Information on EC 1.1.1.292 - 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)

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

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EC NUMBER
COMMENTARY hide
1.1.1.292
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RECOMMENDED NAME
GeneOntology No.
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,5-anhydrofructose degradation
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY hide
206138-19-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Ensifer adhaerens
SwissProt
Manually annotated by BRENDA team
i.e. Ensifer adhaerens
SwissProt
Manually annotated by BRENDA team
C57BL/6J mice
UniProt
Manually annotated by BRENDA team
C57BL/6J mice
UniProt
Manually annotated by BRENDA team
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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 + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
show the reaction diagram
1,5-anhydro-D-glucitol + NADP+
?
show the reaction diagram
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
show the reaction diagram
6-deoxy-D-glucosone + NADPH + H+
6-deoxy-D-mannose + NADP+
show the reaction diagram
9,10-phenanthrenequinone + NADPH
? + NADP+
show the reaction diagram
butane-2,3-dione + NADPH
acetoin + NADP+
show the reaction diagram
D-allosone + NADPH + H+
D-altrose + NADP+
show the reaction diagram
D-glucosone + NADPH + H+
D-mannose + NADP+
show the reaction diagram
D-xylosone + NADPH + H+
D-lyxose + NADP+
show the reaction diagram
17% of the activity with 1,5-anhydro-D-fructose
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?
additional information
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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-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.02 - 49
1,5-Anhydro-D-fructose
11
D-glucosone
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pH 6.5, 30°C
1.1 - 1.2
NADH
0.02 - 1
NADPH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 1300
1,5-Anhydro-D-fructose
63.2
D-glucosone
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pH 6.5, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
288.9
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native enzyme
484
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recombinant enzyme expressed in Escherichia coli
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
assay at, reverse reaction
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
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isoelectric focusing
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Q92KZ3
Rhizobium meliloti (strain 1021);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35100
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1 * 35100, MALDI-TOF-MS
38200
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gel filtration
40000
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1 * 40000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 0°C, 50 days, 50% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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no activity
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.292)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)