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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Arabidopsis thaliana
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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: Arabidopsis thaliana
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
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
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
butan-1-ol + NAD+
butanal + NADH + H+
-
90.7% of the activity with ethanol
-
-
?
isopentan-1-ol + NAD+
isopentanal + NADH + H+
-
34% of the activity with ethanol
-
-
?
pentan-1-ol + NAD+
pentanal + NADH + H+
-
75.6% of the activity with ethanol
-
-
?
propan-1-ol + NAD+
propanal + NADH + H+
-
89.3% of the activity with ethanol
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
LC-MS/MS analysis shows that Cys47 and Cys243 can make a stable disulfide bond with glutathione, suggesting redox sensitivity of these residues. Binding of ADH with its cofactors may limit availability of Cys residues to redox modifications
-
additional information
-
LC-MS/MS analysis shows that Cys47 and Cys243 can make a stable disulfide bond with glutathione, suggesting redox sensitivity of these residues. Binding of ADH with its cofactors may limit availability of Cys residues to redox modifications
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.166
ethanol
recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication
0.251
ethanol
recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
31.5
ethanol
recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication
52.1
ethanol
recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
189.76
ethanol
recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication
207.57
ethanol
recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42.7
purified recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication, aldehyde formation
70.8
purified recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication, aldehyde formation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
Arabidopsis suspension cell cultures show decreased ADH activity upon exposure to H2O2, but not to the thiol oxidizing agent diamide. Purified recombinant ADH shows a significant decrease in the enzyme activity by treatments with H2O2 and diethylamine NONOate (DEA/NO). Treatments leading to the formation of a disulfide bond between ADH and glutathione (protein S-glutathionylation) have no negative effect on the enzyme activity. LC-MS/MS analysis shows that Cys47 and Cys243 can make a stable disulfide bond with glutathione, suggesting redox sensitivity of these residues. Mutation of ADH Cys47 to Ser causes an almost complete loss of the enzyme activity while the Cys243 to Ser mutant have increased specific activity. Incubation of ADH with NAD+ or NADH prevents inhibition of the enzyme by H2O2 or DEA/NO. Binding of ADH with its cofactors may limit availability of Cys residues to redox modifications
physiological function
alcohol dehydrogenase (ADH) catalyzes the reversible conversion of acetaldehyde to ethanol while oxidizing NADH to NAD+. During hypoxia, it ensures the maintenance of the glycolytic flux by recycling NAD+ and controls toxic acetaldehyde produced by the decarboxylation of pyruvate. ADH catalyzes the last step of the ethanol fermentation pathway used by plants to cope with energy deficiency during hypoxic stress
additional information
additional information
six Cys residues are found to be involved in the intrachain disulfide bond formation Cys99, Cys102, Cys105, Cys 113, Cys173, and Cys177. Among the six Cys residues, Cys99, Cys102, Cys105, and Cys 113 are bound to the same structural Zn atom, and Cys 177 is bound to the Zn atom at the catalytic center
additional information
-
six Cys residues are found to be involved in the intrachain disulfide bond formation Cys99, Cys102, Cys105, Cys 113, Cys173, and Cys177. Among the six Cys residues, Cys99, Cys102, Cys105, and Cys 113 are bound to the same structural Zn atom, and Cys 177 is bound to the Zn atom at the catalytic center
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_ARATH
379
0
40699
Swiss-Prot
other Location (Reliability: 3)
ADHL1_ARATH
388
0
42529
Swiss-Prot
other Location (Reliability: 2)
ADHL2_ARATH
386
0
42383
Swiss-Prot
other Location (Reliability: 2)
ADHL3_ARATH
394
0
42908
Swiss-Prot
other Location (Reliability: 4)
ADHL4_ARATH
380
0
41316
Swiss-Prot
other Location (Reliability: 3)
ADHL5_ARATH
389
0
42518
Swiss-Prot
other Location (Reliability: 3)
ADHL6_ARATH
381
0
40724
Swiss-Prot
Chloroplast (Reliability: 3)
ADHL7_ARATH
390
0
42568
Swiss-Prot
Chloroplast (Reliability: 5)
ADH1_ARATH
379
0
41178
Swiss-Prot
other Location (Reliability: 3)
Q0WM36_ARATH
195
0
21109
TrEMBL
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 45000, recombinant His-tagged enzyme, SDS-PAGE, x * 50750, His-tagged enzyme, sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
S-glutathionylation, recombinant ADH activity does not decrease upon incubation with GSSG. In contrast, ADH activity is more stable over time when incubated with GSSG. This increase in the enzyme stability leads to an increase (about 20%) in activity compared to the control. Treatment with GSSG does not significantly promote the release of Zn from recombinant ADH
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C243S
site-directed mutagenesis, the mutant shows increased specific activity, the mutation at Cys243 does not significantly affect ADH kinetic efficiency
C47S
site-directed mutagenesis, the mutation Ser causes an almost complete loss of the enzyme activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by affinity chromatography and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
single gene ADH1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, F.; Hu, T.; An, Y.; Huang, J.; Xu, Y.
Purification and enzymatic characterization of alcohol dehydrogenase from Arabidopsis thaliana
Protein Expr. Purif.
90
74-77
2013
Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 1.1.1.1)
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