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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Saccharolobus solfataricus and UniProt Accession P39462
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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: Saccharolobus solfataricus
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
-
-
-
-
alcohol-aldehyde/ketone oxidoreductase, NAD+-dependent
-
the enzyme transfers the pro-R hydrogen from coenzyme to substrate and is therefore an A-specific dehydrogenase
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
redox reaction
-
-
-
-
oxidation
-
-
-
-
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
2-(3,5-dimethylphenyl)propanal + NADH + H+
(S)-2-(3,5-dimethylphenyl)propanol + NAD+
18 h, 99% yield, 90% enantiomeric excess
-
-
?
2-(3-benzoylphenyl)propanal + NADH + H+
(S)-2-(3-benzoylphenyl)propanol + NAD+
18 h, 85% yield, 95% enantiomeric excess
-
-
?
2-(3-fluorobiphenyl-4-yl)propanal + NADH + H+
(S)-2-(3-(fluoro)biphenyl-4-yl)propanol + NAD+
18 h, 77% yield, 97% enantiomeric excess
-
-
?
2-(3-phenoxyphenyl)propanal + NADH + H+
(S)-2-((3-phenoxy)phenyl)propanol + NAD+
18 h, 85% yield, 95% enantiomeric excess
-
-
?
2-(4-isobutylphenyl)propanal + NADH + H+
(S)-2-(4-isobutylphenyl)propanol + NAD+
18 h, 92% yield, 99% enantiomeric excess
-
-
?
2-(4-trifluoromethylphenyl)propanal + NADH + H+
(S)-2-(4-trifluoromethyl)phenylpropanol + NAD+
18 h, 55% yield, 98% enantiomeric excess
-
-
?
2-(6-methoxynaphthalen-2-yl)propanal + NADH + H+
(S)-2-(6-methoxynaphthalen-2-yl)propan-1-ol + NAD+
18 h, 96% yield, 98% enantiomeric excess
-
-
?
2-(naphthalen-1-yl)propanal + NADH + H+
(S)-2-(naphthalen-1-yl)propanol + NAD+
18 h, 90% yield, 80% enantiomeric excess
-
-
?
2-(naphthalen-2-yl)propanal + NADH + H+
(S)-2-(naphthalen-2-yl)propanol + NAD+
18 h, 57% yield, 94% enantiomeric excess
-
-
?
2-ethoxyethanol + NAD+
2-ethoxyacetaldehyde + NADH + H+
-
-
-
r
2-phenylpropanal + NADH + H+
(S)-2-phenylpropanol + NAD+
18 h, 74% yield, 98% enantiomeric excess
-
-
?
2-[3-(2-phenyl-1,3-dioxolan-2-yl)phenyl]propanal + NADH + H+
(S)-2-(3-(2-phenyl-1,3-dioxolan-2-yl)phenyl)propanol + NAD+
18 h, 95% yield, 61% enantiomeric excess
-
-
?
4-methoxybenzyl alcohol + NAD+
4-methoxybenzaldehyde + NADH + H+
-
-
-
r
trans-cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
-
-
r
2-methylcyclohexanol + NAD+
(+)-2-methylcyclohexanone + NADH + H+
-
-
-
-
r
3-bromobenzyl alcohol + NAD+
3-bromobenzaldehyde + NADH + H+
-
-
-
-
?
3-bromobenzylalcohol + NAD+
3-bromobenzaldehyde + NADH + H+
-
-
-
-
?
3-methoxybenzyl alcohol + NAD+
3-methoxybenzaldehyde + NADH + H+
-
-
-
-
?
3-methoxybenzylalcohol + NAD+
3-methoxybenzaldehyde + NADH + H+
-
-
-
-
?
3-methylbutan-2-one + NADH + H+
3-methylbutan-2-ol + NAD+
-
-
-
-
?
3-methylcyclohexanol + NAD+
3-methylcyclohexanone + NADH
-
-
-
-
r
3-methylcyclohexanone + NADH
3-methylcyclohexanol + NAD+
-
-
-
-
r
4-bromobenzyl alcohol + NAD+
4-bromobenzaldehyde + NADH + H+
-
-
-
-
?
4-bromobenzylalcohol + NAD+
4-bromobenzaldehyde + NADH + H+
-
-
-
-
?
