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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00330
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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: Saccharomyces cerevisiae
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
-
-
-
-
ADH1
ADH2
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
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + NAD+ = an aldehyde + NADH + H+
mechanism is predominantly ordered with ethanol, but partially random with butanol
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
compulsory-order mechanism with the rate-limiting step being the dissociation of the product enzyme-NAD+ complex
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
detailed determination of the reaction and kinetic mechanisms, active site structure and determination of amino acid residues involved in catalysis, 3 isozymes
-
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
4-nitrotetrazolium violet + NADH + H+
a formazan + NAD+
p-NTF, the tetrazolium contacts with NADH on the enzyme surface without intermediate carriers (the zinc in the active ADH site is not a electron carrier) and accepts electrons. Alcohols are not able to reduce p-NTF
-
-
?
5-hydroxymethylfurfural + NADH + H+
(furan-2,5-diyl)dimethanol + NAD+
mutant enzyme S109P/L116S/Y294C
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
mutant enzyme S109P/L116S/Y294C
-
-
?
furfural + NADH + H+
furfuryl alcohol + NAD+
mutant enzyme S109P/L116S/Y294C
-
-
?
(R,S)-2-methylbutan-1-ol + NAD+
(R,S)-2-methyl-butan-1-one + NADH + H+
-
-
-
-
?
(S)-2-methylbutan-1-ol + NAD+
(S)-2-methyl-butanal + NADH + H+
-
-
-
-
?
2-methylpropan-1-ol + NAD+
2-methyl-propan-1-one + NADH + H+
-
-
-
-
?
3-methylbutan-1-ol + NAD+
3-methyl-butan-1-one + NADH + H+
-
-
-
-
?
3-methylbutanal + NADPH + H+
3-methylbutanol + NADP+
low activity, reaction of EC 1.1.1.2
-
-
ir
5-hydroxymethylfurfural + NADH + H+
(furan-2,5-diyl)dimethanol + NAD+
-
no substrate for wild-type, reaction is catalyzed by mutants Y295C and S110P/Y295C
-
-
?
5-hydroxymethylfurfural + NADH + H+
5-hydroxymethylfurfuryl alcohol + NAD+
low activity
-
-
ir
benzacetaldehyde + NADPH + H+
benzol + NADP+
low activity, reaction of EC 1.1.1.2
-
-
ir
ethyl 3-oxobutyrate + NADH + H+
ethyl (S)-3-hydroxybutyrate + NAD+
-
-
-
-
?
p-methoxybenzyl alcohol + NAD+
p-methoxybenzaldehyde + NADH + H+
-
-
-
-
r
phenylglyoxylic acid + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde retains 48.77% activity of its original activity
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
preferred substrates
-
-
ir
acetaldehyde + NADH + H+
ethanol + NAD+
-
cells with an extra copy of ADH1 display chronological life-span extension. Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1 copy show extended replicative life span and increased Sir2p activity
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
rate-limiting step of the alcoholic fermentation
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
?
furfural + NADH + H+
furfuryl alcohol + NAD+
low activity
-
-
ir
additional information
?
-
a quasi-vibrational process is detected with the use of HEPES buffer in the presence of alcohol: NADH is rapidly oxidized to NAD+ by ubiquinone and NAD+ is then slowly reduced to NADH by the alcohol. The NADH:ubiquinone-and alcohol:NAD+-reductase reactions are partially separated in time caused by considerable differences in the values of binding constants of NADH and NAD+ molecules
-
-
-
additional information
?
-
-
substrate specificity and stereospecificity, substrate binding pocket structure of the 3 isozymes, involving Met294, Trp57, and Trp93
-
-
?
additional information
?
-
-
effects of pressure on deuterium isotope effects of yeast alcohol dehydrogenase using alternative substrates
-
-
?
additional information
?
