Any feedback?
Information on EC 1.1.5.14 - fructose 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.5.14Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.5.14 fructose 5-dehydrogenaseIUBMB Comments
The enzyme, characterized from the bacterium Gluconobacter japonicus, is a heterotrimer composed of an FAD-containing large subunit, a small subunit, and a heme c-containing subunit, which is responsible for anchoring the complex to the cytoplasmic membrane and for transferring the electrons to ubiquinone.
Specify your search results
Word Map
- 1.1.5.14
-
electrode
-
biosensors
-
amperometric
-
gluconobacter
- 5-ketofructose
-
oxydans
-
biocathode
-
bioelectrode
-
bioanode
-
tetrathiafulvalene
- 5-keto-d-fructose
- biotechnology
- food industry
- analysis
- synthesis
- biofuel production
- industry
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
an ubiquinone
=
+
an ubiquinol
Synonyms
fructose dehydrogenase, d-fructose dehydrogenase, fdhscl, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-fructose dehydrogenase
dehydrogenase, fructose 5- (acceptor)
-
-
-
-
FDH
FdhL
FdhS
fdhSCL
fructose dehydrogenase
D-fructose dehydrogenase
-
-
-
-
D-fructose dehydrogenase
-
-
FDH
-
-
-
-
FDH
-
-
fdhSCL
-
gene name of the flavoprotein-cytochrome c complex fructose dehydrogenase
fdhSCL
-
gene name of the flavoprotein-cytochrome c complex fructose dehydrogenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-fructose + an ubiquinone = 5-dehydro-D-fructose + an ubiquinol
-
-
-
-
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
ping-pong mechanism
-
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-fructose:ubiquinone 5-oxidoreductase
The enzyme, characterized from the bacterium Gluconobacter japonicus, is a heterotrimer composed of an FAD-containing large subunit, a small subunit, and a heme c-containing subunit, which is responsible for anchoring the complex to the cytoplasmic membrane and for transferring the electrons to ubiquinone.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37250-85-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + 2,6-dichloroindophenol
5-dehydro-D-(-)-fructose + reduced 2,6-dichloroindophenol
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 + 2,5-bis[methyl(phenyl)amino]cyclohexa-2,5-diene-1,4-dione
5-dehydro-D-fructose + 2,5-bis[methyl(phenyl)amino]benzene-1,4-diol
-
-
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
D-fructose + 2-(2-fluoroanilino)cyclohexa-2,5-diene-1,4-dione
5-dehydro-D-fructose + 2-(2-fluoroanilino)benzene-1,4-diol
-
-
-
-
?
D-fructose + 2-(2-methoxyanilino)cyclohexa-2,5-diene-1,4-dione
5-dehydro-D-fructose + 2-(2-methoxyanilino)benzene-1,4-diol
-
-
-
-
?
D-fructose + 2-(3-nitroanilino)cyclohexa-2,5-diene-1,4-dione
5-dehydro-D-fructose + 2-(3-nitroanilino)benzene-1,4-diol
-
-
-
-
?
D-fructose + 2-(4-fluoroanilino)cyclohexa-2,5-diene-1,4-dione
5-dehydro-D-fructose + 2-(4-fluoroanilino)benzene-1,4-diol
-
-
-
-
?
D-fructose + 2-(4-methoxyanilino)cyclohexa-2,5-diene-1,4-dione
5-dehydro-D-fructose + 2-(4-methoxyanilino)benzene-1,4-diol
-
-
-
-
?
D-fructose + 2-[methyl(phenyl)amino]cyclohexa-2,5-diene-1,4-dione
5-dehydro-D-fructose + 2-[methyl(phenyl)amino]benzene-1,4-diol
-
-
-
-
?
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 + electron acceptor
5-dehydro-D-fructose + reduced electron acceptor
-
-
-
-
?
