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Information on EC 1.1.1.292 - 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) and Organism(s) Ensifer adhaerens and UniProt Accession Q2I8V6

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IUBMB Comments
This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family . 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 . 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 .
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Ensifer adhaerens
UNIPROT: Q2I8V6
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The taxonomic range for the selected organisms is: Ensifer adhaerens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
1,5-anhydro-D-fructose reductase, 1,5-anhydro-D-fructose reductase (ambiguous), AF reductase, AFR, AKR1E1, More, NADPH dependent 1,5-anhydro-D-fructose reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,5-anhydro-D-fructose reductase
-
1,5-anhydro-D-fructose reductase (ambiguous)
-
PATHWAY SOURCE
PATHWAYS
-
-
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
-
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 + H+
1,5-anhydro-D-mannitol + NAD+
show the reaction diagram
-
-
-
r
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
23% of the activity with 1,5-anhydro-D-mannitol
-
-
?
6-deoxy-D-glucosone + NADPH + H+
6-deoxy-D-mannose + NADP+
show the reaction diagram
22% of the activity with 1,5-anhydro-D-fructose
-
-
?
D-allosone + NADPH + H+
D-altrose + NADP+
show the reaction diagram
10% of the activity with 1,5-anhydro-D-fructose
-
-
?
D-glucosone + NADPH + H+
D-mannose + NADP+
show the reaction diagram
22% of the activity with 1,5-anhydro-D-fructose
-
-
?
D-xylosone + NADPH + H+
D-lyxose + NADP+
show the reaction diagram
17% of the activity with 1,5-anhydro-D-fructose
-
-
?
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
3.2 - 49
1,5-Anhydro-D-fructose
11
D-glucosone
pH 6.5, 30°C
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
pH 6.5, 30°C
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
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Ensifer adhaerens
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AFR_ENSAD
333
0
35010
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35100
1 * 35100, MALDI-TOF-MS
38200
gel filtration
40000
1 * 40000, SDS-PAGE
SUBUNIT
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
PROTEIN VARIANTS
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 0°C, 50 days, 50% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q2I8V6), Ensifer adhaerens S-30.7.5 (Q2I8V6)
Manually annotated by BRENDA team
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 (Q2I8V6)
Manually annotated by BRENDA team