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Literature summary for 1.1.1.1 extracted from

  • Nussrallah, B.A.; Dam, R.; Wagner, F.W.
    Characterization of Coturnix quail liver alcohol dehydrogenase enzymes (1989), Biochemistry, 28, 6245-6251.
    View publication on PubMed
Search for more literature for 1.1.1.1

Inhibitors

Inhibitors Comment Organism Structure
pyrazole pyrazole-sensitive enzyme forms ADH-1, ADH-2, ADH-3 and the pyrazole-insensitive form ADH-An Coturnix coturnix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0051
-
 NADH reduction of octanal Coturnix coturnix
0.011
-
 octan-1-ol enzyme form ADH-3 Coturnix coturnix
0.013
-
 benzyl alcohol enzyme form ADH-2 Coturnix coturnix
0.04
-
 12-hydroxydodecanoate enzyme form ADH-3 Coturnix coturnix
0.043
-
 octanal enzyme form ADH-2 Coturnix coturnix
0.2
-
 pentan-1-ol enzyme form ADH-3 Coturnix coturnix
0.23
-
 NAD+ oxidation of ethanol Coturnix coturnix
2
-
 butan-1-ol enzyme form ADH-3 Coturnix coturnix
5.2
-
 Cyclohexanol enzyme form ADH-3 Coturnix coturnix
8.1
-
 ethanol enzyme form ADH-3 Coturnix coturnix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 2 * 42000, enzyme form ADH-2 and ADH-3, SDS-PAGE Coturnix coturnix
82750
-
 enzyme form ADH-3, equilibrium sedimentation Coturnix coturnix

Organism

Organism UniProt Comment Textmining
Coturnix coturnix
-
 japonica. ADH-1, ADH-2, ADH-3 and ADH-An
-

Purification (Commentary)

Purification (Comment) Organism
ADH-2 and ADH-3 Coturnix coturnix

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Coturnix coturnix
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
12-hydroxydodecanoate + NAD+
-
 Coturnix coturnix 12-oxododecanoic acid + NADH
-
 ?
benzyl alcohol + NAD+
-
 Coturnix coturnix benzaldehyde + NADH
-
 ?
butanol + NAD+
-
 Coturnix coturnix butyraldehyde + NADH
-
 ?
cyclohexanol + NAD+
-
 Coturnix coturnix cyclohexanone + NADH
-
 ?
ethanol + NAD+
-
 Coturnix coturnix acetaldehyde + NADH
-
 ?
ethylene glycol + NAD+ no activity Coturnix coturnix ? + NADH
-
 ?
methanol + NAD+ no activity Coturnix coturnix formaldehyde + NADH + H+
-
 ?
octan-1-ol + NAD+
-
 Coturnix coturnix n-octanal + NADH
-
 ?
octanal + NADH + H+
-
 Coturnix coturnix octanol + NAD+
-
 ?
pentanol + NAD+
-
 Coturnix coturnix n-pentanal + NADH
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 42000, enzyme form ADH-2 and ADH-3, SDS-PAGE Coturnix coturnix

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.75
-
 Cyclohexanol enzyme form ADH-2 Coturnix coturnix
1.45
-
 12-hydroxydodecanoate enzyme form ADH-3 Coturnix coturnix
1.85
-
 octan-1-ol enzyme form ADH-3 Coturnix coturnix
2.52
-
 benzyl alcohol enzyme form ADH-3 Coturnix coturnix
2.92
-
 pentan-1-ol enzyme form ADH-3 Coturnix coturnix
3.55
-
 Cyclohexanol enzyme form ADH-3 Coturnix coturnix
4.67
-
 NAD+ enzyme form ADH-2 Coturnix coturnix
4.92
-
 ethanol enzyme form ADH-2 Coturnix coturnix
6.18
-
 NAD+ enzyme form ADH-3 Coturnix coturnix
6.63
-
 ethanol enzyme form ADH-3 Coturnix coturnix
7.22
-
 butan-1-ol enzyme form ADH-3 Coturnix coturnix
8.88
-
 NADH enzyme form ADH-3 Coturnix coturnix
17
-
 octanal enzyme form ADH-3 Coturnix coturnix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 reduction of octanal Coturnix coturnix
11
-
 ethanol oxidation, enzyme form ADH-2 and ADH-3 Coturnix coturnix

pH Range

pH Minimum pH Maximum Comment Organism
9.5 11.5 pH 9.5: about 40% of maximal activity, pH 11.5: about 85% of maximal activity, ethanol oxidation enzyme form ADH-3 Coturnix coturnix

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Coturnix coturnix
NADH
-
 Coturnix coturnix