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
-
-
?
fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
D-(-)fructose + 2,6-dichloroindophenol
5-dehydro-D-(-)-fructose + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-(-)fructose + 2,6-dichloroindophenol
5-dehydro-D-(-)-fructose + reduced 2,6-dichloroindophenol
Gluconobacter japonicus NCBR 3260
-
-
-
-
?
D-(-)fructose + cytochrome c
5-dehydro-D-(-)-fructose + reduced cytochrome c
-
-
-
-
?
D-(-)fructose + cytochrome c
5-dehydro-D-(-)-fructose + reduced cytochrome c
Gluconobacter japonicus NCBR 3260
-
-
-
-
?
D-(-)fructose + potassium ferricyanide
5-dehydro-D-(-)-fructose + potassium ferrocyanide
-
-
-
-
?
D-(-)fructose + potassium ferricyanide
5-dehydro-D-(-)-fructose + potassium ferrocyanide
Gluconobacter japonicus NCBR 3260
-
-
-
-
?
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 + reduced 2,6-dichlorophenolindophenol
-
most effective electron acceptor
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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 + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
-
-
-
-
?
D-fructose + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
-
-
-
-
?
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 + oxidized electron acceptor
5-dehydro-D-fructose + reduced electron acceptor
-
-
-
-
?
D-fructose + oxidized electron acceptor
5-dehydro-D-fructose + reduced electron acceptor
-
-
-
-
?
D-fructose + phenazine methosulfate
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + phenazine methosulfate
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + potassium ferricyanide
5-dehydro-D-fructose + potassium ferrocyanide
-
-
-
-
?
D-fructose + potassium ferricyanide
5-dehydro-D-fructose + potassium ferrocyanide
-
-
-
-
?
D-fructose + potassium ferricyanide
5-dehydro-D-fructose + potassium ferrocyanide
-
-
-
-
?
D-fructose + potassium ferricyanide
5-dehydro-D-fructose + potassium ferrocyanide
Gluconobacter japonicus NCBR 3260
-
-
-
-
?
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
-
-
-
-
?
fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
Gluconobacter japonicus LMG 1281
-
-
-
-
?
fructose + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
-
-
-
-
?
fructose + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
Gluconobacter japonicus LMG 1281
-
-
-
-
?
fructose + phenazine methosulfate
5-dehydro-D-fructose + reduced phenazine methosulfate
-
-
-
-
?
fructose + phenazine methosulfate
5-dehydro-D-fructose + reduced phenazine methosulfate
Gluconobacter japonicus LMG 1281
-
-
-
-
?
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
?
-
-
subunit II is equivalent to the cytochrome domain and acts as electron acceptor to the catalytic subunit I of the heterotrimeric enzyme
-
-
-
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
?
-
Gluconobacter japonicus NCBR 3260
-
subunit II is equivalent to the cytochrome domain and acts as electron acceptor to the catalytic subunit I of the heterotrimeric enzyme
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
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 + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
-
-
-
-
?
D-fructose + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
-
-
-
-
?
D-fructose + oxidized electron acceptor
5-dehydro-D-fructose + reduced electron acceptor
-
-
-
-
?
D-fructose + oxidized electron acceptor
5-dehydro-D-fructose + reduced electron acceptor
-
-
-
-
?
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
-
-
-
-
?
fructose + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
-
-
-
-
?
