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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 enzyme appears in viruses and cellular organisms
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
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1,5-anhydro-D-fructose reductase (ambiguous)
NADPH dependent 1,5-anhydro-D-fructose reductase
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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-
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-
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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 + NADH + H+
1,5-anhydro-D-mannitol + NAD+
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-
r
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+
-
-
r
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+
-
-
?
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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?
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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
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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
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NADH
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
inactive towards NADH
NADPH
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
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
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
3.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G, cofactor: NADPH
6.4
1,5-Anhydro-D-fructose
pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
7.1
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
8.3
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme G206I, cofactor: NADPH
8.3
1,5-Anhydro-D-fructose
pH 6.5, native wild-type enzyme, cofactor: NADPH
8.4
1,5-Anhydro-D-fructose
pH 6.5, 30°C
8.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme A13G, cofactor: NADPH
8.9
1,5-Anhydro-D-fructose
pH 8.0, mutant enzyme H180A, cofactor: NADPH
11.1
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme A13G, cofactor: NADH
20.2
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
22.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme K94G, cofactor: NADPH
39
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
49
1,5-Anhydro-D-fructose
pH 7.5, mutant enzyme D176A, cofactor: NADPH
1.1
NADH
pH 6.5, mutant enzyme A13G
1.1
NADH
pH 6.5, mutant enzyme S33D/A13G
1.1
NADH
mutant enzyme A13G/S33D, at pH 6.5 and 30°C
1.2
NADH
pH 6.5, mutant enzyme S10G/A13G
1.2
NADH
mutant enzyme A13G/S10G, at pH 6.5 and 30°C
0.02
NADPH
pH 6.5, mutant enzyme A13G
0.06
NADPH
pH 6.5 recombinant wild-type enzyme
0.06
NADPH
pH 6.5, mutant enzyme G206I
0.1
NADPH
pH 6.5, native wild-type enzyme
0.2
NADPH
pH 6.5, mutant enzyme K94G
0.27
NADPH
pH 6.5, mutant enzyme S10G
0.38
NADPH
pH 6.5, mutant enzyme S10G/A13G
1
NADPH
pH 6.5, mutant enzyme S33D/A13G
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1.3 - 1300
1,5-Anhydro-D-fructose
63.2
D-glucosone
pH 6.5, 30°C
1.3
1,5-Anhydro-D-fructose
pH 7.5, mutant enzyme D176A, cofactor: NADPH
3.7
1,5-Anhydro-D-fructose
pH 8.0, mutant enzyme H180A, cofactor: NADPH
4.2
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme K94G, cofactor: NADPH
5.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
6.3
1,5-Anhydro-D-fructose
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
pH 6.5, mutant enzyme A13G, cofactor: NADH
13.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
119
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G, cofactor: NADPH
145
1,5-Anhydro-D-fructose
pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
156
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme G206I, cofactor: NADPH
216
1,5-Anhydro-D-fructose
pH 6.5, native wild-type enzyme, cofactor: NADPH
286.7
1,5-Anhydro-D-fructose
pH 6.5, 30°C
369
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
405
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme A13G, cofactor: NADPH
1300
1,5-Anhydro-D-fructose
pH 6.5, 30°C
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484
recombinant enzyme expressed in Escherichia coli
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7
assay at, reverse reaction
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5.2 - 8.8
about 50% of maximal activity at pH 5.5 and at pH 8.8
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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
-
UniProt
brenda
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Rhizobium meliloti (strain 1021)
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35100
1 * 35100, MALDI-TOF-MS
40000
1 * 40000, SDS-PAGE
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monomer
1 * 40000, SDS-PAGE
monomer
1 * 35100, MALDI-TOF-MS
monomer
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1 * 40000, SDS-PAGE
monomer
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1 * 35100, MALDI-TOF-MS
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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
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
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
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.4fold lower than wild type value
H180A
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 61.9fold lower than wild type value
K94G
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 137fold lower than wild type value
S10G
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.3fold higher than wild type value
S10G/A13G
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
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1001fold lower than wild type value
S33D/A13G
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
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
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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