4-carboxybenzaldehyde + NADH + H+
4-carboxybenzyl alcohol + NAD+
-
-
-
-
?
4-carboxybenzaldehyde + NADH + H+
4-carboxybenzylalcohol + NAD+
-
-
-
-
?
4-methoxybenzyl alcohol + NAD+
4-methoxybenzaldehyde + NADH + H+
-
-
-
-
r
4-methoxybenzylalcohol + NAD+
4-methoxybenzaldehyde + NADH + H+
-
-
-
-
r
4-nitrobenzaldehyde + NADH + H+
4-nitrobenzyl alcohol + NAD+
-
-
-
-
?
4-nitrobenzaldehyde + NADH + H+
4-nitrobenzylalcohol + NAD+
-
-
-
-
?
anisaldehyde + NADH + H+
anisic alcohol + NAD+
-
-
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
?
additional information
?
-
the enzyme undergoes a substantial conformational change in the apo-holo transition, accompanied by loop movements at the domain interface
-
-
?
additional information
?
-
-
the enzyme undergoes a substantial conformational change in the apo-holo transition, accompanied by loop movements at the domain interface
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
selenium
Zn2+
Zinc
Zn2+
selenium
steady-state fluorescence properties of alcohol dehydrogenase and its selenomethionyl derivative
selenium
the effect of significant decrease in intrinsic fluorescence intensity of the enzyme caused by replacement of S atoms of methionine residues to Se is explained on the basis of the analysis of its 3D structure. All selenium atoms are located far from both Trp95 and Trp117 and can not cause their fluorescence quenching. Substitution of S by Se causes enhanced protein absorption in the UV-region. This effect is explained by the formation of Se complex with some groups of protein
Zn2+
the catalytic active site zinc ion is bound to Glu69 in the apoenzyme state, but not in the ternary complex state
Zn2+
ADH is a putative zinc-dependent alcohol dehydrogenase
Zn2+
-
contains a zinc ion which is directly involved in the structural stabilization of enzyme molecule
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
o-phenanthroline
-
loses 30% of its activity immediately on addition of o-phenanthroline
sodium iodoacetate
-
increasing concentrations od sodium iodoacetate produce a slight decrease in activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
2-ethoxyethanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.27
3-Pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.14
3-bromobenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.12
4-bromobenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.3
4-methoxybenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
2.4
iso-propanol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
0.19
n-Propanol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
0.41
(R)-2-butanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
37.4
(R)-2-butanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.22
(R)-2-pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
11.7
(R)-2-pentanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.012
(S)-2-butanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
29.8
(S)-2-butanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.07
(S)-2-pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
8.8
(S)-2-pentanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.08
1-butanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.6
1-butanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.038
1-Heptanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.21
1-Heptanol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.67
1-Heptanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.035
1-Hexanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.04
1-Hexanol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.88
1-Hexanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.027
1-Pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.26
1-Pentanol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.9
1-Pentanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.24
1-propanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
6.5
1-propanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.07
4-methoxybenzyl alcohol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.12
4-methoxybenzyl alcohol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.3
4-methoxybenzyl alcohol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.03
benzaldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.07
benzaldehyde
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.28
benzaldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.12
benzyl alcohol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.26
benzyl alcohol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.8
benzyl alcohol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.07
Butyraldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.13
Butyraldehyde
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.27
Butyraldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.03
Cyclohexanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.5
Cyclohexanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.6
ethanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
66
ethanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.26
Isobutyraldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.33
Isobutyraldehyde
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.76
Isobutyraldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.5
NAD+
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4
NAD+
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
50
NAD+
Km above 50 mM, mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.008
NADH
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.01
NADH
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.75
NADH
