Creative Enzymes offers reliable activity measurement for aldehyde reductases. The activity assays are performed on the most up-to-date analytic instruments using spectrophotometric assays. We stand out with a quick turnover of the activity assays in response to the request of a typical activity determination or a customized task.

Alcohol dehydrogenase (NADP+) (EC 1.1.1.2) is a group of oxidoreductase enzymes that can be commonly found in bacteria, archaea, and eukaryote. The enzyme mainly catalyzes oxidation of primary alcohols and convert them to aldehydes, although some member of the enzyme family could also act on secondary alcohols. The reaction is reversible and could be catalyzed by the same enzyme to give primary alcohols as the product through reduction of aldehydes. NADP (Nicotinamide adenine dinucleotide phosphate) is employed by the enzyme as the redox cofactor, which acts as the electron donor during reduction of aldehydes, or as the electron acceptor in the oxidation reaction of alcohols. The enzyme is also known as other names:

• NADP-alcohol dehydrogenase;
• NADP+-aldehyde reductase;
• NADP+-dependent aldehyde reductase;
• NADPH-aldehyde reductase;
• NADPH-dependent aldehyde reductase;
• nonspecific succinic semialdehyde reductase;
• ALR 1;
• low-Km aldehyde reductase;
• high-Km aldehyde reductase;
• aldehyde reductase

The enzyme is important and essential in many biological pathways, including glycolysis/gluconeogenesis; pentose and glucuronate interconversions; glycerolipid metabolism; caprolactam degradation; metabolic pathways; biosynthesis of secondary metabolites; microbial metabolism in diverse environments; and biosynthesis of antibiotics.

Because alcohol dehydrogenase (NADP+) uses NADP as the redox cofactor, the progressing of the enzymatic reaction can be monitored at 340 nm, where NADPH has a UV absorption peak and NADP+ does not. Therefore, spectrophotometric assays are conventionally used as the primary method for activity measurement. Creative Enzymes is not only distinguished by many years of high-quality activity using the spectrophotometric assay, but also well known for the colorimetric assay that was developed by our scientists to satisfy special needs in activity determination that cannot be easily performed through the conventional spectrophotometric assay.

Alcohol dehydrogenase (NADP+) is a zinc protein. However, the Zn2+ ion is not necessary for structural stability of the enzyme. Some of these enzymes, especially members from bacteria, are very sensitive to oxygen. Some alcohol dehydrogenases (NADP+) showed a half-life of 4-60 min upon the exposure to air. As a comparison, the enzymes are very stable under anaerobic conditions even at high temperatures, such as 85-95°C. The sensitivity to oxygen certainly increases the barrier to reliable measurement of the enzyme activity. Creative Enzymes developed air-tight, non-interfering activity assays that are specially designed for activity measurement for alcohol dehydrogenase (NADP+). The enzymes stay highly active for several hours to days during the test, maintaining consistency through batches of activity assays.

Creative Enzymes’ leading position in the enzyme activity assays will definitely accelerate your work with alcohol dehydrogenase (NADP+). A common or special alcohol dehydrogenase (NADP+), great accuracy or high reproducibility, we can always bring the correct solution to overcome the obstacles on your way to success.

Figure: The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes
Reference: El-Kabbani, O. et. al., Acta Crystallogr. Sect. D Biol. Crystallogr. 1994, 50 (6), 859.