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EC Tree
IUBMB Comments Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
1,5-anhydro-d-fructose reductase, akr1e1, af reductase, nadph-dependent monomeric reductase,
more
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NADP(H)-dependent 1,5-anhydro-D-fructose reductase
NADP-1,5-anhydro-D-fructose reductase
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NADPH dependent 1,5-anhydro-D-fructose reductase
-
-
NADPH-dependent anhydrofructose reductase
NADPH-dependent monomeric reductase
additional information
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the enzyme belongs to the aldo-keto reductase family 1
1,4-AF-reductase
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-
AFR
-
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NADP(H)-dependent 1,5-anhydro-D-fructose reductase
-
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NADP(H)-dependent 1,5-anhydro-D-fructose reductase
-
-
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NADPH-dependent anhydrofructose reductase
-
-
NADPH-dependent anhydrofructose reductase
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-
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NADPH-dependent monomeric reductase
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-
NADPH-dependent monomeric reductase
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-
-
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1,5-anhydro-D-glucitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose
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oxidation
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reduction
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1,5-anhydro-D-glucitol:NADP+ oxidoreductase
Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose.
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1,5-anhydro-D-fructose + NADH
1,5-anhydro-D-mannitol + NAD+
1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-glucitol + NADPH
? + NADP+
1,5-anhydro-D-mannitol + NADPH
? + NADP+
2,3-butanedione + NADPH
?
-
76.4% of the activity with 1,5-anhydro-D-fructose
-
-
?
2,3-butanedione + NADPH
hydroxybutanone + NADP+
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50% of the activity compared to the natural substrate
-
?
3-keto-1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
6-deoxy-D-glucosone + NADP+
6-deoxy-D-mannose + NADPH
9,10-phenanthrenequinone + NADPH
?
-
18% of the activity with 1,5-anhydro-D-fructose
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
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very low activity
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?
ascopyrone P + NADP+
? + NADPH
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-
-
-
?
D-allosone + NADP+
D-altrose + NADPH
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-
-
-
?
D-galactosone + NADP+
D-talose + NADPH
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-
-
-
?
D-glucosone + NADP+
D-mannose + NADPH
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-
-
-
?
D-xylosone + NADP+
D-lyxose + NADPH
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-
-
-
?
formaldehyde + NADPH
methanol + NADP+
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low activity
-
?
glucosone + NADPH
? + NADP+
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very low activity
-
?
glucuronic acid + NADPH
? + NADP+
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low activity
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?
pyridine-3-aldehyde + NADPH
pyridine-3-ol + NADP+
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good substrate
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?
additional information
?
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substrate specificities of the recombinant enzyme for carbonyl compounds, overview
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-
?
1,5-anhydro-D-fructose + NADH
1,5-anhydro-D-mannitol + NAD+
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-
-
-
?
1,5-anhydro-D-fructose + NADH
1,5-anhydro-D-mannitol + NAD+
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-
-
-
?
1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
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-
-
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r
1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
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-
-
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r
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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-
-
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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-
-
-
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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preferred substrate
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-
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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-
-
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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best substrate, only poorly active with NADH
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ir
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-mannitol + NADP+
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ir
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-mannitol + NADP+
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ir
1,5-anhydro-D-glucitol + NADPH
? + NADP+
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-
-
-
?
1,5-anhydro-D-glucitol + NADPH
? + NADP+
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-
-
-
?
1,5-anhydro-D-mannitol + NADPH
? + NADP+
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-
-
-
?
1,5-anhydro-D-mannitol + NADPH
? + NADP+
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-
-
-
?
3-keto-1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
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-
-
-
?
3-keto-1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
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-
-
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?
6-deoxy-D-glucosone + NADP+
6-deoxy-D-mannose + NADPH
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-
-
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?
6-deoxy-D-glucosone + NADP+
6-deoxy-D-mannose + NADPH
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-
-
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?