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.009
trans-cinnamaldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.09
trans-cinnamaldehyde
mutant enzyme W95L,, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.23
trans-cinnamaldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.33
1-propanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.6
2-propanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.2
3-methoxybenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.2
3-methoxybenzylalcohol
-
in the presence of 5 mM benzylalcohol, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.28
4-carboxybenzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.14
4-methoxybenzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.3
benzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.44
benzylalcohol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
0.8
benzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.045
Cyclohexanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.7
ethanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.33
ethanol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
0.5
NAD+
-
wild type enzyme, at 65°C, in the presence of benzyl alcohol
12.4
NAD+
-
mutant enzyme N249Y, at 65°C, in the presence of benzyl alcohol
0.013
NADH
-
wild type enzyme, at 65°C, in the presence of benzaldehyde
0.03
NADH
-
in 50 mM Tris-HCl (pH 7.5) containing 0.25 mM benzaldehyde, at 65°C
0.21
NADH
-
mutant enzyme N249Y, at 65°C, in the presence of benzaldehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
2-ethoxyethanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.5
3-Pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.2
3-bromobenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.1
4-bromobenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.5
4-methoxybenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.4
benzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1
(R)-2-butanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.7
(R)-2-butanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.1
(R)-2-pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.9
(R)-2-pentanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.2
(S)-2-butanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.8
(S)-2-butanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.6
(S)-2-pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
6.7
(S)-2-pentanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.1
1-butanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
15.1
1-butanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.51
1-Heptanol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.6
1-Heptanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
11.9
1-Heptanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.42
1-Hexanol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2
1-Hexanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
13.3
1-Hexanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.53
1-Pentanol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.5
1-Pentanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
16.3
1-Pentanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.5
1-propanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
15.7
1-propanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.37
4-methoxybenzyl alcohol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.9
4-methoxybenzyl alcohol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
16.8
4-methoxybenzyl alcohol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.36
benzaldehyde
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
11.3
benzaldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
13.1
benzaldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.35
benzyl alcohol
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.6
benzyl alcohol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
20
benzyl alcohol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.36
Butyraldehyde
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
19.7
Butyraldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
19.7
Butyraldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.2
Cyclohexanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
12.4
Cyclohexanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.1
ethanol
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.1
ethanol
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.82
Isobutyraldehyde
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
18.1
Isobutyraldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
29
Isobutyraldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.52
NAD+
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.4
NAD+
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
21
NAD+
Km above 50 mM, mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.38
NADH
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
10.3
NADH
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
34.8
NADH
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.21
trans-cinnamaldehyde
mutant enzyme W95L,, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.1
trans-cinnamaldehyde
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
18.9
trans-cinnamaldehyde
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.2
1-propanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.25
2-propanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.2
3-methoxybenzylalcohol
-
in the presence of 5 mM benzylalcohol, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.4
3-methoxybenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.7
4-carboxybenzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.6
