1.1.5.9: glucose 1-dehydrogenase (FAD, quinone)
This is an abbreviated version!
For detailed information about glucose 1-dehydrogenase (FAD, quinone), go to the full flat file.
Word Map on EC 1.1.5.9
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1.1.5.9
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electrode
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bioanode
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transfer-type
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bioelectrocatalytic
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glomerella
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fungi-derived
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analysis
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cingulata
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biofuel production
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diagnostics
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medicine
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biotechnology
- 1.1.5.9
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electrode
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bioanode
-
transfer-type
-
bioelectrocatalytic
- glomerella
-
fungi-derived
- analysis
- cingulata
- biofuel production
- diagnostics
- medicine
- biotechnology
Reaction
Synonyms
D-glucose:acceptor 1-oxidoreductase, dehydrogenase, glucose (acceptor), dehydrogenase, glucose (Aspergillus), EC 1.1.99.10, FAD dependent glucose dehydrogenase, FAD glucose dehydrogenase, FAD-dependent GDH, FAD-dependent glucose dehydrogenase, FAD-GDH, FAD-glucose dehydrogenase, FAD-glucose dehydrogenases, FADGDH, FADGH, flavin adenine dinucleotide dependent glucose dehydrogenase, flavin adenine dinucleotide-dependent glucose dehydrogenase, GDH, GDH-FAD, GLD, glucose dehydrogenase, glucose dehydrogenase (Aspergillus), glucose dehydrogenase (decarboxylating), thermostable GDH, thermostable glucose dehydrogenase
ECTree
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Engineering
Engineering on EC 1.1.5.9 - glucose 1-dehydrogenase (FAD, quinone)
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H505A
the mutant enzyme shows drastic decrease in the enzymatic activity
H548A
the mutant enzyme shows drastic decrease in the enzymatic activity
V149C/G190C
the mutant shows a 110 min half-life of thermal inactivation at 45°C, which is 13fold greater than that of the wild type enzyme
H505A
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the mutant enzyme shows drastic decrease in the enzymatic activity
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H548A
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the mutant enzyme shows drastic decrease in the enzymatic activity
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A472F
N475D
S326C
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326E
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326G
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326H
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S326K
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the mutant shows increased activity toward D-glucose compared to the wild type enzyme
S326Q
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S326Q/S365Y
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the mutant is virtually non-reactive to maltose while retaining high D-glucose dehydrogenase activity
S326R
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326T
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326V
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S326Y
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365A
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365C
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365D
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365E
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365F
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the mutant shows reduced activity toward D-glucose and increased activity with maltose compared to the wild type enzyme
S365G
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365H
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365I
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365K
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365L
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365M
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365N
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365P
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365Q
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365R
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365T
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365V
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365W
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the mutant shows reduced activity toward D-glucose and maltose compared to the wild type enzyme
S365Y
S365Y/S326E
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326G
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326H
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326K
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326Q
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326R
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326T
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the mutant shows reduced activity compared to the wild type enzyme
S365Y/S326V
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the mutant shows reduced activity compared to the wild type enzyme
additional information
A472F
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mutant with higher substrate specificity for glucose in relation to maltose, constructed by site-directed mutagenesis
N475D
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mutant with higher substrate specificity for glucose in relation to maltose, constructed by site-directed mutagenesis
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the mutant shows reduced activity compared to the wild type enzyme
S365Y
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the mutant shows strongly reduced activity toward D-glucose and maltose compared to the wild type enzyme
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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
additional information
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the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
additional information
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the purified recombinnat enzyme is used as an anode catalyst for enzyme fuel cells, method, overview. The recombinant FAD-GDH is able to maintain its native glucose affinity during immobilization in the carbon nanotube and operation of enzyme fuel cells. Heterogeneous electron transfer coefficient of FAD-GDHmenadione on a glassy carbon electrode was 10.73/s
additional information
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glucose-oxidizing properties of the enzyme on spectrographic graphite electrodes and as a recognition element in glucose biosensors, immobilization on spectrographic graphite electrode's surface, method, overiew. The ratio of GcGDH/Os polymer and the overall loading of the enzyme electrode significantly affect the performance of the enzyme electrode for glucose oxidation. Best suited matiral is osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+, evaluation of different Os polymers, coupled assay method with glucose oxidase, EC 1.1.3.4,overview
additional information
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the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
additional information
-
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview