In enzymology, a 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) (EC 1.1.1.292) is an enzyme that catalyzes the chemical reaction
| 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.292 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- 1,5-anhydro-D-mannitol + NADP+ 1,5-anhydro-D-fructose + NADPH + H+
Thus, the two substrates of this enzyme are 1,5-anhydro-D-mannitol and NADP+, whereas its 3 products are 1,5-anhydro-D-fructose, NADPH, and H+.
This enzyme belongs to the common 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-mannitol:NADP+ oxidoreductase. Other names in common use include 1,5-anhydro-D-fructose reductase (ambiguous), and AFR.
References
edit- Kuhn A, Yu S, Giffhorn F (2006). "Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis". Appl. Environ. Microbiol. 72 (2): 1248–57. doi:10.1128/AEM.72.2.1248-1257.2006. PMC 1392929. PMID 16461673.
- Dambe TR, Kuhn AM, Brossette T, Giffhorn F, Scheidig AJ (2006). "Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: construction of an NADH-accepting mutant and its application in rare sugar synthesis". Biochemistry. 45 (33): 10030–42. doi:10.1021/bi052589q. PMID 16906761.
