Description
Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.
Abbr
ADH, Native (Zymomonas mobilis)
Applications
The enzyme is useful for determination of alcohols or aldehydes.
Enzyme Commission Number
EC 1.1.1.1
Contaminants
(as ZM-ADH activity = 100 %)
Glucose-6-phosphate dehydrogenase: < 0.10 %;
Glucokinase: < 0.02 %;
Pyruvate kinase: < 0.02 %;
NADH oxidase: < 0.01 %;
Lactate dehydrogenase: < 0.01 %.
Molecular Weight
ca. 148,000; Subunit molecular weight : ca. 37,000
Michaelis Constant
(100 mM Glycine-KOH buffer, pH 9.0, at 30 °C)
Ethanol: 110 mM;
Methanol: 350 mM;
NAD+: 0.12 mM;
Acetaldehyde: 1.66 mM;
NADH: 0.03 mM.
Specificity
Ethanol: 100 %;
Methanol: 0.05 %;
n - Propanol: 42.3 %;
n - Butanol: 0.28 %.
Unit Definition
One unit of activity is defined as the amount of ZM-ADH that forms 1 μmol of NADH per minute at 30 °C.
Thermal stability
No detectable decrease in activity up to 40 °C.
Storage
Stable at -20 °C for at least six months.
Synonyms
aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5
Specific Activity
more than 400 U/mg protein
Reaction
Alcohol + NAD+ ←→ Aldehyde + NADH + H+
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