-
the enzyme acts as aldehyde reductase with catalytic functions for reduction of at least six aldehydes, including two furan aldehydes (furfural and 5-hydroxymethylfurfural), three aliphatic aldehydes (acetaldehyde, glycolaldehyde, and 3-methylbutanal), and an aromatic aldehyde (benzaldehyde) with NADH or NADPH as the cofactor. Particularly, Ymr152wp displays the highest specific activity (190.86 U/mg), and the best catalytic rate constant (Kcat), catalytic efficiency (Kcat/Km), and affinity (Km) when acetaldehyde is used as the substrate with NADH as the cofactor. Although Ymr152wp is grouped into the QOR family, no quinone reductase activity was observed using typical quinones as the substrates. No activity with formaldehyde, propionaldehyde, butyraldehyde, glutaraldehyde, 1,2-naphthoquinone, 9,10-phenanthrenequinone, p-benzoquinone, acetone, and acetylacetone. Substrate specificity, overview
-
-
-
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
ethanol + NAD+
acetaldehyde + NADH
-
rate-limiting step of the alcoholic fermentation
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
cells with an extra copy of ADH1 display chronological life-span extension. Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1 copy show extended replicative life span and increased Sir2p activity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
285558, 285641, 285642, 285643, 285644, 285645, 285646, 285649, 655735, 667307, 669148, 695705, 697267, 697658
NADH
-
-
additional information
-
kinetic study on the binding of monomeric and polymeric derivatives of NAD+
-
additional information
no enzyme activities are detected when NAD+ or NADP+ are used as the cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Ca2+
Co2+
-
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
Cu2+
Zn2+
Ca2+
-
CaCl2 and MgCl2 are able to stabilize the enzyme at millimolar concentrations. Ca2+ stabilizes yeast ADH I by preventing the dissociation of the reduced form of the enzyme and by preventing the unfolding of the oxidized form of the enzyme. Ca2+ is fixed by the Asp236 and Glu101 side chains in yeast ADH I
Cu2+
-
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
Zn2+
-
all isozymes, amino acid residues involved in zinc in binding are Cys46, Cys174, His67, Glu68, Asp49, and Thr48, binding mode
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose
-
enzyme activity decreases to half of its original activity at 4 mg/ml of D-glucose. The thiol groups of alcohol dehydrogenase are involved in binding
Glutaraldehyde
-
71% relative activity in the presence of 10 mM glutaraldehyde
Pectin
-
enzyme activity decreases to half of its original activity at 2 mg/ml of pectin. The thiol groups of alcohol dehydrogenase are involved in binding
SDS
-
in the presence of the surfactant the initial reaction rates are consistently lower than in pure buffer at all the surfactant concentrations considered (0.5-50 mM). This effect is mainly due to an increase in the dissociation constant of beta-NAD+ which reaches its maximum value (7.1 mM) at the critical micelle concentration. Above the critical micelle concentration the effect of the surfactant is mainly due to an increase in the Michaels constants of the alcohol, with values of 41 mM for 15 mM SDS and 50 mM for 50 mM SDS
starch
-
enzyme activity decreases to half of its original activity at 10 mg/ml of starch. The thiol groups of alcohol dehydrogenase are involved in binding
tert-butyl hydroperoxide
-
irreversible, inactivation is associated with -SH group oxidation
additional information
-
use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
presence of ethanol or isopropanol and alkalization of the medium sharply activates the NADH:p-NTF-reductase reaction, activity with ubiquinone is also activated
Isopropanol
presence of ethanol or isopropanol and alkalization of the medium sharply activates the NADH:p-NTF-reductase reaction, activity with ubiquinone is also activated
Glutaraldehyde
-
treating with 0.5% glutaraldehyde solution, the activity of the immobilized enzyme is at maximum
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
benzaldehyde
-
isozyme ADH2, in the presence of 0.25 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
33
benzaldehyde
-
isozyme ADH1, in the presence of 0.25 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
34
benzyl alcohol
-
isozyme ADH1, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
49
benzyl alcohol
-
isozyme ADH2, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
2.9
p-Methoxybenzaldehyde
-
isozyme ADH1, in the presence of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
5.9
p-Methoxybenzaldehyde
-
isozyme ADH2, in the presence of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
6.9
p-methoxybenzyl alcohol
-
isozyme ADH2, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
11
p-methoxybenzyl alcohol
-
isozyme ADH1, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
37.55
phenylglyoxylic acid
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
