BRENDA - Enzyme Database
show all sequences of 1.1.5.9

Amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode

Monosik, R.; Stredansky, M.; Luspai, K.; Magdolen, P.; Sturdik, E.; Enzyme Microb. Technol. 50, 227-232 (2012)

Data extracted from this reference:

Application
Application
Commentary
Organism
analysis
the enzyme can be used as O2-independent biosensor for glucoe detection
Aspergillus oryzae
diagnostics
the enzyme can be used as O2-independent biosensor for glucoe detection
Aspergillus oryzae
Engineering
Amino acid exchange
Commentary
Organism
additional information
amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode. Unlike the common glucose oxidase based biosensor, the presented biosensors is O2-independent, method and biosensorevlauation, overview. Polyphenols also do not interfere at used measuring conditions. Determination of D-glucose in beverages and wines using biosensors, HPLC and enzymatic-spectrophotometric assay, overview
Aspergillus oryzae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.09
-
D-glucose
pH 7.4, 37°C, enzyme immobilized on amperometric electrode
Aspergillus oryzae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + a quinone
Aspergillus oryzae
-
D-glucono-1,5-lactone + a reduced quinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus oryzae
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + a quinone
-
724876
Aspergillus oryzae
D-glucono-1,5-lactone + a reduced quinol
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Aspergillus oryzae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Aspergillus oryzae
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
7.5
-
Aspergillus oryzae
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Aspergillus oryzae
Application (protein specific)
Application
Commentary
Organism
analysis
the enzyme can be used as O2-independent biosensor for glucoe detection
Aspergillus oryzae
diagnostics
the enzyme can be used as O2-independent biosensor for glucoe detection
Aspergillus oryzae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Aspergillus oryzae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode. Unlike the common glucose oxidase based biosensor, the presented biosensors is O2-independent, method and biosensorevlauation, overview. Polyphenols also do not interfere at used measuring conditions. Determination of D-glucose in beverages and wines using biosensors, HPLC and enzymatic-spectrophotometric assay, overview
Aspergillus oryzae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.09
-
D-glucose
pH 7.4, 37°C, enzyme immobilized on amperometric electrode
Aspergillus oryzae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + a quinone
Aspergillus oryzae
-
D-glucono-1,5-lactone + a reduced quinol
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + a quinone
-
724876
Aspergillus oryzae
D-glucono-1,5-lactone + a reduced quinol
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Aspergillus oryzae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Aspergillus oryzae
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
7.5
-
Aspergillus oryzae
General Information
General Information
Commentary
Organism
additional information
amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode. Unlike the common glucose oxidase based biosensor, the presented biosensors is O2-independent, method and biosensorevlauation, overview. Polyphenols also do not interfere at used measuring conditions. Determination of D-glucose in beverages and wines using biosensors, HPLC and enzymatic-spectrophotometric assay, overview
Aspergillus oryzae
General Information (protein specific)
General Information
Commentary
Organism
additional information
amperometric glucose biosensor utilizing FAD-dependent glucose dehydrogenase immobilized on nanocomposite electrode. Unlike the common glucose oxidase based biosensor, the presented biosensors is O2-independent, method and biosensorevlauation, overview. Polyphenols also do not interfere at used measuring conditions. Determination of D-glucose in beverages and wines using biosensors, HPLC and enzymatic-spectrophotometric assay, overview
Aspergillus oryzae
Other publictions for EC 1.1.5.9
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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20
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2
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2
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741496
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741724
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2017
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2
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4
2
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10
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8
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3
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4
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740120
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740363
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Thermoascus aurantiacus, Thermoascus aurantiacus NBRC 6766, Thermoascus aurantiacus NBRC 9748
Electrochemistry
84
342-348
2016
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1
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739817
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Aspergillus terreus
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1
1
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740224
Sakai
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1
1
740778
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120
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741412
Yoshida
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Sci. Rep.
5
13498
2015
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740853
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Aspergillus terreus, Aspergillus terreus NIH2624
J. Microbiol. Biotechnol.
24
1516-1524
2014
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13
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726109
Fapyane
High performance enzyme fuel c ...
Burkholderia cepacia
Phys. Chem. Chem. Phys.
15
9508-9512
2013
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740387
Yamashita
Direct electron transfer type ...
Burkholderia cepacia
Enzyme Microb. Technol.
52
123-128
2013
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1
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38
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723928
Zafar
Characterization of different ...
Aspergillus sp., Colletotrichum gloeosporioides, Komagataella pastoris
Anal. Bioanal. Chem.
402
2069-2077
2012
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723944
Zafar
Electron-transfer studies with ...
Colletotrichum gloeosporioides
Anal. Chem.
84
334-341
2012
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724876
Monosik
Amperometric glucose biosensor ...
Aspergillus oryzae
Enzyme Microb. Technol.
50
227-232
2012
-
2
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724639
Mori
Screening of Aspergillus-deriv ...
Aspergillus oryzae, Aspergillus terreus
Biotechnol. Lett.
33
2255-2263
2011
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725879
Sygmund
Heterologous overexpression of ...
Colletotrichum gloeosporioides
Microb. Cell Fact.
10
106
2011
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1
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8
8
725906
Sygmund
Reduction of quinones and phen ...
Colletotrichum gloeosporioides, Colletotrichum gloeosporioides DSM 62728
Microbiology
157
3203-3212
2011
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1
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1
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1
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1
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2
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1
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11
1
1
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2
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1
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2
2
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685757
Yamaoka
Site directed mutagenesis stud ...
Burkholderia cepacia
Biotechnol. Lett.
30
1967-1972
2008
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1
1
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38
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4
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38
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696897
Okuda-Shimazaki
Biofuel cell system employing ...
Burkholderia cepacia, Burkholderia cepacia SM4
Biotechnol. Lett.
30
1753-1758
2008
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1
1
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