4-methoxybenzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
4.6
4-nitrobenzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
3.5
benzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.65
Cyclohexanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.5
ethanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
3.4
NAD+
-
wild type enzyme, at 65°C, in the presence of benzyl alcohol
50
NAD+
-
mutant enzyme N249Y, at 65°C, in the presence of benzyl alcohol
4.5
NADH
-
in 50 mM Tris-HCl (pH 7.5) containing 0.25 mM benzaldehyde, at 65°C
10.3
NADH
-
wild type enzyme, at 65°C, in the presence of benzaldehyde
25.3
NADH
-
mutant enzyme N249Y, at 65°C, in the presence of benzaldehyde
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.5
purified mutant enzyme W95L, using benzyl alcohol as substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
18.6
purified mutant enzyme W95L/N249Y, using benzyl alcohol as substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.2
purified wild type enzyme, using benzyl alcohol as substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.02
-
mutant recombinant enzyme E97C, from crude extract, at 65°C
0.03
crude extract, using benzylalcohol as substrate, at 65°C
0.18
after 5.67fold purification, using benzylalcohol as substrate, at 65°C
0.75
purified enzyme, using benzylalcohol as substrate, at 80°C
4.03
-
recombinant wild type enzyme, after 6fold purification, at 65°C
4.5
-
wild type recombinant enzyme, after 450fold purification, at 65°C
5.2
-
mutant recombinant enzyme E97C, after 260fold purification, at 65°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
for the oxidation reaction, ADH activity shows a slight dependence on pH, displaying a broad peak with a maximum around 9.5
8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highest ethanol consumption rate in cultures grown on 0.79% w/v ethanol
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
homotetramer
tetramer
tetramer
-
crosslinking of ADH with dimethylsuberimidate and ethylene glycol bis [succinimidylsuccinate] produces mainly dimers and tetramers, suggesting a dimer of dimers assembly
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
carboxymethylation with sodium iodoacetate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and ternary complex of enzyme with NADH and 2-ethoxyethanol bound to each subunit, X-ray diffraction structure determination and analysis at 2.3 A resolution
crystals are grown in the Advanced Protein Crystallization Facility during the Life and Microgravity Sciences Spacelab mission on the US Space Shuttle. Large diffracting crystals are obtained by dialysis, whereas only poor-quality crystals are obtained by vapour diffusion. The quality of both the microgravity and ground-based crystals is analysed by X-ray diffraction. There is some improvement in terms of size and diffraction resolution limit for the microgravity crystals. The twinning observed in the Earthgrown crystals is also present for those grown in microgravity
microbatch method in 100 mM Tris-HCl (pH 7.8), 10 mM dithiotreitol with the same volume of 12% (w/v) PEG 4000, 12% (v/v) 2-propanol, 100 mM sodium citrate (pH 5.6) at 20°C
twinned crystals are grown with the sitting drop vapour diffusion method using 2-methyl-2,4-pentanediol (50% v/v), Tris/HCl buffer (150 mM, pH 8.4), and NADH (1 mM), prismatic crystals are grown at 4°C and 20°C by microbatch and free interface diffusion methods with Tris/HCl buffer (130 mM, pH 8.0), NADH (2 mM), polyethyleneglycol 4000 (16% w/v), propan-2-ol or propan-1-ol (16% v/v) in trisodium citrate (100 mM, pH 4.8-5.6)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N249Y
mutant exhibits increased catalytic activity compared to the wild type enzyme
W95L
the mutant displays no apparent activity with short-chain primary and secondary alcohols and poor activity with aromatic substrates and coenzyme, the substitution affects the structural stability of the archaeal ADH, decreasing its thermal stability without relevant changes in secondary structure, optimum pH is at about pH 10
W95L/N249Y
the mutant exhibits higher activity but decreased affinity toward aliphatic alcohols, aldehydes as well as NAD+ and NADH compared to the wild type enzyme, optimum pH is at about pH 8.6
E97C
-
shows the same activity but a reduced thermostability with respect to the wild type recombinant protein
N249Y
N249Y
-
mutant shows increased thermal stability and increased catalytic activity compared to the wild type enzyme
N249Y
-
shows 7fold higher specific activity compared to the wild type enzyme, is active up to 95°C and more stable than the native enzyme, has acquired an improved resistance to proteolysis by thermolysin and shows a decreased activating effect by treatment with denaturants at moderate concentration
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 88
the single and double mutant are less thermoresistant than the wild type enzyme, displaying a transition temperature of 78 and 88°C, respectively, which are 17 and 7°C lower than that of the wild-type enzyme. At 65°C the single mutant W95L is 10fold less active and the double mutant W95L/N249Y is about 6fold more active than wild type enzyme, the reaction rate catalyzed by the double mutant W95L/N249Y increases more markedly than that of the wild type enzyme up to a temperature of about 83°C and then decreases rapidly due to thermal inactivation. The reaction rate of the single mutant W95L increases more slowly up to about 80°C and then decreases rapidly. At 65°C the single mutant is 10fold less active and the double mutant is about 6fold more active than wild type enzyme.