fructose + an ubiquinone
5-dehydro-D-fructose + an ubiquinol
Gluconobacter japonicus LMG 1281
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
FAD
-
-
739769, 739849, 740362, 740364, 740369, 760332, 760337, 760656, 760973, 760974, 760975, 760976, 760977, 761572, 761604
heme
-
quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
heme c
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
-
the addition of Mg2+ has an increasing effect on the catalytic efficiency of the enzyme
Ca2+
-
the addition of Mg2+ has an increasing effect on the catalytic efficiency of the enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 4.5
4.5
7
-
two pH optima at pH 4.5 and 7.0 with cytochrome c as electron acceptor
4.5
-
two pH optima at pH 4.5 and 7.0 with cytochrome c as electron acceptor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
highest activity between pH 3.0 and 6.0 with 2,6-dichloroindophenol as electron acceptor
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
temperature optimum of enzyme immobilized on nanoporous gold electrodes
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
Show AA Sequence and Transmembrane Helices (222 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
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
heterotrimer
-
1 * 67000 + 1 * 50800 + 1 * 19700, calculated from amino acid sequence
heterotrimer
-
1 * 67000 + 1 * 51000 + 1 * 20000, calculated from amino acid sequence
heterotrimer
-
1 * 67000 + 1 * 51000 + 1 * 20000, calculated from amino acid sequence
-
heterotrimer
-
1 * 67000 + 1 * 51000 + 1 * 20000, calculated from amino acid sequence
-
heterotrimer
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
-
heterotrimer
-
1 * 67000 + 1 * 50800 + 1 * 19700, calculated from amino acid sequence
-
heterotrimer
-
1 * 67000 + 1 * 50800 + 1 * 19700, calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M450Q
-
the mutant shows a drastic decrease of the overpotential in the oxidation of D-fructose due to a negative shift in the formal potential of heme 2c as the electron-donating site of the variant
M450Q/DELTA1cFDH
M450Q
-
the mutant shows a drastic decrease of the overpotential in the oxidation of D-fructose due to a negative shift in the formal potential of heme 2c as the electron-donating site of the variant
-
additional information
M450Q/DELTA1cFDH
-
the direct electron transfer-type bioelectrocatalytic activity of the mutant is higher than that of recombinant native enzyme
M450Q/DELTA1cFDH
-
the direct electron transfer-type bioelectrocatalytic activity of the mutant is higher than that of recombinant native enzyme
-
additional information
-
an enzyme variant (DELTA1c2cFDH) which lacks 199 amino acid residues including two heme c moieties from N-terminus transports the electrons to the electrode via heme 3c at a more negative potential and at more improved kinetics than the recombinant (native) enzyme
additional information
-
in mutant M450QDELTA1cFDH, 143 amino acid residues involving heme 1c are removed and M450 as the sixth axial ligand of heme 2c is replaced with glutamine to negatively shift the formal potential of heme 2c
additional information
-
in mutant M450QDELTA1cFDH, 143 amino acid residues involving heme 1c are removed and M450 as the sixth axial ligand of heme 2c is replaced with glutamine to negatively shift the formal potential of heme 2c
-
additional information
-
an enzyme variant (DELTA1c2cFDH) which lacks 199 amino acid residues including two heme c moieties from N-terminus transports the electrons to the electrode via heme 3c at a more negative potential and at more improved kinetics than the recombinant (native) enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Toyopearl CM-650 column chromatography, and Superdex 200 gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Gluconobacter japonicus strain LMG 26773 and Gluconobacter oxydans
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is a satisfactory reagent for microdetermination of D-fructose
biofuel production
-
an enzymatic gold bioanode fabricated with fructose dehydrogenase and a polyaniline film can be used as a single-compartment fructose biofuel cell
biotechnology
food industry
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
synthesis
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
-
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
-
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
food industry
-
the enzyme can be used as biosensor to quantify D-fructose in commercial beverages and honey
food industry
-
the enzyme can be used as biosensor to quantify D-fructose in commercial beverages and honey
-
synthesis
-
Gluconobacter frateurii CHM 43 have D-mannitol dehydrogenase (quinoprotein glycerol dehydrogenase) and flavoprotein D-fructose dehydrogenase in the membranes. When the two enzymes are functional, D-mannitol is converted to 5-keto-D-fructose with 65% yield when cultivated on D-mannitol. 5-Keto-D-fructose production with almost 100% yield is realized with the resting cells
synthesis
Gluconobacter frateurii CHM 43
-
Gluconobacter frateurii CHM 43 have D-mannitol dehydrogenase (quinoprotein glycerol dehydrogenase) and flavoprotein D-fructose dehydrogenase in the membranes. When the two enzymes are functional, D-mannitol is converted to 5-keto-D-fructose with 65% yield when cultivated on D-mannitol. 5-Keto-D-fructose production with almost 100% yield is realized with the resting cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ameyama, M.; Adachi, O.
