Information on EC 1.1.1.263 - 1,5-anhydro-D-fructose reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.263
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RECOMMENDED NAME
GeneOntology No.
1,5-anhydro-D-fructose reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1,5-anhydro-D-glucitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
show the reaction diagram
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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reduction
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
206138-19-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
amaranth
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Manually annotated by BRENDA team
strain S-30.7.5
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Manually annotated by BRENDA team
strain S-30.7.5
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
banana
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
porcine
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-fructose + NADH
1,5-anhydro-D-mannitol + NAD+
show the reaction diagram
1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
show the reaction diagram
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
show the reaction diagram
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-mannitol + NADP+
show the reaction diagram
1,5-anhydro-D-glucitol + NADPH
? + NADP+
show the reaction diagram
1,5-anhydro-D-mannitol + NADPH
? + NADP+
show the reaction diagram
2,3-butanedione + NADPH
?
show the reaction diagram
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76.4% of the activity with 1,5-anhydro-D-fructose
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-
?
2,3-butanedione + NADPH
hydroxybutanone + NADP+
show the reaction diagram
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50% of the activity compared to the natural substrate
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?
3-keto-1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
show the reaction diagram
6-deoxy-D-glucosone + NADP+
6-deoxy-D-mannose + NADPH
show the reaction diagram
9,10-phenanthrenequinone + NADPH
?
show the reaction diagram
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18% of the activity with 1,5-anhydro-D-fructose
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-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
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very low activity
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?
ascopyrone P + NADP+
? + NADPH
show the reaction diagram
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-
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?
D-allosone + NADP+
D-altrose + NADPH
show the reaction diagram
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-
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?
D-galactosone + NADP+
D-talose + NADPH
show the reaction diagram
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-
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?
D-glucosone + NADP+
D-mannose + NADPH
show the reaction diagram
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-
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?
D-xylosone + NADP+
D-lyxose + NADPH
show the reaction diagram
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-
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?
formaldehyde + NADPH
methanol + NADP+
show the reaction diagram
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low activity
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?
glucosone + NADPH
? + NADP+
show the reaction diagram
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very low activity
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?
glucuronic acid + NADPH
? + NADP+
show the reaction diagram
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low activity
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?
pyridine-3-aldehyde + NADPH
pyridine-3-ol + NADP+
show the reaction diagram
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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dependent on
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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activity of AFR was not influenced by NaCl, KCl, MgCl2, CaCl2, MnCl2, FeCl3, and ZnCl2, 1 mM each
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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activity of AFR is not influenced by 1 mM EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.44 - 49
1,5-Anhydro-D-fructose
11
D-glucosone
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1.1 - 1.2
NADH
0.02 - 1
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 1300
1,5-Anhydro-D-fructose
63.2
D-glucosone
Ensifer adhaerens
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
1.16
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3.01
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purified recombinant enzyme
6.5
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in crude cell extract
21
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ascopyrone as substrate; D-galactosone as substrate
53
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D-allosone as substrate
88
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D-xylosone as substrate
118
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6-deoxy-D-glucosone as substrate; D-glucosone as substrate
191
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3-keto-1,5-anhydro-D-fructose as substrate
488.9
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after 75 fold purification
530
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1,5-anhydro-D-fructose 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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x * 34000, about, SDS-PAGE
35000
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gel filtration
35100
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MALDI-TOF-MS
38000
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1 * 38000, SDS-PAGE
38200
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gel filtration
40000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 34000, about, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8.8
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at 30C 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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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decreasing activity above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the highest activity of AFR is measured at 30C 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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 days, 50% loss of activity
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0C, 50 days, 50% loss of activity
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4C, 20 mM sodium phosphate, pH 7.0, one month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A13G
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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
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decreased activity
H180A
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decreased activity
K94G
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decreased activity
S10G
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increased activity
S33D
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decreased activity
A13G
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decreased activity
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A13G/S10G
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decreased activity
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A13G/S33D
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increased activity
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D176A
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decreased activity
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H180A
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decreased activity
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