| 1,5-anhydro-D-fructose reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.263 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
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 (January 1998). "Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose". Journal of Biochemistry. 123 (1): 189–93. doi:10.1093/oxfordjournals.jbchem.a021909. PMID 9504428.
This page was last edited on 26 August 2023, at 12:24