D-Fructose dehydrogenase from Gluconobacter industrius, membrane-bound
Methods Enzymol.
89
154-159
1982
Gluconobacter oxydans
-
brenda
Yamada, Y.; Aida, K.; Uemura, T.
Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase
J. Biochem.
61
636-646
1967
Gluconobacter cerinus
brenda
Ameyama, M.; Shinagawa, E.; Matsushita, K.; Adachi, O.
D-Fructose dehydrogenase of Gluconobacter industrius: purification, characterization, and application to enzymatic microdetermination of D-fructose
J. Bacteriol.
145
814-823
1981
Gluconobacter oxydans
brenda
Marcinkeviciene, J.; Johansson, G.
Kinetic studies of the active sites functioning in the quinohemoprotein fructose dehydrogenase
FEBS Lett.
318
23-26
1993
Gluconobacter sp.
brenda
Kato, K.; Walde, P.; Mitsui, H.; Higashi, N.
Enzymatic activity and stability of D-fructose dehydrogenase and sarcosine dehydrogenase immobilized onto giant vesicles
Biotechnol. Bioeng.
84
415-423
2003
Gluconobacter sp.
brenda
Kamitaka, Y.; Tsujimura, S.; Kano, K.
High current density bioelectrolysis of D-fructose at fructose dehydrogenase-adsorbed and Ketjen black-modified electrodes without a mediator
Chem. Lett.
36
218-219
2007
Gluconobacter sp.
-
brenda
Tominaga, M.; Nomura, S.; Taniguchi, I.
D-fructose detection based on the direct heterogeneous electron transfer reaction of fructose dehydrogenase adsorbed onto multi-walled carbon nanotubes synthesized on platinum electrode
Biosens. Bioelectron.
24
1184-1188
2009
Gluconobacter sp.
brenda
Kimata, S.; Mizuguchi, K.; Hattori, S.; Teshima, S.; Orita, Y.
Evaluation of a new automated, enzymatic inulin assay using D-fructose dehydrogenase
Clin. Exp. Nephrol.
13
341-349
2009
Gluconobacter oxydans
brenda
Hui, H.; Huang, D.; McArthur, D.; Nissen, N.; Boros, L.G.; Heaney, A.P.
Direct spectrophotometric determination of serum fructose in pancreatic cancer patients
Pancreas
38
706-712
2009
Gluconobacter sp.
brenda
Tsujimura, S.; Nishina, A.; Kamitaka, Y.; Kano, K.
Coulometric D-fructose biosensor based on direct electron transfer using D-fructose dehydrogenase
Anal. Chem.
81
9383-9387
2009
Gluconobacter frateurii
brenda
Sasaki, Y.; Sugihara, T.; Osakai, T.
Electron transfer mediated by membrane-bound D-fructose dehydrogenase adsorbed at an oil/water interface
Anal. Biochem.
417
129-135
2011
Gluconobacter sp.
brenda
Kawai, S.; Goda-Tsutsumi, M.; Yakushi, T.; Kano, K.; Matsushita, K.
Heterologous overexpression and characterization of a flavoprotein-cytochrome c complex fructose dehydrogenase of Gluconobacter japonicus NBRC3260
Appl. Environ. Microbiol.
79
1654-1660
2013
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
brenda
Sasakura, K.; Shirai, O.; Hichiri, K.; Goda-Tsutsumi, M.; Tsujimura, S.; Kano, K.
Ion transport across planar bilayer lipid membrane driven by D-fructose dehydrogenase-catalyzed electron transport
Chem. Lett.
40
486-488
2011
Gluconobacter sp.
-
brenda
Hickey, D.; Giroud, F.; Schmidtke, D.; Glatzhofer, D.; Minteer, S.
