In enzymology, a L-iditol 2-dehydrogenase (EC 1.1.1.14) is an enzyme that catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
- L-iditol + NAD+ ⇌ L-sorbose + NADH + H+
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.
Structural studies edit
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1K2W, 1PL6, 1PL7, and 1PL8.
References edit
- Bailey JP, Renz C, McGuinness ET (1981). "Sorbitol dehydrogenase from horse liver: purification, characterization and comparative properties". Comp. Biochem. Physiol. 69B: 909–914.
- Burnell JN, Holmes RS (1983). "Purification and properties of sorbitol dehydrogenase from mouse liver". Int. J. Biochem. 15 (4): 507–11. doi:10.1016/0020-711X(83)90124-6. PMID 6852349.
- Leissing N, McGuinness ET (1978). "Rapid affinity purification and properties of rat liver sorbitol dehydrogenase". Biochim. Biophys. Acta. 524 (2): 254–61. doi:10.1016/0005-2744(78)90162-6. PMID 667078.
- Negm FB, Loescher WH (1979). "Detection and Characterization of Sorbitol Dehydrogenase from Apple Callus Tissue". Plant Physiol. 64 (1): 69–73. doi:10.1104/pp.64.1.69. PMC 543026. PMID 16660917.
- O'Brien MM, Schofield PJ, Edwards MR (1983). "Polyol-pathway enzymes of human brain. Partial purification and properties of sorbitol dehydrogenase". Biochem. J. 211 (1): 81–90. doi:10.1042/bj2110081. PMC 1154331. PMID 6870831.
