Creative Enzymes is committed to being the most reliable service provider for enzyme activity measurement in the global market. We are proud to provide the accurate and fast assays for enzyme activity measurement of sorbitol-6-phosphate 2-dehydrogenase by using spectrophotometric assays. Creative Enzymes is equipped with the leading techniques, the first-class spectrophotometric instruments, and the excellent scientists who have been devoting themselves into enzyme activity assays for many years.

Sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140; S6PDH) is an enzyme that catalyzes a reversible oxidoreduction reaction between D-sorbitol 6-phosphate and D-fructose 6-phosphate, while simultaneously generating NADH, which acts as a hydrogen donor for many biosynthetic processes. Sorbitol-6-phosphate 2-dehydrogenase can be found in many bacteria, such as Escherichia coli, Clostridium pasteurianum, and Lactobacillus casei. This enzyme is a member of the oxidoreductase family, and the systematic name of this enzyme class is D-sorbitol-6-phosphate:NAD⁺2-oxidoreductase, which is also known as ketosephosphate reductase, D-sorbitol 6-phosphate dehydrogenase, D-sorbitol-6-phosphate dehydrogenase, sorbitol-6-P-dehydrogenase, and D-glucitol-6-phosphate dehydrogenase.

Sorbitol-6-phosphate 2-dehydrogenase is involved in one step of the sub-pathway that synthesizes D-fructose 6-phosphate from D-sorbitol 6-phosphate. This sub-pathway is part of the D-sorbitol degradation pathway, which is part of fructose and mannose metabolism. D-sorbitol is one of the three existing hexitols which occur naturally. It can be utilized by bacteria as a total source of carbon and energy. The product of D-sorbitol degradation II is β-D-fructofuranose 6-phosphate, an intermediate of glycolysis, and hence it flows through the pathways of central metabolism to satisfy the cell's need for precursor metabolites, reducing power, and metabolic energy. Sorbitol-6-phosphate 2-dehydrogenase is a poorly studied enzyme. Little research has been done to understand the activity of the enzyme. Properly measuring its activity is even more difficult without the information of its structure and catalytic mechanism. Fortunately, Creative Enzymes developed robust activity assays to satisfy the customer’s request, relying on our own expert team. The spectrophotometric assay was demonstrated to be a reliable method for activity quantification. Creative Enzymes is equipped with the most advanced spectrophotometric instrument and is quite confident to provide precise enzyme assays. We promise that we will deliver the results in the shortest span of time from the date of order placement. Overall, Creative Enzymes is committed to achieving the highest grade of customers’ satisfaction, and to constantly improving its products, services, and quality management system.

Figure: The crystal structure of sorbitol-6-phosphate 2-dehydrogenase from E. coli.
UniProtID: P05707