additional information
additional information
reaction kinetics at different pH values, overview
-
additional information
additional information
-
pH-dependence of Km-value
-
additional information
additional information
-
wild-type and mutant forms of the 3 isozymes, steady-state kinetics, detailed kinetic analysis, at different pH values and temperatures
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.74
pH 7.0, 30°C, substrate 5-hydroxymethylfurfural with NADH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
reduction of glycolaldehyde, furfural, formaldehyde, butyraldehyde, and propionaldehyde
7.5
7.5
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9
high catalytic activity within the range of pH 4.5-6.5, relative activity of Ymr152wp dropped quickly under alkaline conditions of pH 7.0-9.0, 40% of maximal activity at pH 4.5, 15% at pH 9.0
8.2 - 9.5
-
pH 8.2: about 10% of maximal activity, pH 9.5: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
25 - 30
30
35
40
35
-
reduction of glycolaldehyde, furfural, butyraldehyde, and propionaldehyde
40
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 85
-
20°C: about 65% of maximal activity, 85°C: about 90% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
during the biological aging of sherry wines, where Saccharomyces bayanus has to grow on ethanol owing to the absence of glucose, this isoenzyme plays a prominent role by converting the ethanol into acetaldehyde and producing NADH in the process. Overexpression of the gene ADH2 (from Saccharomyces cerevisiae) during alcoholic fermentation has no effect on the proteomic profile or the net production of some metabolites associated with glycolysis and alcoholic fermentation such as ethanol, acetaldehyde, and glycerol. However, it affects indirectly glucose and ammonium uptakes, cell growth, and intracellular redox potential, which lead to an altered metabolome
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the quinone oxidoreductase (QOR) subfamily of the medium-chain dehydrogenase/reductase (MDR) family based on the results of amino acid sequence analysis and phylogenetic analysis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional model of the enzyme structure suggest that Ca2+ can be displaced by replacing Met-168 by an Arg residue
-
trigonal crystal form alcohol dehydrogenase I: evidence for the existence of Zn ions in the crystal, from 20% PEG 4000, 20% 2-propanol, 0.1 M sodium citrate, pH 5.6, and 1 mM NAD+, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTAA200/A201L
-
highly reduced activity compared to the wild-type enzyme
M294L
S110P/Y295C
-
mutant is able to catalyze the NADH-dependent reduction of 5-hydroxymethylfurfural, an inhibitor of yeast fermentation, best activity among the mutants isolated
Y295C
-
mutant is able to catalyze the NADH-dependent reduction of 5-hydroxymethylfurfural, an inhibitor of yeast fermentation
M294L
-
7-10fold increase in reactivity, V/Km, with butanol, pentanol and hexanol
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
at pH 6.0 and 8.0, the activity of free ADH decreases dramatically during the incubation, and 90 min later most of the activity is lost, the immobilized form retains 81% of activity at pH 8.0
695705
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
the specific activity of ADH decreases rapidly above 30°C, ADH is almost completely inactive after a 36 min incubation at 55°C
25
35 - 60
-
58% of the original activity is retained after incubation of the immobilized enzyme at 35°C for 32 h, free enzyme loses 68% activity over a 60 min incubation at 60°C, whereas immobilized ADH retains 44% over a 60 min incubation at 60°C
45
50 - 60
-
thermal unfolding of ADH is not observed below 60°C while the kinetic deactivation is observed even at 50°C
56
60
65
-
60 min, about 80% loss of activity of soluble enzyme, about 55% loss of activity of enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
additional information
-
effect of salts in the high concentration range on the thermal stability
45
-
2 h, free YADH is increasingly deactivated during its incubation with decrease of the enzyme concentration from 3.3 to 0.01 mg/ml because of the dissociation of tetrameric YADH into its subunits
56
-
thermal aggregation occurs at 56°C, the thermal denaturation of ADH is irreversible
60
-
60 min, about 35% loss of activity, soluble enzyme and enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ADH immobilized on derived attapulgite nanofibers via glutaraldehyde covalent binding retains higher activity over wider ranges of pH and temperature than those of the free enzyme. After shaking at 125 rpm at 35°C for 32 h, a rapid loss in activity is observed, and almost complete activity of immobilized enzyme is lost in 52 h. The activity of immobilized ADH decreases to 80% of its initial value after four cycles of operation and afterwards gradually decreases with every reuse, but it retains 42% activity after eight cycles for bioreduction of ethyl 3-oxobutyrate.