Enzyme cascade for catalyzing sucrose oxidation in a biofuel cell
ACS Catal.
3
2729-2737
2013
Gluconobacter sp.
-
brenda
Sarauli, D.; Wettstein, C.; Peters, K.; Schulz, B.; Fattakhova-Rohlfing, D.; Lisdat, F.
Interaction of fructose dehydrogenase with a sulfonated polyaniline: application for enhanced bioelectrocatalysis
ACS Catal.
5
2081-2087
2015
Gluconobacter japonicus
-
brenda
Wettstein, C.; Kano, K.; Schfer, D.; Wollenberger, U.; Lisdat, F.
Interaction of flavin-dependent fructose dehydrogenase with cytochrome c as basis for the construction of biomacromolecular architectures on electrodes
Anal. Chem.
88
6382-6389
2016
Gluconobacter japonicus, Gluconobacter japonicus NBRCA3260
brenda
Kawai, S.; Yakushi, T.; Matsushita, K.; Kitazumi, Y.; Shirai, O.; Kano, K.
The electron transfer pathway in direct electrochemical communication of fructose dehydrogenase with electrodes
Electrochem. Commun.
38
28-31
2014
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
Funabashi, H.; Murata, K.; Tsujimura, S.
Effect of pore size of MgO-templated carbon on the direct electrochemistry of D-fructose dehydrogenase
Electrochemistry
83
372-375
2015
Gluconobacter japonicus
-
brenda
Hichiri, K.; Shirai, O.; Kitazumi, Y.; Kano, K.
Coupling of proton transport across planar lipid bilayer and electron transport catalyzed by membrane-bound enzyme D-fructose dehydrogenase
Electrochemistry
84
328-333
2016
Gluconobacter japonicus
-
brenda
Kawai, S.; Yakushi, T.; Matsushita, K.; Kitazumi, Y.; Shirai, O.; Kano, K.
Role of a non-ionic surfactant in direct electron transfer-type bioelectrocatalysis by fructose dehydrogenase
Electrochim. Acta
152
19-24
2015
Gluconobacter japonicus
-
brenda
Sugimoto, Y.; Kitazumi, Y.; Shirai, O.; Yamamoto, M.; Kano, K.
Role of 2-mercaptoethanol in direct electron transfer-type bioelectrocatalysis of fructose dehydrogenase at Au electrodes
Electrochim. Acta
170
242-247
2015
Gluconobacter sp.
-
brenda
Sugimoto, Y.; Kawai, S.; Kitazumi, Y.; Shirai, O.; Kano, K.
Function of C-terminal hydrophobic region in fructose dehydrogenase
Electrochim. Acta
176
976-981
2015
Gluconobacter oxydans, Gluconobacter oxydans 621H
-
brenda
Kawai, S.; Kitazumi, Y.; Shirai, O.; Kano, K.
Bioelectrochemical characterization of the reconstruction of heterotrimeric fructose dehydrogenase from its subunits
Electrochim. Acta
210
689-694
2016
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
Xia, H.; Hibino, Y.; Kitazumi, Y.; Shirai, O.; Kano, K.
Interaction between D-fructose dehydrogenase and methoxy-substituent-functionalized carbon surface to increase productive orientations
Electrochim. Acta
218
41-46
2016
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
Bollella, P.; Hibino, Y.; Kano, K.; Gorton, L.; Antiochia, R.
The influence of pH and divalent/monovalent cations on the internal electron transfer (IET), enzymatic activity, and structure of fructose dehydrogenase
Anal. Bioanal. Chem.
410
3253-3264
2018
Gluconobacter japonicus, Gluconobacter japonicus NCBR 3260
brenda
Bollella, P.; Hibino, Y.; Kano, K.; Gorton, L.; Antiochia, R.
Highly sensitive membraneless fructose biosensor based on fructose dehydrogenase immobilized onto aryl thiol modified highly porous gold electrode characterization and application in food samples
Anal. Chem.
