SORD Human
Escherichia Coli.
EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,
SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH
Greater than 90.0% as determined by SDS-PAGE.
Description
SORD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-357a.a.) and having a molecular mass of 38.3kDa.
SORD is purified by proprietary chromatographic techniques.
Product Specs
EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,
SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH
Escherichia Coli.
MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP
Product Science Overview
Sorbitol dehydrogenase (SDH), also known as L-iditol 2-dehydrogenase or SORD, is a crucial enzyme in carbohydrate metabolism. It catalyzes the conversion of sorbitol, a sugar alcohol form of glucose, into fructose. This enzyme plays a significant role in the polyol pathway, which is essential for the metabolism of glucose and fructose in various tissues .
Sorbitol dehydrogenase is a member of the zinc-containing alcohol dehydrogenase family. It exists as a homotetramer and binds one zinc ion per subunit . The enzyme’s activity requires a catalytic zinc atom, which is coordinated by the side chains of three amino acids (Cys44, His69, and Glu70) and one water molecule . NAD+ binds to the protein first, followed by sorbitol, facilitating the oxidation process.
In humans, the SORD gene encodes sorbitol dehydrogenase. The enzyme is widely expressed, with the highest levels found in the kidney and the lens of the eye . It is also present in the epithelial cells of both benign and malignant prostate tissue . The enzyme’s expression is up-regulated by androgens and down-regulated by castration, indicating its potential role in reproductive physiology .
Recombinant human sorbitol dehydrogenase is produced using various expression systems, such as E. coli and HEK293 cells . The recombinant form is often tagged with a His-tag to facilitate purification. For example, a bioactive recombinant protein with an N-terminal His-tag corresponding to the amino acids 1-357 of human sorbitol dehydrogenase has been expressed in E. coli and purified using conventional chromatography techniques .
Recombinant sorbitol dehydrogenase is used in various research applications, including enzyme activity assays and studies on carbohydrate metabolism. It is also employed in investigating the enzyme’s role in different physiological and pathological conditions, such as diabetic complications and sperm motility .
