KEGG   ENZYME: 1.1.1.292Help
Entry
EC 1.1.1.292                Enzyme                                 

Name
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming);
1,5-anhydro-D-fructose reductase (ambiguous);
AFR
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
1,5-anhydro-D-mannitol:NADP+ oxidoreductase
Reaction(IUBMB)
1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+ [RN:R08194]
Reaction(KEGG)
Substrate
1,5-anhydro-D-mannitol [CPD:C16538];
NADP+ [CPD:C00006]
Product
1,5-anhydro-D-fructose [CPD:C06485];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
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].
History
EC 1.1.1.292 created 2007
Orthology
K19181  
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
Genes
MARS: 
VEI: 
DEL: 
LCH: 
MLO: 
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MAM: 
AAK: 
SME: 
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 » show all
Taxonomy
Reference
1  [PMID:16461673]
  Authors
Kuhn A, Yu S, Giffhorn F.
  Title
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.
  Journal
Appl. Environ. Microbiol. 72 (2006) 1248-57.
  Sequence
Reference
2  [PMID:16906761]
  Authors
Dambe TR, Kuhn AM, Brossette T, Giffhorn F, Scheidig AJ.
  Title
Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis.
  Journal
Biochemistry. 45 (2006) 10030-42.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 

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