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, 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, ADS1, AFPDH, alcohol dehydrogenase, alcohol dehydrogenase (NAD), alcohol dehydrogenase 1, alcohol dehydrogenase 10, alcohol dehydrogenase 2, alcohol dehydrogenase 3, alcohol dehydrogenase 5, 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, APE2239, APE_2239.1, ARAD1B16786p, 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, GSH-FDH, HLAD, HpADH3, HtADH, HvADH1, HVO_2428, iron-containing alcohol dehydrogenase, KlADH4, KlDH3, KmADH3, KmADH4, long-chain alkyl alcohol dehydrogenase, LSADH, medium chain alcohol dehydrogenase, medium-chain NAD+-dependent ADH, medium-chain secondary alcohol dehydrogenase, NAD(H)-dependent alcohol dehydrogenase, NAD+-ADH, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, NAD+-dependent alcohol 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, Octanol dehydrogenase, PF0991 protein, PF1960, primary alcohol dehydrogenase, Retinol dehydrogenase, SaADH, SaADH2, Saci_1232, SADH, SCAD, sec-ADH A, short-chain ADH, short-chain NAD(H)-dependent dehydrogenase/reductase, 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

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.1 alcohol dehydrogenase

Temperature Stability

Temperature Stability on EC 1.1.1.1 - alcohol dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-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
32 - 41
-
more than 80% of maximum activity, recombinant enzyme expressed in Saccharomyces cerevisiae; purified recombinant enzyme expressed from Saccharomyces cerevisiae, 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; purified recombinant enzyme expressed from Hansenula polymorpha, at least 80% of the initial activity is retained after 4 min
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
38.5 - 42.5
-
more than 80% of maximum activity, recombinant enzyme expressed in Arxula adeninivorans; purified recombinant enzyme expressed from Arxula adeninivorans, at least 80% of the initial activity is retained after 4 min
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
69
-
Cu-ADH enzyme
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
73
-
inactivation above
85
-
remaining 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
-
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
85
-
slight residual activity
88
-
30-min half-inactivation temperature
98
-
the enzyme maintains 24% of the original catalytic activity after incubation for 30 min
100
-
half-life 130 min
additional information