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

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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 30C, ADH is almost completely inactive after a 36 min incubation at 55C
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 35C for 32 h, free enzyme loses 68% activity over a 60 min incubation at 60C, whereas immobilized ADH retains 44% over a 60 min incubation at 60C
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 60C while the kinetic deactivation is observed even at 50C
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 88C, respectively, which are 17 and 7C lower than that of the wild-type enzyme. At 65C 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 83C and then decreases rapidly due to thermal inactivation. The reaction rate of the single mutant W95L increases more slowly up to about 80C and then decreases rapidly. At 65C 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 70C, the mutant enzyme seems more thermoresistant than the wild type enzyme up to a temperature of 80C, after which its activity decreases abruptly
73
-
inactivation above
85
-
remaining activity
85 - 90
-
half-life of 3 h at 85C and 1 h at 90C, the catalytic efficiency is considerably higher at temperatures below 90C
85
-
pH 8.0, protein concentration 0.5 mg/ml, 3 h, 50% loss of activity
85 - 90
half-life of 3 h at 85C and 1 h at 90C
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