SORD Human, His

Sorbitol Dehydrogenase (SORD), also known as L-iditol 2-dehydrogenase or SORD1, is an enzyme that plays a crucial role in the polyol pathway. This enzyme is responsible for the zinc-dependent interconversion of polyols, such as sorbitol and xylitol, to their respective ketoses . The recombinant form of this enzyme, tagged with a His-tag, is widely used in research to study its structure, function, and potential therapeutic applications.

The recombinant human Sorbitol Dehydrogenase is typically expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The protein consists of 357 amino acids and has a molecular weight of approximately 40.4 kDa . The His-tag, which is fused to the N-terminus of the protein, facilitates its purification and detection.

Sorbitol Dehydrogenase catalyzes the conversion of sorbitol to fructose, a reaction that is essential for the metabolism of glucose and fructose . This enzyme is widely expressed in various tissues, with the highest expression observed in the kidney and the lens of the eye . The specific activity of the recombinant enzyme is greater than 20,000 pmol/min/µg, indicating its high catalytic efficiency .

The recombinant form of Sorbitol Dehydrogenase is used extensively in biochemical and physiological studies. Researchers utilize this enzyme to investigate its role in diabetic complications, such as diabetic retinopathy and neuropathy, where the accumulation of sorbitol is implicated . Additionally, the enzyme is used in studies related to fructose metabolism and its impact on various metabolic disorders.

For optimal stability, the recombinant Sorbitol Dehydrogenase should be stored at 4°C for short-term use and at -20°C for long-term storage . It is important to avoid repeated freeze-thaw cycles to maintain the enzyme’s activity and integrity.