EC 184.108.40.206, 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
SORD, also referred to as sorbitol dehydrogenase, belongs to the zinc-containing alcohol dehydrogenase family. It is widely produced. The lens of the eyeand the kidney are the protein highest production areas. Zinc-dependent interconversion of polyols, like sorbitol and xylitol, are enzymatically catalysed to their respective ketoses by SORD.
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.
The SORD solution (0.5mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.5) and 1mM DTT.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Greater than 90.0% as determined by SDS-PAGE.
Specific activity > 15unit/mg. Defined by the amount of enzyme that catalyze the reduction 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 37˚C.
Amino acid sequence
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