Information on EC 1.1.99.11 - fructose 5-dehydrogenase

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The expected taxonomic range for this enzyme is: Gluconobacter

EC NUMBER
COMMENTARY hide
1.1.99.11
-
RECOMMENDED NAME
GeneOntology No.
fructose 5-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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SYSTEMATIC NAME
IUBMB Comments
D-fructose:acceptor 5-oxidoreductase
2,6-Dichloroindophenol can act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-85-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ASAI IFO 3267
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Manually annotated by BRENDA team
formerly Gluconobacter industrius
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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
D-fructose + 1,1'-dimethylferricenium ion
5-dehydro-D-fructose + 1,1'-dimethylferrocenium ion
show the reaction diagram
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-
-
-
?
D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinol
show the reaction diagram
D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
show the reaction diagram
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + ?
show the reaction diagram
D-fructose + 7,7,8,8-tetracyanoquinodimethane
5-dehydro-D-fructose + reduced 7,7,8,8-tetracyanoquinodimethane
show the reaction diagram
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-
-
-
?
D-fructose + acceptor
2-dehydro-D-fructose + reduced acceptor
show the reaction diagram
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direct electron-transfer bioelectrocatalytic oxidation, DET-type
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-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
show the reaction diagram
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
show the reaction diagram
D-fructose + nitro blue tetrazolium
5-dehydro-D-fructose + ?
show the reaction diagram
D-fructose + oxidized 1-methoxy-5-methylphenazinium methylsulfate
5-dehydro-D-fructose + reduced 1-methoxy-5-methylphenazinium methylsulfate
show the reaction diagram
-
-
-
-
?
D-fructose + phenazine methosulfate
5-dehydro-D-fructose + ?
show the reaction diagram
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
show the reaction diagram
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
show the reaction diagram
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in the presence of phenazine methosulfate
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-
?
D-fructose + [Fe(CN)6]3-
5-dehydro-D-fructose + [Fe(CN)6]4-
show the reaction diagram
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-
-
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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
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
show the reaction diagram
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
show the reaction diagram
additional information
?
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oxygen is completely inactive as an electron acceptor
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
heme c
pyrroloquinoline quinone
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quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Atebrine
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slight
o-phenanthroline
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slight
p-chloromercuribenzoate
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Phenylmercuric nitrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6 - 11
D-fructose
0.0011 - 0.47
ferricyanide
4.2 - 11.8
fructose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
95 - 250
D-fructose
93 - 162
ferricyanide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6.4
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pH 4.5: about 85% of maximal activity, pH 6.4: about 50% of maximal activity
4.5 - 6.5
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enzymatic activity is significantly inhibited at pH lower than 4.5 or higher than 6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
particulate fraction
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
18000
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1 * 68000 + 1 * 51000 + 1 * 18000, SDS-PAGE
19700
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1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
49000
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1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
50800
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1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
51000
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1 * 68000 + 1 * 51000 + 1 * 18000, SDS-PAGE
60000
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1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
67000
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1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
68000
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1 * 68000 + 1 * 51000 + 1 * 18000, SDS-PAGE
140000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 140000
heterotrimer
trimer
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1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 8.5
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immediately inactivated below pH 2.5 and above 8.5
348282
4.5 - 6
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stable
348283
5 - 7
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1 h, 30C, stable
348282
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25C, while the activity of the free enzyme dropps to about 20% of its initial activity during the same period of time
35
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rapid inactivation beyond
40
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10 min, no loss of activity
45
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10 min, 15% loss of activity
50
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10 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
D-fructose, 5-10%, stabilizes
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detergents stabilize
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glycerol, 5-10%, stabilizes
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sucrose, 5-10%, stabilizes
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the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25C, 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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Triton X-100 is essential for preservation of purified enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or below, activity completely preserved
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0-4C, 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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DEAE-Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Gluconobacter oxydans strain NBRC12528
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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the enzyme is a satisfactory reagent for microdetermination of D-fructose
biotechnology
industry
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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