90
12131-12136
2018
Gluconobacter japonicus, Gluconobacter japonicus NCBR 3260
brenda
Adachi, T.; Kaida, Y.; Kitazumi, Y.; Shirai, O.; Kano, K.
Bioelectrocatalytic performance of D-fructose dehydrogenase
Bioelectrochemistry
129
1-9
2019
Gluconobacter japonicus
brenda
Siepenkoetter, T.; Salaj-Kosla, U.; Magner, E.
The immobilization of fructose dehydrogenase on nanoporous gold electrodes for the detection of fructose
ChemElectroChem
4
905-912
2017
Gluconobacter sp.
-
brenda
Voitechovic, E.; Vektariene, A.; Vektaris, G.; Janciene, R.; Razumiene, J.; Gureviciene, V.
1,4-Benzoquinone derivatives for enhanced bioelectrocatalysis by fructose dehydrogenase from Gluconobacter japonicus Towards promising D-fructose biosensor development
Electroanalysis
32
1005-1016
2020
Gluconobacter japonicus
-
brenda
Hibino, Y.; Kawai, S.; Kitazumi, Y.; Shirai, O.; Kano, K.
Construction of a protein-engineered variant of D-fructose dehydrogenase for direct electron transfer-type bioelectrocatalysis
Electrochem. Commun.
77
112-115
2017
Gluconobacter japonicus, Gluconobacter japonicus NCBR 3260
-
brenda
Kaida, Y.; Hibino, Y.; Kitazumi, Y.; Shirai, O.; Kano, K.
Ultimate downsizing of D-fructose dehydrogenase for improving the performance of direct electron transfer-type bioelectrocatalysis
Electrochem. Commun.
98
101-105
2019
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
Hibino, Y.; Kawai, S.; Kitazumi, Y.; Shirai, O.; Kano, K.
Protein-engineering improvement of direct electron transfer-type bioelectrocatalytic properties of D-fructose dehydrogenase
Electrochemistry
87
47-51
2019
Gluconobacter japonicus, Gluconobacter japonicus NBRC 3260
-
brenda
Kaida, Y.; Hibino, Y.; Kitazumi, Y.; Shirai, O.; Kano, K.
Discussion on direct electron transfer-type bioelectrocatalysis of downsized and axial-ligand exchanged variants of D-fructose dehydrogenase
Electrochemistry
88
195-199
2020
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
Hoffmann, J.; Hoevels, M.; Kosciow, K.; Deppenmeier, U.
Synthesis of the alternative sweetener 5-ketofructose from sucrose by fructose dehydrogenase and invertase producing Gluconobacter strains
J. Biotechnol.
307
164-174
2020
Gluconobacter japonicus, Gluconobacter japonicus LMG 1281
brenda
Suzuki, Y.; Kano, K.; Shirai, O.; Kitazumi, Y.
Diffusion-limited electrochemical D-fructose sensor based on direct electron transfer-type bioelectrocatalysis by a variant of D-fructose dehydrogenase at a porous gold microelectrode
J. Electroanal. Chem.
877
114651
2020
Gluconobacter japonicus, Gluconobacter japonicus NBRC 3260
-
brenda
Kuwahara, T.; Kameda, M.; Isozaki, K.; Toriyama, K.; Kondo, M.; Shimomura, M.
Bioelectrocatalytic fructose oxidation with fructose dehydrogenase-bearing conducting polymer films for biofuel cell application
React. Funct. Polym.
116
87-91
2017
Gluconobacter sp.
-
brenda
Adachi, O.; Nguyen, T.M.; Hours, R.A.; Kataoka, N.; Matsushita, K.; Akakabe, Y.; Yakushi, T.
5-Keto-D-fructose production from sugar alcohol by isolated wild strain Gluconobacter frateurii CHM 43
Biosci. Biotechnol. Biochem.
84
1745-1747
2020
Gluconobacter frateurii, Gluconobacter frateurii CHM 43
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.5.14)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