55
-
the native enzyme remains completely stable after heating for 3 h at 55°C while the carboxymethylated enzyme loses 10% of activity under the same conditions
65
70
70 - 80
-
wild type and mutant enzyme N249Y are stable at 70°C, the mutant enzyme seems more thermoresistant than the wild type enzyme up to a temperature of 80°C, after which its activity decreases abruptly
85
-
pH 8.0, protein concentration 0.5 mg/ml, 3 h, 50% loss of activity
85 - 90
-
half-life of 3 h at 85°C and 1 h at 90°C, the catalytic efficiency is considerably higher at temperatures below 90°C
90
-
at 90°C the specific activity is about three times as high as that measured at 65°C
95
65
-
pH 8.0, protein concentration 2.5 mg/ml, 16 h, stable. 50% loss of activity after 8 h at protein concentration of 0.5 mg/ml
65
-
at 65°C the half-lives of the native and carboxymethylated enzymes are 9 h and 4 h, respectively
65
-
the activity of the recombinant wild type enzyme slowly decreases to 50% after 16 h at 65°C
70
-
remains quite stable at 70°C in the absence of chelating agents
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
does not require the presence of reducing agents to mantain its stability even at high temperature, evidently due to the lack in free cysteines
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 M NaCl in 20 mM Tris-HCl (pH 8.4) in the presence of an equal volume of glycerol, 12 months, no loss of activity
-
4°C, 1 M NaCl in 20 mM Tris-HCl (pH 8.4) in the absence of glycerol, 4 months, 60% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose Fast Flow column chromatography and G75 gel filtration
-
DEAE-Sepharose Fast Flow column chromatography, Matrex Gel Red A column chromatography, and Blue A column chromatography
-
HiTrap heparin-Sepharose column chromatography, DEAE-Sepharose fast-flow column chromatography, and HiLoad Superdex S-75 gel filtration
-
Toyopearl Butyl 650 S column chromatography, Q Sepharose fast flow column chromatography, Superose 12 prep-grade gel filtration, and TosoHaas G 2000 SWXL gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli RB791 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pearl, L.H.; Demasi, D.; Hemmings, A.M.; Sica, F.; Mazzarella, L.; Raia, C.A.; D'Auria, S.; Rossi, M.
Crystallization and preliminary X-ray analysis of an NAD(+)-dependent alcohol dehydrogenase fromthe extreme thermophilic archaebacterium Sulfolobus solfataricus
J. Mol. Biol.
229
782-784
1993
Saccharolobus solfataricus
Rella, R.; Raia, C.A.; Pensa, M.; Pisani, F.M.; Gambacorta, A.; de Rosa, M.; Rossi, M.
A novel archaebacterial NAD+-dependent alcohol dehydrogenase. Purification and properties
Eur. J. Biochem.
167
475-479
1987
Saccharolobus solfataricus
Ammendola, S.; Raia, C.A.; Caruso, C.; Camardella, L.; D'Auria, S.; De Rosa, M.; Rossi, M.
Thermostable NAD(+)-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases
Biochemistry
31
12514-12523
1992
Saccharolobus solfataricus
Esposito, L.; Bruno, I.; Sica, F.; Raia, C.A.; Giordano, A.; Rossi, M.; Mazzarella, L.; Zagari, A.
Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus
Biochemistry
42
14397-14407
2003
Saccharolobus solfataricus (P39462), Saccharolobus solfataricus
Sica, F.; Demasi, D.; Mazzarella, D.L.; Zagari, A.; Capasso, S.; Pearl, L.H.; D'Auria, S.; Raia, C.A.; Rossi, M.
Elimination of twinning in crystals of Sulfolobus sofataricus alcohol dehydrogenase holo-enzyme by growth in agarose gels
Acta Crystallogr. Sect. D
50
508-511
1994
Saccharolobus solfataricus
Raia, C.A.; Caruso, C.; Marino, M.; Vespa, N.; Rossi, M.
Activation of Sulfolobus solfataricus alcohol dehydrogenase by modification of cysteine residue 38 with iodoacetic acid
Biochemistry
35
638-647
1996
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617
Giordano, A.; Cannio, R.; La Cara, F.; Bartolucci, S.; Rossi, M.; Raia, C.A.
Asn249Tyr substitution at the coenzyme binding domain activates Sulfolobus solfataricus alcohol dehydrogenase and increases its thermal stability.
Biochemistry
38
3043-3054
1999
Saccharolobus solfataricus
Trincone, A.; Lama, L.; Rella, R.; D'Auria, S.; Raia, C.A.; Nicolaus, B.
Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus
Biochim. Biophys. Acta
1041
94-96
1990
Saccharolobus solfataricus
Esposito, L.; Bruno, I.; Sica, F.; Raia, C.A.; Giordano, A.; Rossi, M.; Mazzarella, L.; Zagari, A.
Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity.
FEBS Lett.
539
14-18
2003
Saccharolobus solfataricus (P39462), Saccharolobus solfataricus
Cannio, R.; Fiorentino, G.; Rossi, M.; Bartolucci, S.
The alcohol dehydrogenase gene: distribution among Sulfolobales and regulation in Sulfolobus solfataricus
FEMS Microbiol. Lett.
