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

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)
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].
CAS REGISTRY NUMBER
COMMENTARY hide
206138-19-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain S-30.7.5, 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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.02 - 49
1,5-Anhydro-D-fructose
11
D-glucosone
pH 6.5, 30C
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
Q2I8V6
pH 6.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
288.9
native enzyme
484
recombinant enzyme expressed in Escherichia coli
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
assay at, reverse reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8.8
about 50% of maximal activity at pH 5.5 and at pH 8.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
isoelectric focusing
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhizobium meliloti (strain 1021)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35100
1 * 35100, MALDI-TOF-MS
38200
gel filtration
40000
1 * 40000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or 0C, 50 days, 50% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and recombinant enzyme
recombinant enzyme 17.6fold from Escherichia coli strain BL21 (DE3) by anion exchange and adsorption chromatography
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
overexpression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
no activity
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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