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

General Stability

General Stability on EC 1.1.1.1 - alcohol dehydrogenase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
100fold purified enzyme is destroyed by freezing
-
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 35C 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.
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dialysis against 50 mM Tris-HCl buffer, stable after 5 h, 3% loss of activity after 1 day, 82% loss of activity after 6 days
-
dithiothreitol stabilizes activity at all stages of purification
-
does not require the presence of reducing agents to mantain its stability even at high temperature, evidently due to the lack in free cysteines
-
effects of salts on the rate constants of inactivation by heat of alcohol dehydrogenase YADH at 60.0C. 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
-
enzyme form ADH I is more stable during purification than enzyme form ADH-II
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even at 50C 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
-
highly stable against 0.1 M urea and 0.05% SDS
-
isozymes are stabilized by MgCl2 and DTT during purification
-
sucrose, glucose, and betaine stabilize ADH substantially while D-ribose and sarcosine destabilize the enzyme
-
the catalytic zinc ions have an important stabilizing effect on the tertiary and quaternary structure of the immobilized enzyme
-
the presence of a second phase of a water-insoluble solvent like hexane or octane has only minor effects on the enzyme, which retains 80% of its activity, allowing the use of these solvents in aqueous/organic mixtures to increase the availability of low-water soluble substrates
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
-