EC 18.104.22.168 - L-iditol 2-dehydrogenase
IntEnz Enzyme Nomenclature
NAD-dependent sorbitol dehydrogenase
NAD+-dependent sorbitol dehydrogenase
10160 [IUBMB]L-iditolL-iditolName origin: UniProt - CHECKED (C)Formula: C6H14O6
Charge: 0ChEBI compound status: CHECKED (C)NAD+NAD(+)Name origin: UniProt - CHECKED (C)Formula: C21H26N7O14P2
Charge: -1ChEBI compound status: CHECKED (C)<?>L-sorbopyranoseL-sorbopyranoseName origin: UniProt - CHECKED (C)Formula: C6H12O6
Charge: 0ChEBI compound status: CHECKED (C)H+H(+)Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)
This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+.
Links to other databases
Sorbitol dehydrogenase from horse liver: purification, characterization and comparative properties.Comp. Biochem. Physiol. 69B: 909-914 (1981).
Purification and properties of sorbitol dehydrogenase from mouse liver.Int. J. Biochem. 15: 507-511 (1983). [PMID: 6852349]
Rapid affinity purification and properties of rat liver sorbitol dehydrogenase.Biochim. Biophys. Acta 524: 254-261 (1978). [PMID: 667078]
Detection and characterization of sorbitol dehydrogenase from apple callus tissue.Plant Physiol. 64: 69-73 (1979).
Polyol-pathway enzymes of human brain. Partial purification and properties of sorbitol dehydrogenase.Biochem. J. 211: 81-90 (1983). [PMID: 6870831]
Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning.J. Biol. Chem. 267: 24989-24994 (1992). [PMID: 1460002]
[EC 22.214.171.124 created 1961, modified 2011]