CATH Classification

Domain Context

CATH Clusters

Superfamily Dihydrodipicolinate Reductase; domain 2
Functional Family 1,5-anhydro-D-fructose reductase

Enzyme Information

1.1.1.292
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming).
based on mapping to UniProt Q92KZ3
1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + NADPH.
-!- Present in some but not all Rhizobium species. -!- Differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). -!- In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro- D-mannitol, can be further metabolized to D-mannose. -!- Also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. -!- Does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones.
1.1.1.-
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt Q92KZ3

UniProtKB Entries (1)

Q92KZ3
AFR_RHIME
Sinorhizobium meliloti 1021
1,5-anhydro-D-fructose reductase

PDB Structure

PDB 4KOA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation.
Schu, M., Faust, A., Stosik, B., Kohring, G.W., Giffhorn, F., Scheidig, A.J.
Acta Crystallogr.,Sect.F