EC 1.1.1.292 - 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)

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IntEnz Enzyme Nomenclature
EC 1.1.1.292

Names

Accepted name:
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
Other names:
1,5-anhydro-D-fructose reductase [ambiguous]
AFR
Systematic name:
1,5-anhydro-D-mannitol:NADP+ oxidoreductase

Reaction

Comments:

This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family [2]. This enzyme 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 [1]. The enzyme 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. It does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones [1].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033712
UniProtKB/Swiss-Prot:

References

  1. Kühn, A., Yu, S. and Giffhorn, F.
    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: 1248-1257 (2006). [PMID: 16461673]
  2. Dambe, T.R., Kühn, A.M., Brossette, T., Giffhorn, F. and Scheidig, A.J.
    Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis.
    Biochemistry 45: 10030-10042 (2006). [PMID: 16906761]

[EC 1.1.1.292 created 2007]