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1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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-
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?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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-
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?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
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best substrate, only poorly active with NADH
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ir
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NADPH
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NADPH
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can not replaced by NADH
NADPH
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can not replaced by NADH
NADPH
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can not replaced by NADH
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additional information
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activity of AFR was not influenced by NaCl, KCl, MgCl2, CaCl2, MnCl2, FeCl3, and ZnCl2, 1 mM each
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1,5-anhydro-D-glucitol
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2.3% inhibition at 100 mM
2-mercaptoethanol
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2.3% inhibition at 1 mM
ascorbic acid
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30% inhibition at 1 mM
Barbital
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15% inhibition at 1 mM
D-glucose
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2.6% inhibition at 100 mM
D-glucose-1-phosphate
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25.5% inhibition at 50 mM
D-Glucose-6-phosphate
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2% inhibition at 50 mM
EDTA
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59% inhibition at 10 mM
iodoacetamide
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41% inhibition at 1 mM
iodoacetic acid
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27% inhibition at 1 mM
p-chloromercuribenzoic acid
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79% inhibition at 0.1 mM, partially reversed by 0.1 mM 2-mercaptoethanol
Phenobarbital
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22% inhibition at 1 mM
additional information
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activity of AFR was not influenced by 1 mM EDTA or by any of the given metal salts NaCl, KCl, MgCl2, CaCl2, MnCl2, FeCl3, and ZnCl2, 1 mM each
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additional information
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activity of AFR is not influenced by 1 mM EDTA
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0.44 - 49
1,5-Anhydro-D-fructose
0.44
1,5-Anhydro-D-fructose
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1.02
1,5-Anhydro-D-fructose
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pH 7.0, 37°C, recombinant enzyme
3.2
1,5-Anhydro-D-fructose
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mutant A13G/S33D in the presence of NADH
3.5
1,5-Anhydro-D-fructose
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mutant S10G in the presence of NADPH
6.4
1,5-Anhydro-D-fructose
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recombinant wild type enzyme in the presence of NADPH
7.1
1,5-Anhydro-D-fructose
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mutant A13G/S10Gin the presence of NADPH
8.3
1,5-Anhydro-D-fructose
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mutant G206I in the presence of NADPH
8.3
1,5-Anhydro-D-fructose
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native wild type enzyme in the presence of NADPH
8.4
1,5-Anhydro-D-fructose
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8.5
1,5-Anhydro-D-fructose
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mutant A13G in the presence of NADPH
8.9
1,5-Anhydro-D-fructose
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mutant H108A in the presence of NADPH
11.1
1,5-Anhydro-D-fructose
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mutant A13G in the presence of NADH
20.2
1,5-Anhydro-D-fructose
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mutant A13G/S33D in the presence of NADPH
22.5
1,5-Anhydro-D-fructose
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mutant K94G in the presence of NADPH
39
1,5-Anhydro-D-fructose
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mutant A13G/S10G in the presence of NADH
49
1,5-Anhydro-D-fructose
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mutant D176A in the presence of NADPH
1.1
NADH
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mutant A13G in the presence of 1,5-anhydro-D-fructose
1.1
NADH
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mutant A13G/S33D in the presence of 1,5-anhydro-D-fructose
1.2
NADH
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mutant A13G/S10G in the presence of 1,5-anhydro-D-fructose
0.02
NADPH
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mutant A13G in the presence of 1,5-anhydro-D-fructose
0.06
NADPH
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mutant G206I in the presence of 1,5-anhydro-D-fructose
0.06
NADPH
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recombinant wild type enzyme in the presence of 1,5-anhydro-D-fructose
0.1
NADPH
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native wild type enzyme in the presence of 1,5-anhydro-D-fructose
0.2
NADPH
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mutant K94G in the presence of 1,5-anhydro-D-fructose
0.27
NADPH
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mutant S10G in the presence of 1,5-anhydro-D-fructose
0.38
NADPH
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mutant A13G/S10G in the presence of 1,5-anhydro-D-fructose
1
NADPH
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mutant A13G/S33D in the presence of 1,5-anhydro-D-fructose
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1.3 - 1300
1,5-Anhydro-D-fructose
1.3
1,5-Anhydro-D-fructose
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mutant D176A in the presence of NADPH
3.7
1,5-Anhydro-D-fructose
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mutant H108A in the presence of NADPH
4.2
1,5-Anhydro-D-fructose
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mutant K94G in the presence of NADPH
5.5
1,5-Anhydro-D-fructose
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mutant A13G/S10G in the presence of NADH
6.3
1,5-Anhydro-D-fructose
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mutant A13G/S33D in the presence of NADPH
8.7
1,5-Anhydro-D-fructose
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-
12.4
1,5-Anhydro-D-fructose
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mutant A13G in the presence of NADH
13.5
1,5-Anhydro-D-fructose
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mutant S33D in the presence of NADH
119
1,5-Anhydro-D-fructose
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mutant S10G in the presence of NADPH
145
1,5-Anhydro-D-fructose
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recombinant wild type enzyme in the presence of NADPH
156
1,5-Anhydro-D-fructose
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mutant G206I in the presence of NADPH
216
1,5-Anhydro-D-fructose
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native wild type enzyme in the presence of NADPH
286.7
1,5-Anhydro-D-fructose
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-
369
1,5-Anhydro-D-fructose
