HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.1.99.11 - fructose 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.99.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.99.11 fructose 5-dehydrogenaseIUBMB Comments
2,6-Dichloroindophenol can act as acceptor.
Specify your search results
Word Map
- 1.1.99.11
-
electrode
-
biosensors
-
amperometric
- gluconobacter
-
bioelectrode
-
biocathode
-
bioanode
-
tetrathiafulvalene
- 5-keto-d-fructose
- biotechnology
- analysis
- industry
The enzyme appears in viruses and cellular organisms
Synonyms
D-fructose dehydrogenase, dehydrogenase, fructose 5- (acceptor), FDH, FdhL, FdhS, fdhSCL, fructose 5-dehydrogenase, fructose dehydrogenase, 
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
-
-
-
-
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 + acceptor = 5-dehydro-D-fructose + reduced acceptor
-
-
-
-
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
ping-pong mechanism
-
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:acceptor 5-oxidoreductase
2,6-Dichloroindophenol can act as acceptor.
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 + 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 + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
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 + 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 + 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
-
-
?
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 + ubiquinone
5-dehydro-D-fructose + ubiquinol
-
-
-
-
?
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
heme
-
quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Show AA Sequence and Transmembrane Helices (221 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 * 60000 + 1 * 49000 + 1 * 16000, 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.
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
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
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
-
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
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.; Schäfer, 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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.99.11)
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.
Information
