L-iditol 2-dehydrogenase | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() Sorbitol dehydrogenase tetramer, Human | |||||||||
Identifiers | |||||||||
EC no. | 1.1.1.14 | ||||||||
CAS no. | 9028-21-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a L-iditol 2-dehydrogenase (EC 1.1.1.14) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are L-iditol and NAD+, whereas its 3 products are L-sorbose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-iditol:NAD+ 2-oxidoreductase. Other names in common use include polyol dehydrogenase, sorbitol dehydrogenase, L-iditol:NAD+ 5-oxidoreductase, L-iditol (sorbitol) dehydrogenase, glucitol dehydrogenase, L-iditol:NAD+ oxidoreductase, NAD+-dependent sorbitol dehydrogenase, NAD+-dependent sorbitol dehydrogenase, and NAD+-sorbitol dehydrogenase. This enzyme participates in fructose and mannose metabolism.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1K2W, 1PL6, 1PL7, and 1PL8.