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mutant A13G/S10Gin the presence of NADPH
405
1,5-Anhydro-D-fructose
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mutant A13G in the presence of NADPH
1300
1,5-Anhydro-D-fructose
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-
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0.01
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1,5-anhydro-D-glucitol as substrate
0.06
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1,5-anhydro-D-mannitol as substrate
191
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3-keto-1,5-anhydro-D-fructose as substrate
3.01
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purified recombinant enzyme
488.9
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after 75 fold purification
53
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D-allosone as substrate
530
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1,5-anhydro-D-fructose as substrate
6.5
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in crude cell extract
88
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D-xylosone as substrate
additional information
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AFR of S. morelense S-30.7.5 was inactive toward pyridine-3-aldehyde, 2,3-butanedione, glucuronic acid, acetaldehyde, and formaldehyde
118
-
6-deoxy-D-glucosone as substrate
118
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D-glucosone as substrate
21
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ascopyrone as substrate
21
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D-galactosone as substrate
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7
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37
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assay at
50
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amaranth
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brenda
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-
brenda
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-
brenda
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-
brenda
banana
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-
brenda
-
-
-
brenda
-
UniProt
brenda
porcine
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-
brenda
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-
-
brenda
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brenda
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higher activity compared to the porcine liver enzyme
brenda
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-
brenda
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AKCL2_HUMAN
320
0
36589
Swiss-Prot
other Location (Reliability: 2 )
AKCL2_MACFA
320
0
36418
Swiss-Prot
other Location (Reliability: 2 )
AKCL2_MOUSE
301
0
34461
Swiss-Prot
other Location (Reliability: 2 )
AKCL2_PIG
301
0
34107
Swiss-Prot
other Location (Reliability: 3 )
AKCL2_RAT
301
0
34500
Swiss-Prot
other Location (Reliability: 2 )
A0A084GGE5_PSEDA
329
0
37042
TrEMBL
other Location (Reliability: 2 )
A0A061I7A5_CRIGR
236
0
26907
TrEMBL
other Location (Reliability: 2 )
A0A1W2TBT8_ROSNE
323
0
36260
TrEMBL
other Location (Reliability: 2 )
A0A061IAU3_CRIGR
262
0
29721
TrEMBL
other Location (Reliability: 3 )
A0A084G895_PSEDA
318
0
35111
TrEMBL
Mitochondrion (Reliability: 3 )
G3GR83_CRIGR
301
0
34375
TrEMBL
other Location (Reliability: 3 )
A0A084G2F0_PSEDA
324
0
36176
TrEMBL
other Location (Reliability: 1 )
AFR_RHIME
Rhizobium meliloti (strain 1021)
333
0
34852
Swiss-Prot
-
AFR_ENSAD
333
0
35010
Swiss-Prot
-
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34000
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x * 34000, about, SDS-PAGE
38000
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1 * 38000, SDS-PAGE
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?
-
x * 34000, about, SDS-PAGE
monomer
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1 * 35100, MALDI-TOF-MS
monomer
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1 * 35100, MALDI-TOF-MS
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monomer
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1 * 38000, SDS-PAGE
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hanging-drop vapour diffusion
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to 1.93 A resolution. The structure displays an empty substrate-binding site in an open conformation reflecting 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 seems to function as a molecular switch
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A13G
-
decreased activity
A13G/S10G
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decreased activity
A13G/S33D
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increased activity
D176A
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decreased activity
G206I
-
decreased activity
H180A
-
decreased activity
K94G
-
decreased activity
S10G
-
increased activity
S33D
-
decreased activity
A13G
-
decreased activity
-
A13G/S10G
-
decreased activity
-
A13G/S33D
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increased activity
-
D176A
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decreased activity
-
H180A
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decreased activity
-
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5.2 - 8.8
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at 30°C the highest activity of AFR is measured in 100 mM Bistris-HCl at pH 6.5, with 50% remaining activity at pH 5.2 (in citrate buffer) and pH 8.8 (in Tris-HCl buffer)
667264
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45
-
decreasing activity above
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the highest activity of AFR is measured at 30°C in 100 mM Bistris-HCl at pH 6.5, with 50% remaining activity at pH 5.2 (in citrate buffer) and pH 8.8 (in Tris-HCl buffer)
-
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-20°C, 50 days, 50% loss of activity
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0°C, 50 days, 50% loss of activity
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4°C, 20 mM sodium phosphate, pH 7.0, one month
-
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Q-Sepharose HP column chromatography, Superdex 200 HR10 30 column chromatography and Red Sepharose CL-6B chromatography
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recombinant enzyme 17.4fold from Escherichia coli strain BL21(DE3) by anion exchange and adsorption chromatography, and gel filtration
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to homogeneity, chromatography techniques
-
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DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strain BL21(DE3)
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expressed in Escherichia coli
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expression in Escherichia coli
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Sakuma, M.; Kametani, S.; Akanuma, H.
Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose
J. Biochem.
123
189-193
1998
Rattus sp., Sus scrofa
brenda
Konishi, Y.; Hashima, K.; Kishida, K.
Increases in 1,5-anhydroglucitol levels in germinating amaranth seeds and in ripening banana
Biosci. Biotechnol. Biochem.
64
2462-2465
2000
Amaranthus hypochondriacus, Musa acuminata
brenda
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, Ensifer adhaerens S-30.7.5
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, Ensifer adhaerens S-30.7.5
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
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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