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Enzyme Nomenclature
Information on EC 1.1.1.292 - 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.1.292
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RECOMMENDED NAME
GeneOntology No.
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
1,5-anhydro-D-mannitol:NADP+ oxidoreductase
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].
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CAS REGISTRY NUMBER
COMMENTARY
206138-19-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylosone + NADPH + H+
D-lyxose + NADP+
17% of the activity with 1,5-anhydro-D-fructose
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?
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
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-
-
-
?
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
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-
-
r
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
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-
-
-
?
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
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-
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r
1,5-anhydro-D-glucitol + NADP+
?
23% of the activity with 1,5-anhydro-D-mannitol
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?
1,5-anhydro-D-glucitol + NADP+
?
23% of the activity with 1,5-anhydro-D-mannitol
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?
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-fructose is the preferred substrate for the reductase reaction
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r
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
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-
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r
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-fructose is the preferred substrate for the reductase reaction
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r
6-deoxy-D-glucosone + NADPH + H+
6-deoxy-D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
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?
6-deoxy-D-glucosone + NADPH + H+
6-deoxy-D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
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?
D-allosone + NADPH + H+
D-altrose + NADP+
10% of the activity with 1,5-anhydro-D-fructose
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?
D-allosone + NADPH + H+
D-altrose + NADP+
10% of the activity with 1,5-anhydro-D-fructose
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?
D-glucosone + NADPH + H+
D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
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?
D-glucosone + NADPH + H+
D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
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?
additional information
?
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D-glucose, D-fructose, glucuronic acid, DL-glyceraldehyde, formaldehyde, and acetone are poor substrates, substrate specificity of the recombinant enzyme, overview
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additional information
?
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D-glucose, D-fructose, glucuronic acid, DL-glyceraldehyde, formaldehyde, and acetone are poor substrates, substrate specificity of the recombinant enzyme, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
Q9DCT1
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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wild-type enzyme and mutant enzymes S10G, S33D, K94G, D176A, H180A and G206I shows no activity with NADH. Mutant enzymes A13G, S10G/A13G and S33D/A13G are active with NADH
NADPH
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the N-terminal domain displays a Rossman fold and contains the cofactor binding site. The intact crystals contain the oxidized cofactor NADP+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
6.4
1,5-Anhydro-D-fructose
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pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
7.1
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
8.3
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme G206I, cofactor: NADPH; pH 6.5, native wild-type enzyme, cofactor: NADPH
20.2
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
39
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
0.06
NADPH
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pH 6.5, mutant enzyme G206I; pH 6.5 recombinant wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.5
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
6.3
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
13.5
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
145
1,5-Anhydro-D-fructose
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pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
216
1,5-Anhydro-D-fructose
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pH 6.5, native wild-type enzyme, cofactor: NADPH
369
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, enzyme crystallized in complex with the cofactor NADP(H) and its structure is determined to 2.2 A resolution using selenomethionine single-wavelength anomalous dispersion
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in complex with NADP(H), to 1.93 A resolution. The structure displays an empty substrate-binding, showing an open conformation of the enzyme state shortly after the release of product, presumably with bound oxidized cofactor NADP+. Amino-acid residues Lys94, His151, Trp162, Arg163, Asp176 and His180 are involved in substrate binding, catalysis or product release. The side chain of Lys94 may function as a molecular switch
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 17.6fold from Escherichia coli strain BL21 (DE3) by anion exchange and adsorption chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AKR1E1 gene, cloning from liver RNA, DNA and amino acid sequence determination, analysis, and comparison, expression in Escherichia coli strain BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A13G
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.8fold higher than wild type value. Mutant enzyme shows activity with NADH as cofactor
G206I
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.4fold lower than wild type value
H180A
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 61.9fold lower than wild type value
K94G
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 137fold lower than wild type value
S10G
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.3fold higher than wild type value
S10G/A13G
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 2fold higher than wild type value. Mutant enzyme shows activity with NADH as cofactor
S176A
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1001fold lower than wild type value
S33D/A13G
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kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 84fold lower than wild type value. Mutant enzyme shows activity with NADH as cofactor
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.292)
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