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Creative Enzymes offers reliable activity measurement for L-iditol 2-dehydrogenase by spectrophotometric assays. The reliability of the test result is assured by our experienced scientists and the most up-to-date analytic instruments. We are the leading company performing the activity assays of L-iditol 2-dehydrogenase with a variety of choices of substrates for a pure L-iditol 2-dehydrogenase or for an enzyme in a mixture.
L-iditol 2-dehydrogenase (EC 1.1.1.14) is a member of the medium-chain dehydrogenase/reductase protein family. It is categorized as an oxidoreductase, belonging to those acting on the CH-OH group of the electron donor with NAD+ (nicotinamide adenine dinucleotide) specifically, but not NADP+ (nicotinamide adenine dinucleotide phosphate), as the electron acceptor. In enzymology, L-iditol 2-dehydrogenase is the enzyme that catalyzes L-iditol and NAD+ to L-sorbose, NADH and H+. The systematic name of this enzyme class is L-iditol:NAD+ 2-oxidoreductase. The enzyme is also known as other names:
This enzyme is almost expressed ubiquitously in all animal tissues, as well as widely found in plants, archaea, bacteria and yeast. In mammal, the liver and seminal vesicle are the tissues that use this enzyme most frequently. It is important to point out that this enzyme, named as sorbitol dehydrogenase, is involved in fructose and mannose metabolism, and sugar accumulation. As a cytosolic enzyme, a sorbitol dehydrogenase converts sorbitol, the sugar alcohol form of glucose, into fructose, in carbohydrate metabolism. Together with aldose reductase, it can transfer glucose to fructose without using ATP, but it requires NAD+ with respect to conserved zinc binding motif and a hydrophobic substrate-binding pocket. Overall, this enzyme is essential due to its implication in the development of diabetic complications and thus its tertiary structure may facilitate the development of drugs for the treatment of diabetes sufferers.
The substrate specificity of L-iditol 2-dehydrogenase is quite versatile, since it works on a large number of sugar alcohols, including but not limited to L-iditol, D-glucitol, D-xylitol, and D-galactitol. However, its enzymatic activity can be strongly inhibited by both heavy metal ions such as mercury, and thiol compounds, such as L-cysteine. As a result, activity determination of the enzyme becomes a challenge in biological conditions. Creative Enzymes is able to quantify the enzymatic activity of L-iditol 2-dehydrogenase by continuous spectrophotometric rate determination, while avoiding interferences from heavy metals and cysteine.
Creative Enzymes has served the pharmaceutical and nutritional industries for many years with quantification of the enzymatic activity of L-iditol 2-dehydrogenase. Your special needs may involve challenging activity measurement or routine activity screening. In any case, we will be your first choice for the most reliable services.
Figure: The structure of the enzyme sorbitol dehydrogenase from human, as the main biological tetramer, in the complex with four NAD molecules (green) and four zinc ions (blue).
Reference: Pauly TA. et. al., Structure. 2003, 11(9), 1071-1085.
