1,5-anhydro-D-fructose reductase
| 1,5-anhydro-D-fructose reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.263 | ||||||||
| CAS number | 206138-19-4 | ||||||||
| 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 / EGO | ||||||||
| 
 | |||||||||
In enzymology, a 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) is an enzyme that catalyzes the chemical reaction
- 1,5-anhydro-D-glucitol + NADP+ 1,5-anhydro-D-fructose + NADPH + H+
Thus, the two substrates of this enzyme are 1,5-anhydro-D-glucitol and NADP+, whereas its 3 products are 1,5-anhydro-D-fructose, NADPH, 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 1,5-anhydro-D-glucitol:NADP+ oxidoreductase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GLX.
References
- Sakuma M; Kametani S; Akanuma H. "Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose". J. Tokyo. Biochem. (1): 189–193. PMID 9504428.
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