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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Drosophila melanogaster
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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: Drosophila melanogaster
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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + NAD+ = an aldehyde + NADH + H+
ordered bi-bi mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
rapid equilibrium random mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
-
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
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of ethanol oxidation
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of ethanol oxidation
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). ADHX_DROME
379
0
40389
Swiss-Prot
other Location (Reliability: 2)
ADH_DROME
256
0
27761
Swiss-Prot
other Location (Reliability: 4)
Q29QY4_DROME
209
0
23312
TrEMBL
other Location (Reliability: 4)
Q1ECB3_DROME
179
0
19481
TrEMBL
other Location (Reliability: 4)
X2J986_DROME
256
0
29014
TrEMBL
other Location (Reliability: 3)
Q9I7R3_DROME
267
0
29281
TrEMBL
other Location (Reliability: 1)
A0A077HCQ5_DROME
238
0
25682
TrEMBL
other Location (Reliability: 4)
A0A077HCY9_DROME
238
0
25709
TrEMBL
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vilageliu, L.; Juan, E.; Gonzalez-Duarte, R.
Determination of some biochemical features of alcohol dehydrogenase from Drosophila melanogaster, Drosophila simulans, Drosophila virilis, Drosophila funebris, Drosophila imigrans and drosophila lebanonensis. Comparison of their properties and estimation of the homology of the ADH enzyme of different species
Adv. Genet. , Dev. , Evol. Drosophila, [Proc. Eur. Drosophila Res. Conf. ] (Lakovaara, S. , ed. ) Plenum N. Y.
7
237-250
1982
Drosophila funebris, Drosophila immigrans, Scaptodrosophila lebanonensis, Drosophila melanogaster, Drosophila simulans, Drosophila virilis
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Winberg, J.O.; McKinley-McKee, J.S.
Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies
Biochem. J.
301
901-909
1994
Drosophila melanogaster
Retzios, A.; Thatcher, D.R.
Characterization of the Adhf and Adhus alleloenzymes of Drosophila melanogaster (fruitfly) alcohol dehydrogenase
Biochem. Soc. Trans.
9
298-299
1981
Drosophila melanogaster
-
Winberg, J.O.; McKinley-McKee, J.S.
Drosophila melanogaster alcohol dehydrogenase. Biochemical properties of the NAD+-plus-acetone-induced isoenzyme conversion
Biochem. J.
251
223-227
1988
Drosophila melanogaster
Heinstra, P.W.H.; Thoerig, G.E.W.; Scharloo, W.; Drenth, W.; Nolte, R.J.M.
Kinetics and thermodynamics of ethanol oxidation catalyzed by genetic variants of the alcohol dehydrogenase from Drosophila melanogaster and D. simulans
Biochim. Biophys. Acta
967
224-233
1988
Drosophila melanogaster, Drosophila simulans
Juan, E.; Gonzalez-Duarte, R.
Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Comparison of their properties with the Drosophila melanogaster Adhs enzyme
Biochem. J.
195
61-69
1981
Drosophila melanogaster, Drosophila simulans, Drosophila virilis
Lee, C.Y.
Alcohol dehydrogenase from Drosophila melanogaster
Methods Enzymol.
89
445-450
1982
Drosophila melanogaster
-
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