1.1.1.1: alcohol dehydrogenase This is an abbreviated version! For detailed information about alcohol dehydrogenase, go to the full flat file .
Reaction
a primary alcohol +
NAD+ =
an aldehyde +
NADH +
H+
Synonyms (R)-specific alcohol dehydrogenase, 40 kDa allergen, Aadh1, acetaldehyde-alcohol dehydrogenase, ADH, ADH 1, ADH class III, ADH I, ADH II, ADH-10, ADH-A, ADH-A2, ADH-B2, ADH-C2, ADH-HT, ADH-I, ADH1, ADH1B, ADH1C, ADH1C*1, ADH1C*2, Adh1p, ADH2, ADH3, ADH4, ADH5, ADH6Hp, ADH8, AdhA, AdhB, AdhC, AdhD, AdhE, ADHES77, ADS1, AFPDH, alcohol dehydrogenase, alcohol dehydrogenase (NAD), alcohol dehydrogenase 1, alcohol dehydrogenase 10, alcohol dehydrogenase 2, alcohol dehydrogenase 3, alcohol dehydrogenase 5, alcohol dehydrogenase class-P, alcohol dehydrogenase D, alcohol dehydrogenase GroES domain protein, alcohol dehydrogenase I, alcohol dehydrogenase II, Alcohol dehydrogenase-B2, alcohol dependent dehydrogenase, alcohol-aldehyde/ketone oxidoreductase, NAD+-dependent, alcohol:NAD+ oxidoreductase, aldehyde dehydrogenase, aldehyde reductase, aldehyde/alcohol dehydrogenase, ALDH, aliphatic alcohol dehydrogenase, alpha-ketoaldehyde dehydrogenase, anti-Prelog reductase, APE2239, APE_2239.1, ARAD1B16786p, bi-functional alcohol/aldehyde dehydrogenase, bifunctional acetaldehyde-alcohol dehydrogenase, bifunctional alcohol/aldehyde dehydrogenase, CHY1186, class I ADH, class I ALDH, class II ADH, class III ADH, class III alcohol dehydrogenase, class IV ADH, Cm-ADH2, Cthe_0423, DADH, dehydrogenase, alcohol, ethanol dehydrogenase, FALDH, FDH, Gastric alcohol dehydrogenase, Glutathione-dependent formaldehyde dehydrogenase, glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase, GSH-FDH, GSH-FDH/ADH, HLAD, hLADH, HpADH3, HtADH, HvADH1, HVO_2428, iron-containing alcohol dehydrogenase, KlADH4, KlDH3, KmADH3, KmADH4, LSADH, medium chain alcohol dehydrogenase, medium-chain NAD+-dependent ADH, medium-chain secondary alcohol dehydrogenase, MGD, More, NAD(H)-dependent alcohol dehydrogenase, NAD+-ADH, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, NAD+-dependent alcohol dehydrogenase, NAD+-dependent SDR, NAD+-linked alcohol dehydrogenase 1, NAD+-linked methylglyoxal dehydrogenase, NAD-dependent alcohol dehydrogenase, NAD-dependent medium-chain ADH, NAD-specific aromatic alcohol dehydrogenase, NADH-alcohol dehydrogenase, NADH-aldehyde dehydrogenase, NADH-dependent alcohol dehydrogenase, NADH-dependent anti-Prelog specific ADH, NADH:p-NTF-reductase, Octanol dehydrogenase, Pcal_1311, PF0991 protein, PF1960, PFADH, primary alcohol dehydrogenase, Retinol dehydrogenase, SaADH, SaADH2, Saci_1232, SADH, SCAD, sec-ADH A, short-chain ADH, short-chain dehydrogenase/reductase, short-chain NAD(H)-dependent dehydrogenase/reductase, slr1192, SSADH, SsADH-10, SSO2536, ST0053, Ta1316 ADH, TaDH, TBADH, Teth39_0206, Teth39_0218, Teth514_0627, TK0845, Tsac_0416, Y-ADH, YADH, YADH-1, yeast alcohol dehydrogenase, YIM1, YLL056C, YMR152W, Ymr152wp
ECTree
Temperature Stability
Temperature Stability on EC 1.1.1.1 - alcohol dehydrogenase
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-20
-
loss of activity after 24 h
23
-
unstable at room temperature and above
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
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
50 - 60
-
thermal unfolding of ADH is not observed below 60°C while the kinetic deactivation is observed even at 50°C
62.6
wild-type, thermal denaturation midpoint
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.