-
effects of salts on the rate constants of inactivation by heat of alcohol dehydrogenase YADH at 60.0°C. At high concentrations, some salts have stabilizing effects, while others are destabilizing. The effects of salts in the high concentration range examined can be described as follows: (decreased thermal stability) NaClO4, NaI = (C2H5)4NBr, NH4Br, NaBr = KBr = CsBr = (no addition), (CH3)4NBr, KCl, KF, Na2SO4 (increased thermal stability). The decreasing effect of NaClO4 controlls the thermal stability of the enzyme absolutely and is not compensated by the addition of Na2SO4, which stabilizes the enzyme
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde shows enhanced thermal stability and good durability in the repeated use after recovered by magnetic separations. Within 7 cycles of usage, the remaining activity is about 100%, 89.15%, 79.42%, 69.50%, 62.80%, 56.48%, and 48.26% of the first use
-
even at 50°C the stabilization effect of lipid membranes on the tertiary and quaternary structures of the liposomal YADH allows the enzyme to form its thermostable complex with NAD+ in liposomes
-
sucrose, glucose, and betaine stabilize ADH substantially while D-ribose and sarcosine destabilize the enzyme
-
the recycling stability of YADH in silica-coated alginate gel beads is found to be increased significantly mainly due to the effective inhibition of enzyme leakage by compact silica film
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethylformamide
-
50% v/v, 75% remaining activity at 4°C after 100 min, 15% remaining activity after 100 min at 25°C
dioxane
-
50% v/v, 50% remaining activity at 4°C after 100 min, 10% remaining activity after 100 min at 25°C
dodecane
-
active, from 25°C up to 75°C, 3 h, stabilization of the enzyme at elevated temperature
octane
-
active, from 25°C up to 75°C, 3 h, stabilization of the enzyme at elevated temperature
toluene
-
active, from 25°C up to 75°C, 3 h, stabilization of the enzyme at elevated temperature
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Adh1p is oxidatively modified during ageing and, consequently, its activity becomes reduced
-
688866
among all the cysteine residues, Cys43 is the most susceptible to H2O2 oxidation, and the major oxidation products of this cysteine are Cys-SO2H and Cys-SO3H. The oxidation of Cys43 might be responsible for the inactivation of the enzyme upon H2O2 treatment
-
688657
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose CL-4B column chromatograhy and octyl-Sepharose column chromatography
-
using reactive Green 19 covalently immobilized ontomagnetic poly(2-hydroxyethyl methacrylate) nanostructures. Maximum alcohol dehydrogenase adsorption capacity is 176.09 mg/g polymer. Alcohol dehydrogenase molecules are desorbed by using 1.0 M NaCl with 98.4% recovery, purification is 45.63fold in a single step
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YIM1, cloned from Saccharomyces cerevisiae strain BY4742, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strain INVSc1
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is significantly upregulated under high furfural (2-furaldehyde) or 5-(hydroxymethyl)-2-furaldehyde concentrations
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Zn2+ withdrawal by inactivation with Chelex 100, reactivation of the apoenzyme by addition of CuSO4, 1 h at 25°C, pH 7.6
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
energy production
-
preparation of a bioanode for use in ethanol oxidation. The bioanode is obtained via immobilization of dehydrogenase enzymes (alcohol dehydrogenase or aldehyde dehydrogenase) with polyamidoamine dendrimers onto carbon paper platforms, using the layer-by-layer technique. The prepared bioanode proves to be capable of producing good power density values
synthesis
synthesis
-
the photochemical and enzymatic synthesis of methanol from formaldehyde with alcohol dehydrogenase and NAD+ photoreduction by the visible-light photosensitization of zinc tetraphenylporphyrin tetrasulfonate in the presence of methylviologen, diaphorase, and triethanolamine is developed
synthesis
-
in order to increase production of isobutanol, 2-oxoacid decarboxylase (KDC) and alcohol dehydrogenase (ADH) are expressed in Saccharomyces cerevisiae to enhance the endogenous activity of the Ehrlich pathway. Overexpression Ilv2, which catalyzes the first step in the valine synthetic pathway, and deletion of the PDC1 gene encoding a major pyruvate decarboxylase alters the abundant ethanol flux via pyruvate. Along with modification of culture conditions, the isobutanol titer is elevated 13fold, from 11 mg/l to 143 mg/l, and the yield is 6.6 mg/g glucose
synthesis
-
simplified production scheme for isobutanol based on a cell-free immobilized enzyme system. Immobilized enzymes keto-acid decarboxylase (KdcA) and alcohol dehydrogenase (ADH) plus formate dehydrogenase (FDH) for NADH recycle in solution produce isobutanol titers 8 to 20 times higher than the highest reported titers with Saccharomyces cerevisiae on a mol/mol basis. Conversion rates and low protein leaching are achieved by covalent immobilization on methacrylate resin. The enzyme system without in situ removal of isobutanol achieves a 55% conversion of ketoisovaleric acid to isobutanol at a concentration of 0.135 mol isobutanol produced for each mol ketoisovaleric acid consumed
synthesis
-
yeast alcohol dehydrogenase with its cofactor NAD+ can be stably encapsulated in liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The liposomes are 100 nm in mean diameter, the liposomal ADH and NAD+ concentrations are 2.3 mg/ml and 3.9 mM, respectively. Free ADH is increasingly deactivated during its incubation at 45°C for 2 h with decrease of the enzyme concentration from 3.3 to 0.01 mg/ml because of the dissociation of tetrameric ADH into its subunits. Both liposomal enzyme systems, in presence and absence of NAD+, show stabilities at both 45 and 50°C much higher than those of the free enzyme systems, implying that the liposome membranes stabilize the enzyme tertiary and quaternary structures. The enzyme activity of the liposomes in presence of NAD+ show a stability higher than that in absence of NAD+ with a more remarkable effect of NAD+ at 50°C than at 45°C
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Saccharomyces cerevisiae (P28625), Saccharomyces cerevisiae ATCC 204508 (P28625)
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