| EC |
1.1.1.292 |
| Accepted name: |
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) |
| Reaction: |
1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+ |
| Other name(s): |
1,5-anhydro-D-fructose reductase (ambiguous); AFR (ambiguous) |
| Systematic name: |
1,5-anhydro-D-mannitol:NADP+ oxidoreductase |
| 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: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB |
| 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 (2006) 1248–1257. [DOI] [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 (2006) 10030–10042. [DOI] [PMID: 16906761] |
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| [EC 1.1.1.292 created 2007] |
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