65.3
mutant C257L, thermal denaturation midpoint
68
-
purified recombinant enzyme, most stable at
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
88
30-min half-inactivation temperature
98
the enzyme maintains 24% of the original catalytic activity after incubation for 30 min
25
purified recombinant His-tagged enzyme, 10 min, completely stable up to
25
-
6 h, more than 90% residual activity
25
purified recombinant enzyme 6 h, 70% activity remaining
25
the half-life of the enzyme is 20 h at 25°C in ammonium bicarbonate buffer pH 7.9 with 1 mM NAD+
25
-
purified native enzyme, stable up to
30
-
1 h, 90 mM potassium phosphate buffer, pH 6.5, stable
30
-
1 h in 20 mM Tris-HCl buffer, pH 7.0, stable below
32 - 41
-
purified recombinant enzyme expressed from Saccharomyces cerevisiae, at least 80% of the initial activity is retained after 4 min
32 - 41
-
more than 80% of maximum activity, recombinant enzyme expressed in Saccharomyces cerevisiae
34 - 38
-
purified recombinant enzyme expressed from Hansenula polymorpha, at least 80% of the initial activity is retained after 4 min
34 - 38
-
more than 80% of maximum activity, recombinant enzyme expressed in Hansenula polymorpha
35
-
30 min, no significant loss of activity
35
-
HLAD is a mesophilic enzyme whose activity and stability are significantly impaired at temperatures over 35°C
38.5 - 42.5
-
purified recombinant enzyme expressed from Arxula adeninivorans, at least 80% of the initial activity is retained after 4 min
38.5 - 42.5
-
more than 80% of maximum activity, recombinant enzyme expressed in Arxula adeninivorans
40
60 min, stable up to
40
-
1 h in 20 mM Tris-HCl buffer, pH 7.0, retains 80% of its activity
40
-
purified enzyme, inactivation
45
-
1 h, 90 mM potassium phosphate buffer, pH 6.5, 70% loss of activity
45
-
thermal denaturation starts above 45°C. The conformational lock number is 2 when calculated both experimentally and computationally. The enzyme becomes monomer at 46°C, its activity starts to decrease at this temperature. The activity decreases to only 11% of the native ADH activity with a two-phase manner at 49°C. The subunits are dissociated and several intermediates appear
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
45
-
complete loss of activity within 6 h
50
-
30 min, 50% loss of activity
50
60 min, about 50% loss of activity
50
-
1 h, 90 mM potassium phosphate buffer, pH 6.5, complete loss of activity
50
half-life: 304 min in absence of NAD+
50
-
1 h in 20 mM Tris-HCl buffer, pH 7.0, retains 70% of its activity
50
-
1 h, 15% loss of activity
50
-
24 h, 30% loss of activity
50
-
stable up to, about 20% remaining activity after 3 h
50
24 h, 109% of initial activity
50
-
wild-type enzyme Adh1-1S is more stable than mutant enzyme Adh1-1S1108
55
ADH loses less than 30% of its initial activity after a 36 min incubation at 55°C
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
55
-
ADH is insensitive to thermal stress at 55°C and remains fully active after a 36 min incubation at 55°C
55
-
60 min, 73% loss of activity of enzyme 1, 10% loss of activity of enzyme 2, 21% loss of activity of enzyme 3
56
-
native Zn-ADH enzyme
56
-
thermal aggregation occurs at 56°C, the thermal denaturation of ADH is irreversible
60
-
denaturation above
60
60 min, complete loss of activity
60
half-life: 50 min in absence of NAD+, 143 min in presence of 0.01 mM NAD+
60
14 h, more than 50% of initial activity
60
-
1 h in 20 mM Tris-HCl buffer, pH 7.0, retains 24% of its activity
60
-
1 h, 20% loss of activity
60
-
half-life: 2 min in absence of NAD+
60
-
60 min, about 35% loss of activity, soluble enzyme and enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
60
purified recombinant enzyme 15 min, inactivation
65
half-life: 20 min in absence of NAD+
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
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
65
-
inactivation constant for ADHI: 1.23 per min, inactivation constant for ADH II: 0.13 per min
70
30 min, no loss of activity
70
half-life: 6 min in absence of NAD+
70
-
1 h in 20 mM Tris-HCl buffer, pH 7.0, complete loss of activity
70
-
1 h, 40% loss of activity
70
-
purified recombinant enzyme expressed from Hansenula polymorpha, over 80% of the initial activity is retained after 60 min
70
-
remains quite stable at 70°C in the absence of chelating agents
70
-
above, Co-ADH enzyme
70
pH 9.0, 50 mM Tris-HCl, 24% loss of acrtivity
70
24 h, 76% of initial activity
70
10 min, stable. 120 min, 50% loss of activity
75
-
inactivation
75
-
and above, rapid loss of activity
80
30 min, about 20% loss of activity
80
-
1 h, 50% loss of activity
80
12 h, 80% residual activity
80
-
5 h, more than 60% residual activity
85
-
remaining activity
85
-
pH 8.0, protein concentration 0.5 mg/ml, 3 h, 50% loss of activity
85
-
slight residual 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
85 - 90
half-life of 3 h at 85°C and 1 h at 90°C
90
-
1 h, 95% loss of activity
90
3 h, 90% residual activity. No significant change in the CD spectra up to 90 °C
90
-
at 90°C the specific activity is about three times as high as that measured at 65°C
90
half-inactivation temperature is 30 min
95
activity increases with temperature up to 95°C
95
-
stable and active up to 95°C
additional information
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distinct subunits have different deactivation properties
additional information
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alpha-cyclodextrin causes thermal stabilization and delays the onset of secondary structural unfolding and aggregation by approx. 10°C and the midpoint temperatures by more than 5°C. alpha-Cyclodextrin diminishes the deactivation of the enzyme, decreasing the deactivation constant by more than 50%, and clearly reveals the stabilization of the enzyme not only structurally but also kinetically at higher temperatures
additional information
-
-
additional information
-
-
additional information
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temperature stability profiles of recombinantly expressed enzymes, overview
additional information
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effect of salts in the high concentration range on the thermal stability