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Information on EC 1.1.1.292 - 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) for references in articles please use BRENDA:EC1.1.1.292
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EC Tree
IUBMB Comments This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family . 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 . 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 .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
1,5-anhydro-D-fructose reductase, 1,5-anhydro-D-fructose reductase (ambiguous), AF reductase, AFR, AKR1E1, More, NADPH dependent 1,5-anhydro-D-fructose reductase,
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1,5-anhydro-D-fructose reductase
1,5-anhydro-D-fructose reductase (ambiguous)
NADPH dependent 1,5-anhydro-D-fructose reductase
1,5-anhydro-D-fructose reductase
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1,5-anhydro-D-fructose reductase
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1,5-anhydro-D-fructose reductase (ambiguous)
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1,5-anhydro-D-fructose reductase (ambiguous)
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AF reductase
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AFR
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AKR1E1
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NADPH dependent 1,5-anhydro-D-fructose reductase
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NADPH dependent 1,5-anhydro-D-fructose reductase
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additional information
the enzyme is a member of the aldo-keto reductase family 1
additional information
the enzyme is a member of the aldo-keto reductase family 1
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1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
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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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1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-glucitol + NADP+
?
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
6-deoxy-D-glucosone + NADPH + H+
6-deoxy-D-mannose + NADP+
9,10-phenanthrenequinone + NADPH
? + NADP+
butane-2,3-dione + NADPH
acetoin + NADP+
D-allosone + NADPH + H+
D-altrose + NADP+
D-glucosone + NADPH + H+
D-mannose + NADP+
D-xylosone + NADPH + H+
D-lyxose + NADP+
17% of the activity with 1,5-anhydro-D-fructose
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?
additional information
?
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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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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
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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
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
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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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?
9,10-phenanthrenequinone + NADPH
? + NADP+
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?
9,10-phenanthrenequinone + NADPH
? + NADP+
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-
-
?
butane-2,3-dione + NADPH
acetoin + NADP+
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-
-
?
butane-2,3-dione + NADPH
acetoin + NADP+
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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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1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
Q9DCT1
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r
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
Q9DCT1
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r
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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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inactive towards 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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1.02 - 49
1,5-Anhydro-D-fructose
11
D-glucosone
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pH 6.5, 30°C
1.02
1,5-Anhydro-D-fructose
pH 7.0, 37°C, recombinant enzyme
3.2
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
3.5
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G, cofactor: NADPH
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
8.4
1,5-Anhydro-D-fructose
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pH 6.5, 30°C
8.5
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme A13G, cofactor: NADPH
8.9
1,5-Anhydro-D-fructose
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pH 8.0, mutant enzyme H180A, cofactor: NADPH
11.1
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme A13G, cofactor: NADH
20.2
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
22.5
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme K94G, cofactor: NADPH
39
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
49
1,5-Anhydro-D-fructose
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pH 7.5, mutant enzyme D176A, cofactor: NADPH
1.1
NADH
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pH 6.5, mutant enzyme A13G; pH 6.5, mutant enzyme S33D/A13G
1.2
NADH
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pH 6.5, mutant enzyme S10G/A13G
0.02
NADPH
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pH 6.5, mutant enzyme A13G
0.06
NADPH
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pH 6.5, mutant enzyme G206I; pH 6.5 recombinant wild-type enzyme
0.1
NADPH
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pH 6.5, native wild-type enzyme
0.2
NADPH
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pH 6.5, mutant enzyme K94G
0.27
NADPH
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pH 6.5, mutant enzyme S10G
0.38
NADPH
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pH 6.5, mutant enzyme S10G/A13G
1
NADPH
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pH 6.5, mutant enzyme S33D/A13G
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1.3 - 1300
1,5-Anhydro-D-fructose
63.2
D-glucosone
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pH 6.5, 30°C
1.3
1,5-Anhydro-D-fructose
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pH 7.5, mutant enzyme D176A, cofactor: NADPH
3.7
1,5-Anhydro-D-fructose
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pH 8.0, mutant enzyme H180A, cofactor: NADPH
4.2
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme K94G, cofactor: NADPH
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
9.3
1,5-Anhydro-D-fructose
pH 7.0, 37°C, recombinant enzyme
12.4
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme A13G, cofactor: NADH
13.5
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
119
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G, cofactor: NADPH
145
1,5-Anhydro-D-fructose
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pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
156
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme G206I, cofactor: NADPH
216
1,5-Anhydro-D-fructose
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pH 6.5, native wild-type enzyme, cofactor: NADPH
286.7
1,5-Anhydro-D-fructose
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pH 6.5, 30°C
369
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
405
1,5-Anhydro-D-fructose
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pH 6.5, mutant enzyme A13G, cofactor: NADPH
1300
1,5-Anhydro-D-fructose
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pH 6.5, 30°C
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484
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recombinant enzyme expressed in Escherichia coli
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7
assay at, reverse reaction
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5.2 - 8.8
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about 50% of maximal activity at pH 5.5 and at pH 8.8
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4.3
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isoelectric focusing
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i.e. Ensifer adhaerens
SwissProt
brenda
i.e. Ensifer adhaerens
SwissProt
brenda
C57BL/6J mice
UniProt
brenda
C57BL/6J mice
UniProt
brenda
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UniProt
brenda
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Rhizobium meliloti (strain 1021)
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35100
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1 * 35100, MALDI-TOF-MS
40000
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1 * 40000, SDS-PAGE
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monomer
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1 * 35100, MALDI-TOF-MS; 1 * 40000, SDS-PAGE
monomer
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1 * 35100, MALDI-TOF-MS; 1 * 40000, SDS-PAGE
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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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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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-20°C or 0°C, 50 days, 50% loss of activity
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native and recombinant enzyme
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recombinant enzyme 17.6fold from Escherichia coli strain BL21 (DE3) by anion exchange and adsorption chromatography
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AKR1E1 gene, cloning from liver RNA, DNA and amino acid sequence determination, analysis, and comparison, expression in Escherichia coli strain BL21 (DE3)
expression in Escherichia coli
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expresssion in Escherichia coli
overexpression in Escherichia coli
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Kuehn, A.; Yu, S.; 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
Ensifer adhaerens (Q2I8V6), Ensifer adhaerens S-30.7.5 (Q2I8V6)
brenda
Dambe, T.R.; Kuehn, A.M.; Brossette, T.; Giffhorn, F.; Scheidig, A.J.
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
Biochemistry
45
10030-10042
2006
Ensifer adhaerens (Q2I8V6)
brenda
Sakuma, M.; Kubota, S.
Mouse AKR1E1 is an ortholog of pig liver NADPH dependent 1,5-anhydro-D-fructose reductase
Biosci. Biotechnol. Biochem.
72
872-876
2008
Mus musculus (Q9DCT1), Mus musculus C57/BL6J (Q9DCT1)
brenda
Schu, M.; Faust, A.; Stosik, B.; Kohring, G.W.; Giffhorn, F.; Scheidig, A.J.
The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation
Acta Crystallogr. Sect. F
69
844-849
2013
Sinorhizobium meliloti (Q92KZ3)
brenda
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1.1.1.292 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
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