathione
- biofuel production
- biotechnology
- pargyline
-
aversion
- ichthyosis
-
17beta-hydroxysteroid
- energy production
-
drank
- degradation
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
adh, alcohol dehydrogenase, aldehyde dehydrogenase, adh1b, short-chain dehydrogenase/reductase, ssadh, adh1c, yeast alcohol dehydrogenase, retinol dehydrogenase, faldh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
40 kDa allergen
-
-
-
-
ADH
ADH-A2
-
-
-
-
ADH-B2
-
-
-
-
ADH-C2
-
-
-
-
ADH-HT
-
-
-
-
ADH3
alcohol dehydrogenase (NAD)
-
-
-
-
Alcohol dehydrogenase-B2
-
-
-
-
aldehyde reductase
-
-
-
-
aliphatic alcohol dehydrogenase
-
-
-
-
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
-
-
-
-
ADH
-
-
-
-
ADH3
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + NAD+ = an aldehyde + NADH + H+
ordered bibi mechanism, structural and functional implications of amino acid residue 47
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
redox reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
alpha-Linolenic acid metabolism, Biosynthesis of secondary metabolites, Chloroalkane and chloroalkene degradation, Drug metabolism - cytochrome P450, Fatty acid degradation, Glycine, serine and threonine metabolism, Glycolysis / Gluconeogenesis, Metabolism of xenobiotics by cytochrome P450, Microbial metabolism in diverse environments, Naphthalene degradation, Pyruvate metabolism, Retinol metabolism, Tyrosine metabolism
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9031-72-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
13-cis-retinol + NAD+
13-cis-retinal + NADH
-
no activity with isozyme ADH1
-
-
?
a primary alcohol + NAD+
an aldehyde + NADH + H+
-
ADH3 is involved in multiple cellular pathways, as diverse as formaldehyde detoxification, retinoid metabolism and NO homeostasis, ADH3 is considered to play only a minor role in hepatic alcohol metabolism because ethanol concentrations rarely exceed 50 mM
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
reduced by isoenzyme A2 and C2, no activity with isoenzyme B2
-
-
?
allyl alcohol + NAD+
acrolein + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
benzaldehyde + NADH
benzyl alcohol + NAD+
-
reduced by isoenzyme A2 and C2, no activity with isoenzyme B2
-
-
r
crotyl alcohol + NAD+
crotonaldehyde + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
cyclohexanol + NAD+
cyclohexanone + NADH
-
oxidized by isoenzyme A2, no activity with isoenzymes B2 and C2
-
-
?
ethylene glycol + NAD+
? + NADH
-
oxidized by isoenzyme A2, no activity with isoenzyme B2 and C2
-
-
?
formaldehyde + NADH + H+
methanol + NAD+
-
reduced by isoenzyme A2, no activity with isoenzyme B2 and C2
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
weak activity with isoenzyme A2, no activity with isoenzyme B2 and C2
-
-
?, r
pentanal + NAD+
pentanone + NADH
-
oxidized by isoenzyme A2 and B2, no activity with isoenzyme C2
-
-
?
benzyl alcohol + NAD+
benzaldehyde + NADH
-
oxidized by isoenzyme A2 and C2 no activity with isoenzyme B2
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
no activity with isoenzyme B2, oxidized by isoenzyme A2 and C2
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
role of the major liver isoenzyme A2 in ethanol metabolism
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
DH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a primary alcohol + NAD+
an aldehyde + NADH + H+
-
ADH3 is involved in multiple cellular pathways, as diverse as formaldehyde detoxification, retinoid metabolism and NO homeostasis, ADH3 is considered to play only a minor role in hepatic alcohol metabolism because ethanol concentrations rarely exceed 50 mM
-
-
?
