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show all sequences of 1.1.1.118

Increased activity of glucose dehydrogenase co-immobilized with a redox mediator in a bioreactor with electrochemical NAD+ regeneration

Manjon, A.; Obon, J.M.; Casanova, P.; Fernandez, V.M.; Ilborra1, J.L.; Biotechnol. Lett. 24, 1227-1232 (2002)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
biotechnology
immobilization of GDH1 on the surface of a graphite felt electrode, construction and optimization of an electrochemical bioreactor, co-immobilization of 3,4-dihydroxybenzaldehyde as mediator allows the system to operate at 0.2 V and increases both the activity (2.4-times) and the stability of the immobilized enzyme by 2.2-times, the immobilized enzyme is termed IMGDH1
Komagataeibacter xylinus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + NAD+
Komagataeibacter xylinus
-
D-glucono-1,5-lactone + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Komagataeibacter xylinus
-
i.e. Acetobacter xylinum
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NAD+
-
668049
Komagataeibacter xylinus
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Komagataeibacter xylinus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Komagataeibacter xylinus
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Komagataeibacter xylinus
Application (protein specific)
Application
Commentary
Organism
biotechnology
immobilization of GDH1 on the surface of a graphite felt electrode, construction and optimization of an electrochemical bioreactor, co-immobilization of 3,4-dihydroxybenzaldehyde as mediator allows the system to operate at 0.2 V and increases both the activity (2.4-times) and the stability of the immobilized enzyme by 2.2-times, the immobilized enzyme is termed IMGDH1
Komagataeibacter xylinus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Komagataeibacter xylinus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + NAD+
Komagataeibacter xylinus
-
D-glucono-1,5-lactone + NADH + H+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NAD+
-
668049
Komagataeibacter xylinus
D-glucono-1,5-lactone + NADH + H+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Komagataeibacter xylinus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Komagataeibacter xylinus
Other publictions for EC 1.1.1.118
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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2008
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4
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2
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-
Increased activity of glucose ...
Komagataeibacter xylinus
Biotechnol. Lett.
24
1227-1232
2002
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1
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1
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1
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1
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1
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87
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639110
Giardina
Glucose dehydrogenase from the ...
Sulfolobus solfataricus, Sulfolobus solfataricus MT-4
Biochem. J.
239
517-522
1986
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8
7
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4
3
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6
20
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1
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2
3
25
2
1
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1
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1
2
1
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2
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2
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2
8
1
7
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4
3
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6
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1
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2
3
25
2
1
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1
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1
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285777
Kobayashi
-
Identification and growth char ...
Corynebacterium sp., Corynebacterium sp. No. 93-1
Agric. Biol. Chem.
44
41-47
1980
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2
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1
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1
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1
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1
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285778
Anderson
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Pseudomonas sp., Pseudomonas sp. MSU-1
Methods Enzymol.
41
147-150
1975
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3
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8
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1
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1
1
16
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2
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1
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1
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1
16
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2
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285776
Hu
The regulation of some sugar d ...
Pseudomonas sp.
Biochim. Biophys. Acta
93
237-245
1964
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