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Literature summary for 1.1.1.1 extracted from

  • Bosron, W.F.; Li, T.K.
    Isolation and characterization of an anodic form of human liver alcohol dehydrogenase (1977), Biochem. Biophys. Res. Commun., 74, 85-91.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
2 * 42000, anodic enzyme form, SDS-PAGE Homo sapiens
78000 85000 amino acid analysis, ultracentrifugation Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ethanol + NAD+ Homo sapiens the anodic enzyme form may contribute significantly to alcohol elimination in man, particularly at high concentrations when the other enzyme species are saturated acetaldehyde + NADH
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
anodic enzyme form
-

Purification (Commentary)

Purification (Comment) Organism
anodic enzyme form Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3
-
-
Homo sapiens

Storage Stability

Storage Stability Organism
4°C, 5 mM Na phosphate, pH 7.5, the half-life is 24 h. 0.01 mM ethanol effectively stabilizes for several weeks Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-pyridylcarbinol + NAD+
-
Homo sapiens pyridine-3-carbaldehyde + NADH
-
?
butanol + NAD+
-
Homo sapiens butyraldehyde + NADH
-
?
ethanol + NAD+
-
Homo sapiens acetaldehyde + NADH
-
?
ethanol + NAD+ the anodic enzyme form may contribute significantly to alcohol elimination in man, particularly at high concentrations when the other enzyme species are saturated Homo sapiens acetaldehyde + NADH
-
?
methanol + NAD+ anodic enzyme form shows no activity Homo sapiens formaldehyde + NADH + H+
-
?
pentanal + NAD+
-
Homo sapiens pentanone + NADH
-
?

Subunits

Subunits Comment Organism
dimer 2 * 42000, anodic enzyme form, SDS-PAGE Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.667
-
Pentanol pH 7.5, anodic enzyme form Homo sapiens
0.683
-
3-Pyridylcarbinol pH 7.5, anodic enzyme form Homo sapiens
0.7
-
ethanol pH 7.5, anodic enzyme form Homo sapiens
0.7
-
butanol pH 7.5, anodic enzyme form Homo sapiens
0.717
-
NAD+ pH 7.5, anodic enzyme form Homo sapiens
10.2
-
ethanol pH 10.0, anodic enzyme form Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
NADH
-
Homo sapiens