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Creative Enzymes is renowned for its particular service of measuring the activity of alcohol dehydrogenases using spectrophotometric assays. Our activity test results are highly accurate and reproducible, thanks to many years of service experiences in this field. With our core technology, we are leading the activity assays of alcohol dehydrogenases with a variety of choices of substrates for a pure alcohol dehydrogenase or for an enzyme in a mixture.
Alcohol dehydrogenases (ADH, EC 1.1.1.1) are a group of dehydrogenase enzymes that act on primary or secondary alcohols, or hemi-acetals and convert them to aldehydes or ketones via reduction of the cofactor NAD (nicotinamide adenine dinucleotide). Alcohol dehydrogenase is a zinc protein, in a dimer complex with a mass of 80 kDa. The enzymes can be found in many organisms, including human, and in various biological activities, including glycolysis/gluconeogenesis; fatty acid degradation; metabolism of glycine, serine, tyrosine, threonine and alpha-linolenic acid; chloroalkane and chloroalkene degradation; naphthalene degradation; retinol metabolism; metabolism of xenobiotics by cytochrome p450; drug metabolism by cytochrome p450; biosynthesis of secondary metabolites; and biosynthesis of antibiotics. For example, in humans and many other animals, alcohol dehydrogenases serve to decompose alcohols to avoid poisoning. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the reversed reaction, the reduction of aldehydes and ketones, in conjugation with oxidation of NAD, to constantly yield enough NAD+ for fermentation. For the large number of reactions that the enzymes catalyze, they could also go with other names:
Spectrophotometric assays are often used to quantify the enzymatic activity of alcohol dehydrogenases, because the reduction of NAD+ to NADH during oxidation of alcohols can be conveniently detected at 340 nm. However, substrate specificity of alcohol dehydrogenases could be very broad, covering many primary and secondary alcohols. For instance, the enzyme from the animal, but not the yeast, also catalyzes oxidation of cyclic secondary alcohols. Therefore, the conventional assay method could be problematic under some the reaction conditions. Furthermore, in some cases the only available sample could be a mixture of alcohol dehydrogenase isozymes or alcohol dehydrogenases with other enzymes, which makes activity measurement even more difficult. Creative Enzymes established robust activity assays that accurately measure the activity of alcohol dehydrogenases under convoluted conditions, such as bovine liver extracts or fermentation lysates, and even in the presence of unconventional substrates other than ethanol. Deep understanding of the properties of alcohol dehydrogenases enables us to face the most challenging activity measurement. In addition to the traditional spectrophotometric assays, we have also developed colorimetric assays that could satisfy special needs such as quick activity screening or reporting enzyme activity in special systems.
Overall, Creative Enzymes is your trustworthy partner for activity measurement for alcohol dehydrogenases. We have not yet disappointed any of our customers in the enzymatic assay of alcohol dehydrogenase. The activity quantification has never been this easy until you choose Creative Enzymes.
Figure: The structure of the enzyme alcohol dehydrogenase class-3, which helps with the metabolism of toxic formaldehyde in human.
