The structure of human sorbitol dehydrogenase was determined through crystallization experiments and X-ray diffraction (with a resolution of 2.20 Å).

Sorbitol dehydrogenase belongs to the oxidoreductase family, which means that it helps catalyze oxidation reduction reactions.

[5] The general binding process in SDH is described by the gain in free energy, which can be determined from the rate of association and dissociation between subunits.

For example, a study of SDH that used diverse methods such as protein sequence alignments, structural comparisons, energy calculations, gelfiltration experiments, and enzyme kinetics experiments could reveal an important hydrogen-bonding network that stabilizes the tetrameric quaternary structure in mammalian SDH.

In uncontrolled diabetes, large amounts of glucose enter these tissues and is then converted to sorbitol by aldose reductase.

Sorbitol then accumulates, causing water to be drawn into the cell due to the increased osmotic pressure, impairing tissue function.