Sorbitol dehydrogenase  (Synonyms: L-Iditol dehydrogenase; Polyol dehydrogenase; SDH)

Sorbitol dehydrogenase (L-Iditol dehydrogenase) is an oxidoreductasea and catalyses the conversion of sorbitol to fructose with NAD⁺ as the coenzyme. Sorbitol dehydrogenase catalyses pH-dependent redox reactions between NAD⁺/NADH and sorbitol/fructose. Sorbitol dehydrogenase is implicated in diabetic complications and is a biomarker of drug-induced liver injury. Sorbitol dehydrogenase can be used for the research of diabetes and liver injury^[1][2].

Sorbitol dehydrogenase exhibits substrate inhibition at sorbitol concentrations >30 mM and fructose concentrations >100 mM at pH 7.4, with dissociation of the enzyme-coenzyme binary complex as the rate-limiting reaction step^[1].
Sorbitol dehydrogenase exhibits higher apparent affinity for fructose and NADH than for sorbitol and NAD^+[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9028-21-1

Solid

White to off-white

[Sorbitol dehydrogenase]

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• [1]. El-Kabbani O, et al. Sorbitol dehydrogenase: structure, function and ligand design. Curr Med Chem. 2004 Feb;11(4):465-76.

  [2]. Bekhit M, et al. Determination of sorbitol dehydrogenase in microsamples of human serum. Talanta. 2021;235:122730.  [Content Brief]