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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redox reaction
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-
-
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reduction
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-
-
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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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ASAI IFO 3267
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-
Manually annotated by BRENDA team
formerly Gluconobacter industrius strain IFO3260
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-
Manually annotated by BRENDA team
formerly Gluconobacter industrius strain IFO3260
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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
-
-
-
-
?
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
-
-
-
-
?
D-fructose + acceptor
2-dehydro-D-fructose + reduced acceptor
show the reaction diagram
-
direct electron-transfer bioelectrocatalytic oxidation, DET-type
-
-
?
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 + [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
-
in the presence of phenazine methosulfate
-
-
?
D-fructose + [Fe(CN)6]3-
5-dehydro-D-fructose + [Fe(CN)6]4-
show the reaction diagram
-
-
-
-
?
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
additional information
?
-
-
oxygen is completely inactive as an electron acceptor
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-
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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
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
10 - 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
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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
140000
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gel filtration
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
-
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
DEAE-Sepharose column chromatography
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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