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Enzyme Activity Measurement for Lactaldehyde Dehydrogenase



Creative Enzymes has be engaged in the industry of enzyme activity measurement for many years. We are committed to being the most reliable service provider of enzyme activity assays in the global market. Our spectrophotometric assay was demonstrated to be a highly reliable method for activity quantification of lactaldehyde dehydrogenase.

Lactaldehyde dehydrogenase (EC 1.2.1.22) is an NAD+-dependent enzyme that catalyzes the irreversible oxidation of lactaldehyde to lactate via using NAD+ as the redox cofactor, while simultaneously generating NADH, which acts as a hydrogen donor for many biosynthetic processes. This enzyme is a member of the oxidoreductase family, more specifically, the oxidoreductases that catalyze the CH-OH group of the substrate and use NAD+ or NADP+ as the cofactor. This enzyme can be isolated and characterized from both bacteria and eukaryotes, such as Azotobacter vinelandii, Bacillus subtilis, and Escherichia coli which is the most extensively studied with lactaldehyde dehydrogenase. The systematic name of this enzyme class is (S)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include L-lactaldehyde:NAD+ oxidoreductase, and nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase.

Lactaldehyde dehydrogenase participates in the conversion of lactaldehyde to pyruvate, which is a critical part of the pyruvate metabolism. First, lactaldehyde dehydrogenase oxidizes lactaldehyde to lactate using NAD+ as the cofactor. Then lactate is oxidized to produce pyruvate, which subsequently undergoes decarboxylation and conversion to acetyl CoA for entry into the Krebs cycle in a series of reactions. Additionally, lactaldehyde dehydrogenase from E.coli was reported to be capable of catalyzing the oxidation of the metabolic intermediate glycolaldehyde to glycolate. Meanwhile, evidence suggests that lactaldehyde dehydrogenase may function in multiple metabolic pathways due to its ability to oxidize a variety of small α-hydroxyaldehyde substrates. To this point, lactaldehyde dehydrogenase is hence generally classified as an aldehyde dehydrogenase because of its broad substrate specificity.

Despite of the multiple functions performed by lactaldehyde dehydrogenase, activity assays of this enzyme using spectrophotometry have not been well established in an industrial scale. Creative Enzymes is proud to offer the most reliable, accurate, and fast activity measurement for lactaldehyde dehydrogenase. Spectrophotometric assays for lactaldehyde dehydrogenase activities are performed at room temperature by following the absorbance at 340 nm (NADH formation). Creative Enzymes promises to deliver the test results in the shortest span of time from the date of order placement. Overall, Creative Enzymes is your best choice of enzyme activity tests. We are always looking forward to having your business.

Enzyme Activity Measurement for Lactaldehyde Dehydrogenase Figure: The crystal structure of lactaldehyde dehydrogenase from E. coli.
PDB: 2OPX



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