allyl alcohol + NAD+
acrolein + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
crotyl alcohol + NAD+
crotonaldehyde + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
ethanol + NAD+
acetaldehyde + NADH
-
role of the major liver isoenzyme A2 in ethanol metabolism
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
DH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
-
isoenzyme A2 contains 2.7 mol of zinc per mol of enzyme, isoenzyme b2 contains 1.9 mol of zinc per mol of enzyme, isoenzyme C2 contains 3.2 mol of zinc per mol of enzyme. A and C subunits each contain two atoms of zinc, with at least one being involved catalytically, the b subunit probably contains a single non-catalytic zinc atom
Zn2+
Zn2+
-
2 atoms are included in each 40 kDa subunit, while one of the zinc ions is considered to serve a structural function only, the other zinc ion functions as a Lewis acid and activates the substrate in the active site, which is located in a cleft between the catalytic and the coenzyme binding domain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
inhibition of isoenzyme A2 and C2, no inhibition of isoenzyme B2
4-Methylpyrazole
-
inhibits cell protein carbonylation following exposure to crotyl alcohol
pyrazole
-
inhibition of isoenzyme A2 and C2. Isoenzyme B2 is insensitive to pyrazole inhibition with trans-2-hexen-1-ol as substrate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-nitrosoglutathione
-
ADH3-mediated alcohol oxidation is promoted in the presence of S-nitrosoglutathione
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km for isozymes ADH1, and ADH4 for all retinoid substrates in forward and reverse reaction
-
additional information
additional information
-
effects of tert-butanol, butyramide, valeramide and capronamide on KM-value for ethanol
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat for isozymes ADH1, and ADH4 for all retinoid substrates in forward and reverse reaction
-
additional information
additional information
-
effects of tert-butanol, butyramide, valeramide and capronamide on turnover-number of ethanol
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
cyclohexylformamide
pH 7.5, 25°C, wild-type enzyme, versus benzaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ADH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
additional information
additional information
-
tissue-specific expression patterns of class I, III, and IV Adh
additional information
-
ADH3 is expressed ubiquitously and with relatively little inter-tissue variation in mammals, in contrast to other ADHs
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ADH7_MOUSE
374
0
39904
Swiss-Prot
other Location (Reliability: 4)
ADH1_MOUSE
375
0
39771
Swiss-Prot
other Location (Reliability: 3)
ADHX_MOUSE
374
0
39548
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P47A
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
P47H
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
P47Q
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Edenberg, H.J.; Brown, C.J.; Carr, L.G.; Ho, W.H.; Hu, M.W.
Alcohol dehydrogenase gene expression and cloning of the mouse chi-like ADH
Adv. Exp. Med. Biol.
284
253-262
1991
Mus musculus
Algar, E.M.; Seeley, T.L.; Holmes, R.S.
Purification and molecular properties of mouse alcohol dehydrogenase isozymes
Eur. J. Biochem.
137
139-147
1983
Mus musculus
Stroemberg, P.; Svensson, S.; Berst, K.B.; Plapp, B.V.; Hg, J.O.
Enzymatic mechanism of low-activity mouse alcohol dehydrogenase 2
Biochemistry
43
1323-1328
2004
Mus musculus (Q9QYY9), Mus musculus
Fontaine, F.R.; Dunlop, R.A.; Petersen, D.R.; Burcham, P.C.
Oxidative bioactivation of crotyl alcohol to the toxic endogenous aldehyde crotonaldehyde: association of protein carbonylation with toxicity in mouse hepatocytes
Chem. Res. Toxicol.
15
1051-1058
2002
Equus caballus, Mus musculus
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
Haseba, T.; Duester, G.; Shimizu, A.; Yamamoto, I.; Kameyama, K.; Ohno, Y.
In vivo contribution of class III alcohol dehydrogenase (ADH3) to alcohol metabolism through activation by cytoplasmic solution hydrophobicity
Biochim. Biophys. Acta
1762
276-283
2006
Mus musculus
Westerlund, M.; Galter, D.; Carmine, A.; Olson, L.
Tissue- and species-specific expression patterns of class I, III, and IV Adh and Aldh 1 mRNAs in rodent embryos
Cell Tissue Res.
322
227-236
2005
Mus musculus, Rattus norvegicus
Staab, C.A.; Hellgren, M.; Hoeoeg, J.O.
Medium- and short-chain dehydrogenase/reductase gene and protein families: Dual functions of alcohol dehydrogenase 3: implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities
Cell. Mol. Life Sci.
65
3950-3960
2008
Mus musculus
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