1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)

1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
Identifiers
EC number	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
Search PMC articles PubMed articles

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-mannitol + NADP⁺ $\rightleftharpoons$ 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 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

• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1392929. 
• 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 A 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.