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Enzyme Nomenclature
Information on EC 1.1.99.11 - fructose 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.99.11
Word Map on EC 1.1.99.11
- 1.1.99.11
-
electrode
-
biosensors
-
amperometric
- gluconobacter
-
screen-printed
-
tetrathiafulvalene
- ferrocene
-
bioanode
-
biocathode
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bioelectrode
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one-compartment
- biotechnology
- 5-keto-d-fructose
-
transfer-type
-
alkanethiolate
-
open-circuit
-
bioelectrocatalysts
- analysis
- industry
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The expected taxonomic range for this enzyme is: Gluconobacter
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EC NUMBER 
COMMENTARY 
1.1.99.11
-
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RECOMMENDED NAME
GeneOntology No.
fructose 5-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
-
-
-
-
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
ping-pong mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-fructose:acceptor 5-oxidoreductase
2,6-Dichloroindophenol can act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
37250-85-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose + 1,1'-dimethylferricenium ion
5-dehydro-D-fructose + 1,1'-dimethylferrocenium ion
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinol
D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
D-fructose + 7,7,8,8-tetracyanoquinodimethane
5-dehydro-D-fructose + reduced 7,7,8,8-tetracyanoquinodimethane
-
-
-
-
?
D-fructose + acceptor
2-dehydro-D-fructose + reduced acceptor
-
direct electron-transfer bioelectrocatalytic oxidation, DET-type
-
-
?
D-fructose + oxidized 1-methoxy-5-methylphenazinium methylsulfate
5-dehydro-D-fructose + reduced 1-methoxy-5-methylphenazinium methylsulfate
-
-
-
-
?
D-fructose + [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide]
5-dehydro-D-fructose + [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] formazan
-
in the presence of phenazine methosulfate
-
-
?
D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + ?
-
most effective electron acceptor
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
involved in utilization of D-fructose by acetic acid bacteria
-
-
-
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + nitro blue tetrazolium
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + nitro blue tetrazolium
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + phenazine methosulfate
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + phenazine methosulfate
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
-
-
-
-
?
additional information
?
-
-
oxygen is completely inactive as an electron acceptor
-
-
-
additional information
?
-
-
when FDH is adsorbed onto a porous carbon electrode surface, it can transfer electrons from D-fructose to the electrode directly without a mediator
-
-
-
additional information
?
-
-
cells producing only subunits FdhS and FdhL have no fructose-oxidizing activity, but show significantly high D-fructose:ferricyanide oxidoreductase activity in the soluble fraction of cell extracts, whereas the cells producing the FDH complex show activity in the membrane fraction
-
-
-
additional information
?
-
-
cells producing only subunits FdhS and FdhL have no fructose-oxidizing activity, but show significantly high D-fructose:ferricyanide oxidoreductase activity in the soluble fraction of cell extracts, whereas the cells producing the FDH complex show activity in the membrane fraction
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
oxygen is completely inactive as an electron acceptor
-
-
-
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
involved in utilization of D-fructose by acetic acid bacteria
-
-
-
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
cytochrome c
-
contains a cytochrome c like electron carrier, tightly bound
cytochrome c
-
the cytochrome c subunit is responsible not only for membrane anchoring but also for ubiquinone reduction
heme
-
quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
D-fructose
-
in presence of 2,6-dichlorophenolindophenol, 67 mM, pH 5.5, 15°C
10
D-fructose
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irreversibly adsorbed on Ketjen black - modified glassy carbon electrodes
11
D-fructose
-
Km is determined using FDH adsorbed onto multi-walled carbon nanotubes synthesized on platinum electrode
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6.4
-
pH 4.5: about 85% of maximal activity, pH 6.4: about 50% of maximal activity
4.5 - 6.5
-
enzymatic activity is significantly inhibited at pH lower than 4.5 or higher than 6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
19700
49000
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
50800
51000
60000
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
67000
140000
19700
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
50800
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
67000
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
trimer
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
heterotrimer
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence; 1 * 68000 + 1 * 51000 + 1 * 18000, SDS-PAGE
heterotrimer
-
1 * 67000 + 1 * 50800 + 1 * 19700, calculated from amino acid sequence
heterotrimer
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence; 1 * 67000 + 1 * 51000 + 1 * 20000, SDS-PAGE; 1 * 68000 + 1 * 51000 + 1 * 18000, SDS-PAGE
-
heterotrimer
-
1 * 67000 + 1 * 50800 + 1 * 19700, calculated from amino acid sequence
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25°C, while the activity of the free enzyme dropps to about 20% of its initial activity during the same period of time
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25°C, while the activity of the free enzyme dropps to about 20% of its initial activity during the same period of time
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, pH 4.0-5.0, 0.1% Triton X-100, 1 mM 2-mercaptoethanol, for at least 2 weeks
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Toyopearl CM-650 column chromatography, and Superdex 200 gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is a satisfactory reagent for microdetermination of D-fructose
biotechnology
industry
-
direct electron-transfer bioelectrocatalysis can be used in biosensors, biofuel cells and bioreactors, FDH immobilised on Ketjen black electroconductive material produces a catalytic oxidation wave of D-fructose without a mediator, the electron in FDH seems to be directly transferred to the electrode via the heme c site
biotechnology
-
multi-walled carbon nanotubes synthesized on platinum plate (MWCNTs/Pt) electrode are immediately immersed into solutions of FDH to immobilize the enzyme onto electrode surfaces. Thereafter, a well-defined catalytic oxidation current based on FDH is observed from ca. -0.15V, which is close to the redox potential of heme c as a prosthetic group of FDH. From an analysis of a plot of the catalytic current versus substrate, the calibration range for the fructose concentration is up to ca. 40 mmol/dm3, and the apparent Michaelis-Menten constant is evaluated to be 11 mmol/l. The obtained results are useful in applications to prepare the third-generation biosensors and other future bioelectrochemical devices
biotechnology
-
an automated, enzymatic insulin assay is developed. Principle: Fructose is produced by the action of inulinase on inulin present in the sample. The resulting fructose reacts with D-fructose dehydrogenase in the presence of the oxidized form of 1-methoxy-5-methylphenazinium methylsulfate (1-m-PMS) to produce the reduced form of 1-m-PMS. Reduced 1-m-PMS acts on dissolved oxygen to produce hydrogen peroxide, which, through the action of peroxidase, oxidatively condenses N-ethyl-N-(2-hydroxy-3-sulfopropyl)-m-toluidine and 4-aminoantipyrine to transform them into quinoneimine dye. The absorbance of the quinoneimine dye is measured spectrophotometrically to determine the concentration of inulin in the sample. The new enzymatic assay offers a more convenient and more accurate measurement of inulin and may be suitable for routine procedures by automated analyzers in clinical laboratories
biotechnology
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using fructose dehydrogenase-catalyzed conversion of d-fructose to 5-ketofructose, followed by quantitation of MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] formazan production by direct spectrophotometry, an assay to measure serum fructose concentration is developed. The fructose dehydrogenase-based enzymatic assay correlates highly with gas chromatography-mass spectroscopic analysis of serum fructose. The assay is highly specific, exhibits no cross-reactivity with other sugars and is easy to perform
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