Creative Enzymes is a superior company in the field of catalytic activity measurement for oxidoreductases. We have a brilliant team with experienced enzymology experts show are specialized in enzyme activity measurement. Creative Enzymes constantly offers the most reliable results to our customers.

Tagaturonate reductase (EC1.1.1.58) is an NAD-dependent enzyme that catalyzes the oxidation of D-altronate, using NAD⁺ as the redox cofactor to produce D-tagaturonate. This enzyme exists in a wide spectrum of bacteria, such as Paenibacillus polymyxa, Escherichia coli, and Lactococcus lactis. Tagaturonate reductase is a member from the group of oxidoreductases that catalyze the CH-OH group of the substrate and use NAD⁺ or NADP⁺ as the cofactor. The systematic name of this enzyme class is D-altronate:NAD⁺ 3-oxidoreductase. Other names in common use include altronic oxidoreductase, altronate oxidoreductase, TagUAR, altronate dehydrogenase, and D-tagaturonate reductase. Tagaturonate reductase is identified to be closely related with the pathway of pentose and glucuronate interconversions.

Tagaturonate reductase is the second enzyme in the galacturonate catabolism pathway, catalyzing the reversible NADH-dependent reduction of D-tagaturonate to D-altronate. Through this pathway, Escherichia coli can use the hexuronate D-galacturonate as the sole energy source for growth. The first step in the pathway of D-galacturonate degradation is the isomerization to D-tagaturonate, which then undergoes an NADH-dependent reduction to D-altronate which catalyzed by tagaturonate reductase. The subsequent dehydration yields 2-dehydro-3-deoxy-D-gluconate. At this point, the superpathway of β-D-glucuronide, D-glucuronate degradation, and D-galacturonate degradation I pathways converge. As indicated, tagaturonate reductase is a critical enzyme for D-galacturonate degradation I pathway, and it is essential to the growth of Escherichia coli. Although the enzyme presents high potential values in biotechnology, little research has been done to understand the catalytic activity and structure of this enzyme. Thus, Creative Enzymes developed robust activity assays to satisfy the customers’ request of activity determination for tagaturonate reductase. The spectrophotometric assay was demonstrated to be a reliable method for activity quantification. Creative Enzymes offers the extraordinary services and has the most advanced techniques for enzyme activity measurement. Overall, Creative Enzymes is your best choice for the further research and applications of tagaturonate reductase.

Figure: The crystal structure of tagaturonate reductase. UniProt ID: B5Z1X8