Enzyme Activity Measurement for D-Malate Dehydrogenase (Decarboxylating) Using Spectrophotometric Assays

Creative Enzymes is a leading company in the field of enzyme activity measurement. We are well known to provide the assay service of utmost quality. The spectrophotometric assay is considered to be the most effective and reliable method for the measurement of catalytic activity for D-malate dehydrogenase (decarboxylating). Creative Enzymes is proud to supply the most accurate spectrophotometric assays for the enzyme activity measurement.

D-malate dehydrogenase (decarboxylating) (EC 1.1.1.83) is an enzyme that catalyzes a reversible oxidoreduction reaction between (R)-malate and pyruvate. The reaction simultaneously generates NADH and CO₂, which acts as a hydrogen donor for many biosynthetic processes, and as a vital gas for various chemical reactions, respectively. This enzyme belongs to the family of oxidoreductases, and the systematic name of this enzyme class is (R)-malate:NAD⁺ oxidoreductase (decarboxylating). The other names in common use include: D-malate dehydrogenase, D-malic enzyme, and bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating).

D-malate dehydrogenase (decarboxylating) is a member of the β-decarboxylating dehydrogenase super-family, which catalyze the successive oxidation and decarboxylation of substrates with a common R-malate moiety and variable γ-substituents on C-3, with different sizes, polarity, or configurations. Note that D-malate dehydrogenase plays an important role in the degradation of D-malate, which is one route of butanoate metabolism. In E.coli, D-malate is transported into the cell by the proton motivated force-dependent dicarboxylate transporter DctA. Then D-malate is converted to pyruvate catalyzed by D-malate dehydrogenase (decarboxylating). The product of this reaction, pyruvate then enters central metabolism via pyruvate dehydrogenase. Thus the D-malate dehydrogenase from E.coli is responsible for aerobic growth on D-malate as the sole carbon source under aerobic conditions. However, D-malate alone is unable to support growth as the sole source of carbon under anaerobic conditions. Based on the meaningful function performed by D-malate dehydrogenase (decarboxylating), this enzyme serves a vital substance in chemical and biological researches. Therefore, D-malate dehydrogenase (decarboxylating) is getting more and more attentions from chemical and biological industries, so is the activity measurement of this enzyme. But the measurement of catalytic activity for this enzyme was reported to be complicated and difficult. Fortunately, Creative Enzymes made accurate activity assays available for D-malate dehydrogenase (decarboxylating) by using the spectrophotometric assays. Creative Enzymes is the home of many brilliant scientists and the most advanced instrument. Our passion for high-quality and unique service is exceeded only by our excellent reputation in the marketplace. Overall, Creative Enzymes is your trustworthy partner and we will never disappoint our clients.

Figure: The crystal structure of D-malate dehydrogenase (decarboxylating) from E. coli. UniProt ID: P76251