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Information on EC 1.1.1.263 - 1,5-anhydro-D-fructose reductase
for references in articles please use BRENDA:EC1.1.1.263
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.263 1,5-anhydro-D-fructose reductase
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
top
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-AF-reductase
AF reductase
-
-
-
-
AFR
NADP(H)-dependent 1,5-anhydro-D-fructose reductase
NADP-1,5-anhydro-D-fructose reductase
-
-
-
-
NADPH-dependent anhydrofructose reductase
NADPH-dependent monomeric reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
206138-19-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-butanedione + NADPH
?
-
Substrates: 76.4% of the activity with 1,5-anhydro-D-fructose
Products: -
Products: -
?
2,3-butanedione + NADPH
hydroxybutanone + NADP+
-
Substrates: 50% of the activity compared to the natural substrate
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH
?
-
Substrates: 18% of the activity with 1,5-anhydro-D-fructose
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
Substrates: very low activity
Products: -
Products: -
?
pyridine-3-aldehyde + NADPH
pyridine-3-ol + NADP+
-
Substrates: good substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificities of the recombinant enzyme for carbonyl compounds, overview
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADH
1,5-anhydro-D-mannitol + NAD+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADH
1,5-anhydro-D-mannitol + NAD+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
-
Substrates: -
Products: -
Products: -
r
1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
-
Substrates: -
Products: -
Products: -
r
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: preferred substrate
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: best substrate, only poorly active with NADH
Products: -
Products: -
ir
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-mannitol + NADP+
-
Substrates: -
Products: -
Products: -
ir
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-mannitol + NADP+
-
Substrates: -
Products: -
Products: -
ir
1,5-anhydro-D-glucitol + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-mannitol + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
?
3-keto-1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
-
Substrates: -
Products: -
Products: -
?
3-keto-1,5-anhydro-D-fructose + NADP+
1,5-anhydro-D-mannitol + NADPH
-
Substrates: -
Products: -
Products: -
?
6-deoxy-D-glucosone + NADP+
6-deoxy-D-mannose + NADPH
-
Substrates: -
Products: -
Products: -
?
6-deoxy-D-glucosone + NADP+
6-deoxy-D-mannose + NADPH
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: -
Products: -
Products: -
?
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-glucitol + NADP+
-
Substrates: best substrate, only poorly active with NADH
Products: -
Products: -
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity of AFR was not influenced by NaCl, KCl, MgCl2, CaCl2, MnCl2, FeCl3, and ZnCl2, 1 mM each
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoic acid
-
79% inhibition at 0.1 mM, partially reversed by 0.1 mM 2-mercaptoethanol
additional information
-
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
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.4
1,5-Anhydro-D-fructose
-
recombinant wild type enzyme in the presence of NADPH
8.3
1,5-Anhydro-D-fructose
-
native wild type enzyme in the presence of NADPH
0.06
NADPH
-
recombinant wild type enzyme in the presence of 1,5-anhydro-D-fructose
0.1
NADPH
-
native wild type enzyme in the presence of 1,5-anhydro-D-fructose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
145
1,5-Anhydro-D-fructose
-
recombinant wild type enzyme in the presence of NADPH
216
1,5-Anhydro-D-fructose
-
native wild type enzyme in the presence of NADPH
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
118
21
additional information
-
AFR of S. morelense S-30.7.5 was inactive toward pyridine-3-aldehyde, 2,3-butanedione, glucuronic acid, acetaldehyde, and formaldehyde
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 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)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 8.8
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose HP column chromatography, Superdex 200 HR10 30 column chromatography and Red Sepharose CL-6B chromatography
-
recombinant enzyme 17.4fold from Escherichia coli strain BL21(DE3) by anion exchange and adsorption chromatography, and gel filtration
-
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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