170
31-39
1999
Saccharolobus solfataricus, Saccharolobus solfataricus Gtheta
Cannio, R.; Fiorentino, G.; Carpinelli, P.; Rossi, M.; Bartolucci, S.
Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species
J. Bacteriol.
178
301-305
1996
Saccharolobus solfataricus, Sulfolobus sp. (P50381), Sulfolobus sp., Sulfolobus sp. RC3 (P50381)
Fiorentino, G.; Cannio, R.; Rossi, M.; Bartolucci, S.
Transcriptional regulation of the gene encoding an alcohol dehydrogenase in the archaeon Sulfolobus solfataricus involves multiple factors and control elements
J. Bacteriol.
185
3926-3934
2003
Saccharolobus solfataricus
Esposito, L.; Sica, F.; Raia, C.A.; Giordano, A.; Rossi, M.; Mazzarella, L.; Zagari, A.
Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 A resolution
J. Mol. Biol.
318
463-477
2002
Saccharolobus solfataricus (P39462), Saccharolobus solfataricus
Chong, P.K.; Burja, A.M.; Radianingtyas, H.; Fazeli, A.; Wright, P.C.
Proteome and transcriptional analysis of ethanol-grown Sulfolobus solfataricus P2 reveals ADH2, a potential alcohol dehydrogenase
J. Proteome Res.
6
3985-3994
2007
Saccharolobus solfataricus (Q9UXF1), Saccharolobus solfataricus P2 (Q9UXF1), Saccharolobus solfataricus P2
Raia, C.A.; Giordano, A.; Rossi, M.
Alcohol dehydrogenase from Sulfolobus solfataricus
Methods Enzymol.
331
176-195
2001
Saccharolobus solfataricus
Casadio, R.; Martelli, P.L.; Giordano, A.; Rossi, M.; Raia, C.A.
A low-resolution 3D model of the tetrameric alcohol dehydrogenase from Sulfolobus solfataricus
Protein Eng.
15
215-223
2002
Saccharolobus solfataricus
Ammendola, S.; Raucci, G.; Incani, O.; Mele, A.; Tramontano, A.; Wallace, A.
Replacing the glutamate ligand in the structural zinc site of Sulfolobus solfataricus alcohol dehydrogenase with a cysteine decreases thermostability.
Protein Eng.
8
31-37
1995
Saccharolobus solfataricus
Pennacchio, A.; Esposito, L.; Zagari, A.; Rossi, M.; Raia, C.A.
Role of Tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase
Extremophiles
13
751-761
2009
Saccharolobus solfataricus (P39462), Saccharolobus solfataricus
Esposito, L.; Sica, F.; Sorrentino, G.; Berisio, R.; Carotenuto, L.; Giordano, A.; Raia, C.A.; Rossi, M.; Lamzin, V.S.; Wilson, K.S.; Zagari, A.
Protein crystal growth in the advanced protein crystallization facility on the LMS mission: a comparison of Sulfolobus solfataricus alcohol dehydrogenase crystals grown on the ground and in microgravity
Acta Crystallogr. Sect. D
54
386-390
1998
Saccharolobus solfataricus (P39462), Saccharolobus solfataricus
Giordano, A.; Raia, C.A.
Steady-state fluorescence properties of S. solfataricus alcohol dehydrogenase and its selenomethionyl derivative
J. Fluoresc.
13
17-24
2003
Saccharolobus solfataricus (P39462)
-
Giordano, A.; Russo, C.; Raia, C.A.; Kuznetsova, I.M.; Stepanenko, O.V.; Turoverov, K.K.
Highly UV-absorbing complex in selenomethionine-substituted alcohol dehydrogenase from Sulfolobus solfataricus
J. Proteome Res.
3
613-620
2004
Saccharolobus solfataricus (P39462), Saccharolobus solfataricus
Friest, J.A.; Maezato, Y.; Broussy, S.; Blum, P.; Berkowitz, D.B.
Use of a robust dehydrogenase from an archael hyperthermophile in asymmetric catalysis-dynamic reductive kinetic resolution entry into (S)-profens
J. Am. Chem. Soc.
132
5930-5931
2010
Saccharolobus solfataricus (P39462), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P39462)
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